ID AXUD1_HUMAN STANDARD; PRT; 589 AA. AC Q96S65; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 03-OCT-2006, entry version 29. DE Axin-1 up-regulated gene 1 protein (TGF-beta-induced apoptosis protein DE 3) (TAIP-3) (URAX1 protein). GN Name=AXUD1; Synonyms=TAIP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=21417655; PubMed=11526492; DOI=10.1038/sj.onc.1204603; RA Ishiguro H., Tsunoda T., Tanaka T., Fujii Y., Nakamura Y., RA Furukawa Y.; RT "Identification of AXUD1, a novel human gene induced by AXIN1 and its RT reduced expression in human carcinomas of the lung, liver, colon and RT kidney."; RL Oncogene 20:5062-5066(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Akiyama N., Kondoh S.; RT "TGF-beta induced apoptosis protein 3 (TAIP-3)."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May have a tumor-suppressor function. May play a role in CC apoptosis. CC -!- SUBCELLULAR LOCATION: Nucleus (Probable). CC -!- TISSUE SPECIFICITY: Ubiquitous. Most abundantly expressed in lung, CC placenta, skeletal muscle, pancreas and leukocyte. Frequently CC down-regulated in lung, kidney, liver and colon cancers compared CC with their corresponding normal tissues. CC -!- SIMILARITY: Belongs to the AXUD1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB053121; BAB61065.1; -; mRNA. DR EMBL; AB063301; BAB79450.1; -; mRNA. DR EMBL; BC038949; AAH38949.1; -; mRNA. DR UniGene; Hs.370950; -. DR Ensembl; ENSG00000144655; Homo sapiens. DR KEGG; hsa:64651; -. DR HGNC; HGNC:14300; AXUD1. DR MIM; 606458; gene. DR ArrayExpress; Q96S65; -. DR RZPD-ProtExp; W0158; -. DR GO; GO:0006915; P:apoptosis; NAS. KW Apoptosis; Nuclear protein. FT CHAIN 1 589 Axin-1 up-regulated gene 1 protein. FT /FTId=PRO_0000114786. FT COMPBIAS 17 40 Ser-rich. FT COMPBIAS 237 275 Cys-rich. SQ SEQUENCE 589 AA; 63522 MW; B43B5DB86F96B57B CRC64; MTGLLKRKFD QLDEDNSSVS SSSSSSGCQS RSCSPSSSVS RAWDSEEEGP WDQMPLPDRD FCGPRSFTPL SILKRARRER PGRVAFDGIT VFYFPRCQGF TSVPSRGGCT LGMALRHSAC RRFSLAEFAQ EQARARHEKL RQRLKEEKLE MLQWKLSAAG VPQAEAGLPP VVDAIDDASV EEDLAVAVAG GRLEEVSFLQ PYPARRRRAL LRASGVRRID REEKRELQAL RQSREDCGCH CDRICDPETC SCSLAGIKCQ MDHTAFPCGC CREGCENPMG RVEFNQARVQ THFIHTLTRL QLEQEAESFR ELEAPAQGSP PSPGEEALVP TFPLAKPPMN NELGDNSCSS DMTDSSTASS SASGTSEAPD CPTHPGLPGP GFQPGVDDDS LARILSFSDS DFGGEEEEEE EGSVGNLDNL SCFHPADIFG TSDPGGLASW THSYSGCSFT SGILDENANL DASCFLNGGL EGSREGSLPG TSVPPSMDAG RSSSVDLSLS SCDSFELLQA LPDYSLGPHY TSQKVSDSLD NIEAPHFPLP GLSPPGDASS CFLESLMGFS EPAAEALDPF IDSQFEDTVP ASLMEPVPV // ID AXUD1_MOUSE STANDARD; PRT; 583 AA. AC P59054; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 1. DT 03-OCT-2006, entry version 34. DE Axin-1 up-regulated gene 1 protein (TGF-beta-induced apoptosis protein DE 3) (TAIP-3). GN Name=Axud1; Synonyms=Taip3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Lung; RA Akiyama N., Saitoh S., Yamada H., Kondoh S.K.; RT "TGF-beta induced apoptosis protein 3 (TAIP-3)."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N-3; TISSUE=Mammary gland, and Trophoblast; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May have a tumor-suppressor function. May play a role in CC apoptosis. CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- SIMILARITY: Belongs to the AXUD1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB091687; BAC16314.1; -; mRNA. DR EMBL; AK029893; BAC26661.1; -; mRNA. DR EMBL; BC029720; AAH29720.1; -; mRNA. DR EMBL; BC050066; AAH50066.1; -; mRNA. DR UniGene; Mm.125196; -. DR Ensembl; ENSMUSG00000032515; Mus musculus. DR KEGG; mmu:215418; -. DR MGI; MGI:2387989; Axud1. DR ArrayExpress; P59054; -. DR GO; GO:0006915; P:apoptosis; ISS. KW Apoptosis; Nuclear protein. FT CHAIN 1 583 Axin-1 up-regulated gene 1 protein. FT /FTId=PRO_0000114787. FT COMPBIAS 17 40 Ser-rich. FT COMPBIAS 237 275 Cys-rich. SQ SEQUENCE 583 AA; 62525 MW; 9061F7A80404FF27 CRC64; MTGLLKRKFD QLEEDDSSSS SSSSFSSRLS LSSFPASSAS PAWNSDEEGP GGQAPQSDQD SCGLQSFTPP SILKRAPRER PGHVAFNGIT VYYFPRCQGF TSVPSRGGCT LGMASRHSTC RLFSLAEFTQ EQVRARREKL RRRLKEEKLE MLRWKFSVAG VPESGAGVPL TADAIDDASV EEDLAVAVAN GRLEEANFLQ PHPPRQRRAL LRASGVRRID REEKRELQVL RQSREDCGCH CDGVCDPETC SCSLAGIKCQ MDHTSFPCGC CREGCENPNG RVEFNQTRVQ THFIHTLTRL QMEQGAESLG DLESPVEDTP VEQAALSPFP PSKPPVSSEL GDSSCSSDMT DSSTTLSSGS SEPPNHPAHP SLPGPSFRSG VDEDSLEQIL NFSDSDLGIE EEEEEGGGVG NLDNLSCFHL ADIFGTGDPG SLASWTHSQS GSSLASGILD ENANLDASCF LNSGLGGLRE GSLPGSSGSP EGDAVQSSSW DLSLSSCDSF ELLQALPDYS LGPHYTSRRV SGSPDSLETF HPLPSFSPPR DASTCFLESL VGLSEPVTEV LAPLLESQFE DAALAPLLEP VPV // ID FSTL1_MOUSE STANDARD; PRT; 306 AA. AC Q62356; Q99JI9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-OCT-2006, entry version 60. DE Follistatin-related protein 1 precursor (Follistatin-like 1) (TGF- DE beta-inducible protein TSC-36). GN Name=Fstl1; Synonyms=Frp, Fstl, Tsc36; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94039028; PubMed=7901004; RA Shibanuma M., Mashimo J., Mita A., Kuroki T., Nose K.; RT "Cloning from a mouse osteoblastic cell line of a set of transforming- RT growth-factor-beta 1-regulated genes, one of which seems to encode a RT follistatin-related polypeptide."; RL Eur. J. Biochem. 217:13-19(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May modulate the action of some growth factors on cell CC proliferation and differentiation. Binds heparin (By similarity). CC -!- SUBUNIT: Interacts with SCN10A. CC -!- SUBCELLULAR LOCATION: Secreted protein (Potential). CC -!- SIMILARITY: Contains 2 EF-hand domains. CC -!- SIMILARITY: Contains 1 follistatin-like domain. CC -!- SIMILARITY: Contains 1 Kazal-like domain. CC -!- SIMILARITY: Contains 1 VWFC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M91380; AAC37633.1; -; mRNA. DR EMBL; BC006185; -; NOT_ANNOTATED_CDS; mRNA. DR PIR; S38251; S38251. DR HSSP; P01001; 2BUS. DR MEROPS; I01.967; -. DR Ensembl; ENSMUSG00000022816; Mus musculus. DR KEGG; mmu:14314; -. DR MGI; MGI:102793; Fstl1. DR ArrayExpress; Q62356; -. DR InterPro; IPR011992; EF-Hand_type. DR InterPro; IPR002048; EF_hand_Ca_bd. DR InterPro; IPR003645; Fol_N. DR InterPro; IPR002350; Prot_inh_Kazal. DR InterPro; IPR011497; Prot_Inh_Kazal_2. DR InterPro; IPR009041; Prot_inh_PMP_SGC. DR InterPro; IPR001007; VWF_C. DR Pfam; PF00036; efhand; 2. DR Pfam; PF07648; Kazal_2; 1. DR SMART; SM00274; FOLN; 1. DR SMART; SM00280; KAZAL; 1. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS00282; KAZAL; FALSE_NEG. DR PROSITE; PS01208; VWFC_1; FALSE_NEG. DR PROSITE; PS50184; VWFC_2; FALSE_NEG. KW Glycoprotein; Heparin-binding; Repeat; Signal. FT SIGNAL 1 18 By similarity. FT CHAIN 19 306 Follistatin-related protein 1. FT /FTId=PRO_0000010113. FT DOMAIN 28 51 Follistatin-like. FT DOMAIN 52 96 Kazal-like. FT DOMAIN 142 176 EF-hand 1. FT DOMAIN 191 226 EF-hand 2. FT DOMAIN 231 285 VWFC. FT CARBOHYD 142 142 N-linked (GlcNAc...) (Potential). FT CARBOHYD 173 173 N-linked (GlcNAc...) (Potential). FT CARBOHYD 178 178 N-linked (GlcNAc...) (Potential). FT DISULFID 52 82 By similarity. FT DISULFID 56 75 By similarity. FT DISULFID 64 96 By similarity. FT CONFLICT 235 235 V -> D (in Ref. 2). SQ SEQUENCE 306 AA; 34538 MW; 4631070AE81E8FC4 CRC64; MWKRWLALSL VTIALVHGEE EPRSKSKICA NVFCGAGREC AVTEKGEPTC LCIEQCKPHK RPVCGSNGKT YLNHCELHRD ACLTGSKIQV DYDGHCKEKK SASPSASPVV CYQANRDELR RRLIQWLEAE IIPDGWFSKG SNYSEILDKY FKSFDNGDSH LDSSEFLKFV EQNETAINIT TYADQENNKL LRSLCVDALI ELSDENADWK LSFQEFLKCL NPSFNPPEKK CALEVETYAD GAETEVDCNR CVCSCGHWVC TAMTCDGKNQ KGVQTHTEEE KTGYVQELQK HQGTAEKTKK VNTKEI // ID GDF15_HUMAN STANDARD; PRT; 308 AA. AC Q99988; O14629; P78360; Q9NRT0; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 19-SEP-2006, entry version 54. DE Growth/differentiation factor 15 precursor (GDF-15) (Placental bone DE morphogenetic protein) (Placental TGF-beta) (Macrophage inhibitory DE cytokine 1) (MIC-1) (Prostate differentiation factor) (NSAID-regulated DE protein 1) (NRG-1). GN Name=GDF15; Synonyms=MIC1, PDF, PLAB, PTGFB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fibrosarcoma; RX MEDLINE=98006316; PubMed=9348093; RA Yokoyama-Kobayashi M., Saeki M., Sekine S., Kato S.; RT "Human cDNA encoding a novel TGF-beta superfamily protein highly RT expressed in placenta."; RL J. Biochem. 122:622-626(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=97470998; PubMed=9326641; DOI=10.1073/pnas.94.21.11514; RA Bootcov M.R., Bauskin A.R., Valenzuela S.M., Moore A.G., Bansal M., RA He X.Y., Zhang H.P., Donnellan M., Mahler S., Pryor K., Walsh B.J., RA Nicholson R.C., Fairlie W.D., Por S.B., Robbins J.M., Breit S.N.; RT "MIC-1, a novel macrophage inhibitory cytokine, is a divergent member RT of the TGF-beta superfamily."; RL Proc. Natl. Acad. Sci. U.S.A. 94:11514-11519(1997). RN [3] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Placenta; RX MEDLINE=98041637; PubMed=9375789; DOI=10.1016/S0167-4781(97)00122-X; RA Hromas R., Hufford M., Sutton J., Xu D., Li Y., Lu L.; RT "PLAB, a novel placental bone morphogenetic protein."; RL Biochim. Biophys. Acta 1354:40-44(1997). RN [4] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Placenta; RX MEDLINE=98256302; PubMed=9593718; DOI=10.1074/jbc.273.22.13760; RA Paralkar V.M., Vail A.L., Grasser W.A., Brown T.A., Xu H., RA Vukicevic S., Ke H.Z., Qi H., Owen T.A., Thompson D.D.; RT "Cloning and characterization of a novel member of the transforming RT growth factor-beta/bone morphogenetic protein family."; RL J. Biol. Chem. 273:13760-13767(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE OF 14-308. RX MEDLINE=98085971; PubMed=9426002; DOI=10.1016/S0378-1119(97)00485-X; RA Lawton L.N., de Fatima Bonaldo M., Jelenc P.C., Qiu L., Baumes S.A., RA Marcelino R.A., de Jesus G.M., Wellington S., Knowles J.A., RA Warburton D., Brown S., Soares M.B.; RT "Identification of a novel member of the TGF-beta superfamily highly RT expressed in human placenta."; RL Gene 203:17-26(1997). RN [7] RP NUCLEOTIDE SEQUENCE OF 264-308. RA Baek S.J., Nixon J., Eling T.; RT "NRG-1 is associated with apoptosis."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein (Probable). CC -!- TISSUE SPECIFICITY: Highly expressed in placenta, with lower CC levels in prostate and colon and some expression in kidney. CC -!- SIMILARITY: Belongs to the TGF-beta family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB000584; BAA19151.1; -; mRNA. DR EMBL; AF019770; AAB88673.1; -; mRNA. DR EMBL; U88323; AAB88913.1; -; mRNA. DR EMBL; AF003934; AAC24456.1; -; mRNA. DR EMBL; BT019465; AAV38272.1; -; mRNA. DR EMBL; AF008303; AAC39537.1; -; Genomic_DNA. DR EMBL; AF173860; AAF89834.1; -; mRNA. DR HSSP; P18075; 1LXI. DR Ensembl; ENSG00000130513; Homo sapiens. DR KEGG; hsa:9518; -. DR H-InvDB; HIX0014912; -. DR HGNC; HGNC:30142; GDF15. DR MIM; 605312; gene. DR ArrayExpress; Q99988; -. DR RZPD-ProtExp; N0088; -. DR GO; GO:0005576; C:extracellular region; TAS. DR GO; GO:0005125; F:cytokine activity; TAS. DR GO; GO:0007267; P:cell-cell signaling; TAS. DR GO; GO:0007165; P:signal transduction; TAS. DR GO; GO:0007179; P:transforming growth factor beta receptor si...; TAS. DR InterPro; IPR002400; GF_cysknot. DR InterPro; IPR001839; TGFb. DR Pfam; PF00019; TGF_beta; 1. DR PRINTS; PR00438; GFCYSKNOT. DR ProDom; PD000357; TGFb; 1. DR SMART; SM00204; TGFB; 1. DR PROSITE; PS00250; TGF_BETA_1; FALSE_NEG. KW Cytokine; Glycoprotein; Growth factor; Polymorphism; Signal. FT SIGNAL 1 29 Potential. FT PROPEP 30 194 Potential. FT /FTId=PRO_0000033992. FT CHAIN 195 308 Growth/differentiation factor 15. FT /FTId=PRO_0000033993. FT CARBOHYD 70 70 N-linked (GlcNAc...) (Potential). FT DISULFID 211 274 By similarity. FT DISULFID 240 305 By similarity. FT DISULFID 244 307 By similarity. FT DISULFID 273 273 Interchain (By similarity). FT VARIANT 48 48 T -> S (in dbSNP:1059369). FT /FTId=VAR_010386. FT CONFLICT 9 9 L -> V (in Ref. 3). FT CONFLICT 202 202 H -> D (in Ref. 3). FT CONFLICT 269 269 V -> E (in Ref. 3). FT CONFLICT 288 288 T -> A (in Ref. 7). SQ SEQUENCE 308 AA; 34168 MW; A0F3A3ED065ACA2E CRC64; MPGQELRTLN GSQMLLVLLV LSWLPHGGAL SLAEASRASF PGPSELHTED SRFRELRKRY EDLLTRLRAN QSWEDSNTDL VPAPAVRILT PEVRLGSGGH LHLRISRAAL PEGLPEASRL HRALFRLSPT ASRSWDVTRP LRRQLSLARP QAPALHLRLS PPPSQSDQLL AESSSARPQL ELHLRPQAAR GRRRARARNG DHCPLGPGRC CRLHTVRASL EDLGWADWVL SPREVQVTMC IGACPSQFRA ANMHAQIKTS LHRLKPDTVP APCCVPASYN PMVLIQKTDT GVSLQTYDDL LAKDCHCI // ID GFRA1_CHICK STANDARD; PRT; 469 AA. AC O13156; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 30-MAY-2006, entry version 37. DE GDNF family receptor alpha-1 precursor (GFR-alpha-1) (GDNF receptor DE alpha) (GDNFR-alpha) (TGF-beta-related neurotrophic factor receptor DE 1). GN Name=GFRA1; Synonyms=GDNFRA; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=97336104; PubMed=9192899; DOI=10.1038/42729; RA Buj-Bello A., Adu J., Pinon L.G.P., Horton A., Thompson J., RA Rosenthal A., Chinchetru M., Buchman V.L., Davies A.M.; RT "Neurturin responsiveness requires a GPI-linked receptor and the Ret RT receptor tyrosine kinase."; RL Nature 387:721-724(1997). CC -!- FUNCTION: Receptor for GDNF. Mediates the GDNF-induced CC autophosphorylation and activation of the RET receptor (By CC similarity). CC -!- SUBUNIT: 2 molecules of GDNFR-alpha are thought to form a complex CC with the disulfide-linked GDNF dimer and with 2 molecules of RET CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor (By CC similarity). CC -!- SIMILARITY: Belongs to the GDNFR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U90541; AAB61570.1; -; mRNA. DR UniGene; Gga.588; -. DR SMR; O13156; 238-345. DR Ensembl; ENSGALG00000009173; Gallus gallus. DR InterPro; IPR003438; GDNF_rcpt. DR InterPro; IPR003503; GDNF_rcpt_A1. DR Pfam; PF02351; GDNF; 1. DR PRINTS; PR01317; GDNFRALPHA1. DR PRINTS; PR01316; GDNFRECEPTOR. KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Receptor; Signal. FT SIGNAL 1 27 Potential. FT CHAIN 28 430 GDNF family receptor alpha-1. FT /FTId=PRO_0000010775. FT PROPEP 431 469 Removed in mature form (Potential). FT /FTId=PRO_0000010776. FT COMPBIAS 361 368 Poly-Thr. FT LIPID 430 430 GPI-anchor amidated serine (Potential). FT CARBOHYD 62 62 N-linked (GlcNAc...) (Potential). FT CARBOHYD 163 163 N-linked (GlcNAc...) (Potential). FT CARBOHYD 346 346 N-linked (GlcNAc...) (Potential). FT CARBOHYD 405 405 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 469 AA; 52043 MW; B9DB86D15218AF39 CRC64; MFLALLYLAL PLADVLLSAE VSGLPGGDRL DCVKASDQCL KEQSCSTKYR TLRQCVAGKE SNFSRATGLE AKDECKSAME ALKQKSLYNC RCKRGMKKEK NCLRIYWSMY QSLQGNDLLE DSPYEPVNSR LSDIFRLAPI VSVEPVLSKG NNCLDAAKAC NLNDTCKRFR SAYITPCTSS TSNEICNKRK CHKALRLFFD KVPPKHSYGM LFCSCRDVAC TERRRQTIVP VCSYEDREKP NCLNLQESCK KNYICRSRLA DFFTNCQPES RSVSSCLKEN YADCLLAYSG LIGTVMTPNY IDSSSLSVAP WCDCSNSGND IDECRKFLNF FQDNTCLKNA IQAFGNGTDV NVWQPILPVQ TTTATTTTAS RLKNTGSETT NNEIPTHNDS PACANLQAQK KRKSNESVDT ELCLNENAIG KDNTPGVSTS HISSENSFAL PTSFYPSTPL ILMTIALSLF LFLSSSVVL // ID GFRA1_HUMAN STANDARD; PRT; 465 AA. AC P56159; O15507; O43912; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 03-OCT-2006, entry version 58. DE GDNF family receptor alpha-1 precursor (GFR-alpha-1) (GDNF receptor DE alpha) (GDNFR-alpha) (TGF-beta-related neurotrophic factor receptor 1) DE (RET ligand 1). GN Name=GFRA1; Synonyms=GDNFRA, RETL1, TRNR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Substantia nigra; RX MEDLINE=96270513; PubMed=8674117; DOI=10.1016/S0092-8674(00)81311-2; RA Jing S., Wen D., Yu Y., Holst P.L., Luo Y., Fang M., Tamir R., RA Antonio L., Hu Z., Cupples R., Louis J.-C., Hu S., Altrock B.W., RA Fox G.M.; RT "GDNF-induced activation of the ret protein tyrosine kinase is RT mediated by GDNFR-alpha, a novel receptor for GDNF."; RL Cell 85:1113-1124(1996). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 2). RC TISSUE=Kidney; RX MEDLINE=97322356; PubMed=9177201; DOI=10.1073/pnas.94.12.6238; RA Sanicola M., Hession C.A., Worley D.S., Carmillo P., Ehrenfels C., RA Walus L., Robinson S., Jaworski G., Wei H., Tizard R., Whitty A., RA Pepinsky R.B., Cate R.L.; RT "Glial cell line-derived neurotrophic factor-dependent RET activation RT can be mediated by two different cell-surface accessory proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6238-6243(1997). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 1), AND VARIANTS ASN-85 AND ALA-366. RX MEDLINE=98207251; PubMed=9545641; DOI=10.1006/geno.1997.5191; RA Angrist M., Jing S., Bolk S., Bentley K., Nallasamy S., Halushka M., RA Fox G.M., Chakravarti A.; RT "Human GFRA1: cloning, mapping, genomic structure, and evaluation as a RT candidate gene for Hirschsprung disease susceptibility."; RL Genomics 48:354-362(1998). RN [4] RP NUCLEOTIDE SEQUENCE (ISOFORM 1). RC TISSUE=Thyroid carcinoma; RX MEDLINE=98260874; PubMed=9600247; DOI=10.1007/s004390050724; RA Shefelbine S.E., Khorana S., Schultz P.N., Huang E., Thobe N., RA Hu Z.J., Fox G.M., Jing S., Cote G.J., Gagel R.F.; RT "Mutational analysis of the GDNF/RET-GDNFR-alpha signaling complex in RT a kindred with vesicoureteral reflux."; RL Hum. Genet. 102:474-478(1998). RN [5] RP NUCLEOTIDE SEQUENCE (ISOFORM 2). RC TISSUE=Substantia nigra; RA Hishiki T., Kondoh K., Ichimiya S., Nimura Y., Seki N., Ozaki T., RA Sakiyama S., Takahashi H., Ohnuma N., Tanabe M., Fujimura S., RA Nakagawara A.; RT "GDNF-induced differentiation and its enhancement by retinoic acid in RT primary human neuroblastomas expressing c-Ret and GDNFR-alpha."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004). RN [8] RP VARIANTS ALA-366 AND ARG-371. RX MEDLINE=22982299; PubMed=14566559; DOI=10.1007/s00439-003-1036-z; RA Sasaki A., Kanai M., Kijima K., Akaba K., Hashimoto M., Hasegawa H., RA Otaki S., Koizumi T., Kusuda S., Ogawa Y., Tuchiya K., Yamamoto W., RA Nakamura T., Hayasaka K.; RT "Molecular analysis of congenital central hypoventilation syndrome."; RL Hum. Genet. 114:22-26(2003). CC -!- FUNCTION: Receptor for GDNF. Mediates the GDNF-induced CC autophosphorylation and activation of the RET receptor (By CC similarity). CC -!- SUBUNIT: 2 molecules of GDNFR-alpha are thought to form a complex CC with the disulfide-linked GDNF dimer and with 2 molecules of RET CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P56159-1; Sequence=Displayed; CC Name=2; CC IsoId=P56159-2; Sequence=VSP_001660; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay; CC -!- SIMILARITY: Belongs to the GDNFR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U97144; AAC51646.1; -; mRNA. DR EMBL; AF038420; AAC39693.1; -; Genomic_DNA. DR EMBL; AF038411; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038412; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038413; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038414; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038415; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038416; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038417; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038418; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038419; AAC39693.1; JOINED; Genomic_DNA. DR EMBL; AF038421; AAC39692.1; -; mRNA. DR EMBL; AF042080; AAB97371.1; -; mRNA. DR EMBL; AF058999; AAC14431.1; -; Genomic_DNA. DR EMBL; AF058990; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058991; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058992; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058993; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058994; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058995; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058996; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058997; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; AF058998; AAC14431.1; JOINED; Genomic_DNA. DR EMBL; U95847; AAB71811.1; -; mRNA. DR EMBL; BC014962; AAH14962.1; -; mRNA. DR UniGene; Hs.591913; -. DR SMR; P56159; 239-346. DR Ensembl; ENSG00000151892; Homo sapiens. DR KEGG; hsa:2674; -. DR H-InvDB; HIX0009233; -. DR HGNC; HGNC:4243; GFRA1. DR MIM; 601496; gene. DR ArrayExpress; P56159; -. DR GO; GO:0019898; C:extrinsic to membrane; NAS. DR GO; GO:0016167; F:glial cell line-derived neurotrophic factor...; TAS. DR GO; GO:0004872; F:receptor activity; NAS. DR GO; GO:0005102; F:receptor binding; TAS. DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; NAS. DR InterPro; IPR003438; GDNF_rcpt. DR InterPro; IPR003503; GDNF_rcpt_A1. DR Pfam; PF02351; GDNF; 1. DR PRINTS; PR01317; GDNFRALPHA1. DR PRINTS; PR01316; GDNFRECEPTOR. KW Alternative splicing; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; KW Polymorphism; Receptor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 429 GDNF family receptor alpha-1. FT /FTId=PRO_0000010777. FT PROPEP 430 465 Removed in mature form (Potential). FT /FTId=PRO_0000010778. FT COMPBIAS 362 369 Poly-Thr. FT LIPID 429 429 GPI-anchor amidated serine (Potential). FT CARBOHYD 59 59 N-linked (GlcNAc...) (Potential). FT CARBOHYD 347 347 N-linked (GlcNAc...) (Potential). FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 140 144 Missing (in isoform 2). FT /FTId=VSP_001660. FT VARIANT 85 85 Y -> N (in dbSNP:8192662). FT /FTId=VAR_012488. FT VARIANT 366 366 T -> A (in dbSNP:2072276). FT /FTId=VAR_012489. FT VARIANT 371 371 L -> R (may be involved in congenital FT central hypoventilation syndrome). FT /FTId=VAR_018261. FT CONFLICT 245 245 Missing (in Ref. 1). FT CONFLICT 358 358 F -> P (in Ref. 1). SQ SEQUENCE 465 AA; 51456 MW; 91A550D06A6777BD CRC64; MFLATLYFAL PLLDLLLSAE VSGGDRLDCV KASDQCLKEQ SCSTKYRTLR QCVAGKETNF SLASGLEAKD ECRSAMEALK QKSLYNCRCK RGMKKEKNCL RIYWSMYQSL QGNDLLEDSP YEPVNSRLSD IFRVVPFISD VFQQVEHIPK GNNCLDAAKA CNLDDICKKY RSAYITPCTT SVSNDVCNRR KCHKALRQFF DKVPAKHSYG MLFCSCRDIA CTERRRQTIV PVCSYEEREK PNCLNLQDSC KTNYICRSRL ADFFTNCQPE SRSVSSCLKE NYADCLLAYS GLIGTVMTPN YIDSSSLSVA PWCDCSNSGN DLEECLKFLN FFKDNTCLKN AIQAFGNGSD VTVWQPAFPV QTTTATTTTA LRVKNKPLGP AGSENEIPTH VLPPCANLQA QKLKSNVSGN THLCISNGNY EKEGLGASSH ITTKSMAAPP SCGLSPLLVL VVTALSTLLS LTETS // ID GFRA1_MOUSE STANDARD; PRT; 468 AA. AC P97785; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 19-SEP-2006, entry version 45. DE GDNF family receptor alpha-1 precursor (GFR-alpha-1) (GDNF receptor DE alpha) (GDNFR-alpha) (TGF-beta-related neurotrophic factor receptor DE 1). GN Name=Gfra1; Synonyms=Gdnfra, Trnr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Spinal ganglion; RA Watabe K.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Receptor for GDNF. Mediates the GDNF-induced CC autophosphorylation and activation of the RET receptor (By CC similarity). CC -!- SUBUNIT: 2 molecules of GDNFR-alpha are thought to form a complex CC with the disulfide-linked GDNF dimer and with 2 molecules of RET CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor (By CC similarity). CC -!- SIMILARITY: Belongs to the GDNFR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB000800; BAA19185.1; -; mRNA. DR SMR; P97785; 239-346. DR Ensembl; ENSMUSG00000025089; Mus musculus. DR KEGG; mmu:14585; -. DR MGI; MGI:1100842; Gfra1. DR ArrayExpress; P97785; -. DR GO; GO:0019898; C:extrinsic to membrane; TAS. DR GO; GO:0004872; F:receptor activity; TAS. DR GO; GO:0009653; P:morphogenesis; TAS. DR GO; GO:0007399; P:nervous system development; IMP. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kin...; TAS. DR InterPro; IPR003438; GDNF_rcpt. DR InterPro; IPR003503; GDNF_rcpt_A1. DR Pfam; PF02351; GDNF; 1. DR PRINTS; PR01317; GDNFRALPHA1. DR PRINTS; PR01316; GDNFRECEPTOR. KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Receptor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 430 GDNF family receptor alpha-1. FT /FTId=PRO_0000010779. FT PROPEP 431 468 Removed in mature form (Potential). FT /FTId=PRO_0000010780. FT COMPBIAS 362 369 Thr-rich. FT LIPID 430 430 GPI-anchor amidated serine (Potential). FT CARBOHYD 59 59 N-linked (GlcNAc...) (Potential). FT CARBOHYD 347 347 N-linked (GlcNAc...) (Potential). FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 468 AA; 51782 MW; AABE393177307212 CRC64; MFLATLYFVL PLLDLLMSAE VSGGDRLDCV KASDQCLKEQ SCSTKYRTLR QCVAGKETNF SLTSGLEAKD ECRSAMEALK QKSLYNCRCK RGMKKEKNCL RIYWSMYQSL QGNDLLEDSP YEPVNSRLSD IFRAVPFISD VFQQVEHISK GNNCLDAAKA CNLDDTCKKY RSAYITPCTT SMSNEVCNRR KCHKALRQFF DKVPAKHSYG MLFCSCRDVA CTERRRQTIV PVCSYEERER PNCLNLQDSC KTNYICRSRL ADFFTNCQPE SRSVSNCLKE NYADCLLAYS GLIGTVMTPN YIDSSSLSVA PWCDCSNSGN DLEDCLKFLN FFKDNTCLKN AIQAFGNGSD VTMWQPAPPV QTTTAMTTTA FRIKNKPLGP AGSENEIPTH VLPPCANLQA QKLKSNVSGS THLCLSDNDY GKDGLAGASS HITTKSMAAP PSCGLSSLPV MVFTALAALL SVSLAETS // ID GFRA1_RAT STANDARD; PRT; 468 AA. AC Q62997; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-SEP-2006, entry version 46. DE GDNF family receptor alpha-1 precursor (GFR-alpha-1) (GDNF receptor DE alpha) (GDNFR-alpha) (TGF-beta-related neurotrophic factor receptor 1) DE (RET ligand 1). GN Name=Gfra1; Synonyms=Gdnfra, Retl1, Trnr1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retina; RX MEDLINE=96270513; PubMed=8674117; DOI=10.1016/S0092-8674(00)81311-2; RA Jing S., Wen D., Yu Y., Holst P.L., Luo Y., Fang M., Tamir R., RA Antonio L., Hu Z., Cupples R., Louis J.-C., Hu S., Altrock B.W., RA Fox G.M.; RT "GDNF-induced activation of the ret protein tyrosine kinase is RT mediated by GDNFR-alpha, a novel receptor for GDNF."; RL Cell 85:1113-1124(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Kidney; RX MEDLINE=97322356; PubMed=9177201; DOI=10.1073/pnas.94.12.6238; RA Sanicola M., Hession C.A., Worley D.S., Carmillo P., Ehrenfels C., RA Walus L., Robinson S., Jaworski G., Wei H., Tizard R., Whitty A., RA Pepinsky R.B., Cate R.L.; RT "Glial cell line-derived neurotrophic factor-dependent RET activation RT can be mediated by two different cell-surface accessory proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6238-6243(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96273032; PubMed=8657309; DOI=10.1038/382080a0; RA Treanor J.J.S., Googman L., de Sauvage F., Stone D.M., Poulsen K.T., RA Beck C.D., Gray C., Armanini M.P., Pollock R.A., Hefti F., RA Phillips H.S., Goddard A., Moore M.W., Buj-Bello A., Davies A.M., RA Asai N., Takahashi M., Vandlen R., Henderson C.E., Rosenthal A.; RT "Characterization of a multicomponent receptor for GDNF."; RL Nature 382:80-83(1996). RN [4] RP TISSUE SPECIFICITY. RX MEDLINE=20185640; PubMed=10719212; DOI=10.1016/S0169-328X(99)00328-9; RA Stoever T., Gong T.-W.L., Cho Y., Altschuler R.A., Lomax M.I.; RT "Expression of the GDNF family members and their receptors in the RT mature rat cochlea."; RL Brain Res. Mol. Brain Res. 76:25-35(2000). CC -!- FUNCTION: Receptor for GDNF. Mediates the GDNF-induced CC autophosphorylation and activation of the RET receptor. CC -!- SUBUNIT: 2 molecules of GDNFR-alpha are thought to form a complex CC with the disulfide-linked GDNF dimer and with 2 molecules of RET. CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor. CC -!- TISSUE SPECIFICITY: Expressed in liver, brain, kidney and cochlea. CC -!- SIMILARITY: Belongs to the GDNFR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U59486; AAC52663.1; -; mRNA. DR EMBL; U97142; AAC53300.1; -; mRNA. DR UniGene; Rn.88489; -. DR PDB; 1Q8D; X-ray; A=239-346. DR Ensembl; ENSRNOG00000017438; Rattus norvegicus. DR RGD; 2681; Gfra1. DR ArrayExpress; Q62997; -. DR GO; GO:0046658; C:anchored to plasma membrane; TAS. DR GO; GO:0004872; F:receptor activity; IDA. DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS. DR InterPro; IPR003438; GDNF_rcpt. DR InterPro; IPR003503; GDNF_rcpt_A1. DR Pfam; PF02351; GDNF; 1. DR PRINTS; PR01317; GDNFRALPHA1. DR PRINTS; PR01316; GDNFRECEPTOR. KW 3D-structure; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; KW Receptor; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 430 GDNF family receptor alpha-1. FT /FTId=PRO_0000010781. FT PROPEP 431 468 Removed in mature form (Potential). FT /FTId=PRO_0000010782. FT COMPBIAS 362 369 Poly-Thr. FT LIPID 430 430 GPI-anchor amidated serine (Potential). FT CARBOHYD 59 59 N-linked (GlcNAc...) (Potential). FT CARBOHYD 347 347 N-linked (GlcNAc...) (Potential). FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential). FT STRAND 242 242 FT HELIX 243 251 FT TURN 252 252 FT STRAND 253 253 FT HELIX 254 266 FT TURN 267 267 FT STRAND 270 273 FT STRAND 276 276 FT HELIX 279 290 FT TURN 291 294 FT STRAND 295 295 FT TURN 296 297 FT STRAND 312 312 FT STRAND 314 314 FT TURN 316 317 FT HELIX 319 333 FT STRAND 334 334 FT HELIX 336 345 SQ SEQUENCE 468 AA; 51650 MW; B2EE5906F5025E0F CRC64; MFLATLYFAL PLLDLLMSAE VSGGDRLDCV KASDQCLKEQ SCSTKYRTLR QCVAGKETNF SLTSGLEAKD ECRSAMEALK QKSLYNCRCK RGMKKEKNCL RIYWSMYQSL QGNDLLEDSP YEPVNSRLSD IFRAVPFISD VFQQVEHISK GNNCLDAAKA CNLDDTCKKY RSAYITPCTT SMSNEVCNRR KCHKALRQFF DKVPAKHSYG MLFCSCRDIA CTERRRQTIV PVCSYEERER PNCLSLQDSC KTNYICRSRL ADFFTNCQPE SRSVSNCLKE NYADCLLAYS GLIGTVMTPN YVDSSSLSVA PWCDCSNSGN DLEDCLKFLN FFKDNTCLKN AIQAFGNGSD VTMWQPAPPV QTTTATTTTA FRVKNKPLGP AGSENEIPTH VLPPCANLQA QKLKSNVSGS THLCLSDSDF GKDGLAGASS HITTKSMAAP PSCSLSSLPV LMLTALAALL SVSLAETS // ID GFRA2_HUMAN STANDARD; PRT; 464 AA. AC O00451; O15316; O15328; Q7Z5C2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 19-SEP-2006, entry version 54. DE GDNF family receptor alpha-2 precursor (GFR-alpha-2) (Neurturin DE receptor alpha) (NTNR-alpha) (NRTNR-alpha) (TGF-beta-related DE neurotrophic factor receptor 2) (GDNF receptor beta) (GDNFR-beta) (RET DE ligand 2). GN Name=GFRA2; Synonyms=GDNFRB, RETL2, TRNR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX MEDLINE=97325791; PubMed=9182803; DOI=10.1016/S0896-6273(00)80318-9; RA Baloh R.H., Tansey M.G., Golden J.P., Creedon D.J., Heuckeroth R.O., RA Keck C.L., Zimonjic D.B., Popescu N.C., Johnson E.M. Jr., RA Milbrandt J.; RT "TrnR2, a novel receptor that mediates neurturin and GDNF signaling RT through Ret."; RL Neuron 18:793-802(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX MEDLINE=97402208; PubMed=9259272; DOI=10.1093/hmg/6.8.1267; RA Suvanto P., Wartiovaara K., Lindahl M., Arumae U., Moshnyakov M., RA Horelli-Kuitunen N., Airaksinen M.S., Palotie A., Sariola H., RA Saarma M.; RT "Cloning, mRNA distribution and chromosomal localisation of the gene RT for glial cell line-derived neurotrophic factor receptor beta, a RT homologue to GDNFR-alpha."; RL Hum. Mol. Genet. 6:1267-1273(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX MEDLINE=97322356; PubMed=9177201; DOI=10.1073/pnas.94.12.6238; RA Sanicola M., Hession C.A., Worley D.S., Carmillo P., Ehrenfels C., RA Walus L., Robinson S., Jaworski G., Wei H., Tizard R., Whitty A., RA Pepinsky R.B., Cate R.L.; RT "Glial cell line-derived neurotrophic factor-dependent RET activation RT can be mediated by two different cell-surface accessory proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6238-6243(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Yoong L.F., Too H.P.; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Receptor for neurturin. Mediates the NRTN-induced CC autophosphorylation and activation of the RET receptor. Also able CC to mediate GDNF signaling through the RET tyrosine kinase CC receptor. CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long; CC IsoId=O00451-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=O00451-2; Sequence=VSP_001661; CC -!- TISSUE SPECIFICITY: Isoform 1 is found in both brain and placenta. CC -!- SIMILARITY: Belongs to the GDNFR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF002700; AAC52036.1; -; mRNA. DR EMBL; U93703; AAB61922.1; -; mRNA. DR EMBL; U97145; AAC51647.1; -; mRNA. DR EMBL; AY326396; AAP88378.1; -; mRNA. DR Ensembl; ENSG00000168546; Homo sapiens. DR KEGG; hsa:2675; -. DR HGNC; HGNC:4244; GFRA2. DR MIM; 601956; gene. DR ArrayExpress; O00451; -. DR RZPD-ProtExp; M0264; -. DR GO; GO:0019898; C:extrinsic to membrane; TAS. DR GO; GO:0016167; F:glial cell line-derived neurotrophic factor...; TAS. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kin...; TAS. DR InterPro; IPR003438; GDNF_rcpt. DR InterPro; IPR003504; GDNF_rcpt_A2. DR Pfam; PF02351; GDNF; 1. DR PRINTS; PR01318; GDNFRALPHA2. DR PRINTS; PR01316; GDNFRECEPTOR. KW Alternative splicing; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; KW Receptor; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 444 GDNF family receptor alpha-2. FT /FTId=PRO_0000010785. FT PROPEP 445 464 Removed in mature form (Potential). FT /FTId=PRO_0000010786. FT LIPID 444 444 GPI-anchor amidated serine (Potential). FT CARBOHYD 52 52 N-linked (GlcNAc...) (Potential). FT CARBOHYD 357 357 N-linked (GlcNAc...) (Potential). FT CARBOHYD 413 413 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 14 146 Missing (in isoform 2). FT /FTId=VSP_001661. FT CONFLICT 6 6 V -> A (in Ref. 2). FT CONFLICT 462 462 Q -> L (in Ref. 3). SQ SEQUENCE 464 AA; 51559 MW; 8BC604D9530FF21F CRC64; MILANVFCLF FFLDETLRSL ASPSSLQGPE LHGWRPPVDC VRANELCAAE SNCSSRYRTL RQCLAGRDRN TMLANKECQA ALEVLQESPL YDCRCKRGMK KELQCLQIYW SIHLGLTEGE EFYEASPYEP VTSRLSDIFR LASIFSGTGA DPVVSAKSNH CLDAAKACNL NDNCKKLRSS YISICNREIS PTERCNRRKC HKALRQFFDR VPSEYTYRML FCSCQDQACA ERRRQTILPS CSYEDKEKPN CLDLRGVCRT DHLCRSRLAD FHANCRASYQ TVTSCPADNY QACLGSYAGM IGFDMTPNYV DSSPTGIVVS PWCSCRGSGN MEEECEKFLR DFTENPCLRN AIQAFGNGTD VNVSPKGPSF QATQAPRVEK TPSLPDDLSD STSLGTSVIT TCTSVQEQGL KANNSKELSM CFTELTTNII PGSNKVIKPN SGPSRARPSA ALTVLSVLML KQAL // ID GFRA2_MOUSE STANDARD; PRT; 463 AA. AC O08842; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 19-SEP-2006, entry version 50. DE GDNF family receptor alpha-2 precursor (GFR-alpha-2) (Neurturin DE receptor alpha) (NTNR-alpha) (NRTNR-alpha) (TGF-beta-related DE neurotrophic factor receptor 2) (GDNF receptor beta) (GDNFR-beta). GN Name=Gfra2; Synonyms=Gdnfrb, Trnr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX MEDLINE=97325791; PubMed=9182803; DOI=10.1016/S0896-6273(00)80318-9; RA Baloh R.H., Tansey M.G., Golden J.P., Creedon D.J., Heuckeroth R.O., RA Keck C.L., Zimonjic D.B., Popescu N.C., Johnson E.M. Jr., RA Milbrandt J.; RT "TrnR2, a novel receptor that mediates neurturin and GDNF signaling RT through Ret."; RL Neuron 18:793-802(1997). CC -!- FUNCTION: Receptor for neurturin. Mediates the NRTN-induced CC autophosphorylation and activation of the RET receptor. Also able CC to mediate GDNF signaling through the RET tyrosine kinase CC receptor. CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor; GPI-anchor (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Long; CC IsoId=O08842-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=O08842-2; Sequence=VSP_001662; CC -!- TISSUE SPECIFICITY: Neurons of the superior cervical and dorsal CC root ganglia, and adult brain and testis. Low level in the spleen CC and in the adrenal gland. CC -!- SIMILARITY: Belongs to the GDNFR family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF002701; AAC53548.1; -; mRNA. DR Ensembl; ENSMUSG00000022103; Mus musculus. DR KEGG; mmu:14586; -. DR MGI; MGI:1195462; Gfra2. DR ArrayExpress; O08842; -. DR GO; GO:0007399; P:nervous system development; IMP. DR InterPro; IPR003438; GDNF_rcpt. DR InterPro; IPR003504; GDNF_rcpt_A2. DR Pfam; PF02351; GDNF; 1. DR PRINTS; PR01318; GDNFRALPHA2. DR PRINTS; PR01316; GDNFRECEPTOR. KW Alternative splicing; Glycoprotein; GPI-anchor; Lipoprotein; Membrane; KW Receptor; Signal. FT SIGNAL 1 21 Potential. FT CHAIN 22 443 GDNF family receptor alpha-2. FT /FTId=PRO_0000010787. FT PROPEP 444 463 Removed in mature form (Potential). FT /FTId=PRO_0000010788. FT LIPID 443 443 GPI-anchor amidated serine (Potential). FT CARBOHYD 52 52 N-linked (GlcNAc...) (Potential). FT CARBOHYD 357 357 N-linked (GlcNAc...) (Potential). FT CARBOHYD 413 413 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 14 146 Missing (in isoform 2). FT /FTId=VSP_001662. SQ SEQUENCE 463 AA; 51599 MW; 4FB495FA58C61F78 CRC64; MILANAFCLF FFLDETLRSL ASPSSPQGSE LHGWRPQVDC VRANELCAAE SNCSSRYRTL RQCLAGRDRN TMLANKECQA ALEVLQESPL YDCRCKRGMK KELQCLQIYW SIHLGLTEGE EFYEASPYEP VTSRLSDIFR LASIFSGTGA DPVVSAKSNH CLDAAKACNL NDNCKKLRSS YISICNREIS PTERCNRRKC HKALRQFFDR VPSEYTYRML FCSCQDQACA ERRRQTILPS CSYEDKEKPN CLDLRSLCRT DHLCRSRLAD FHANCRASYR TITSCPADNY QACLGSYAGM IGFDMTPNYV DSNPTGIVVS PWCNCRGSGN MEEECEKFLK DFTENPCLRN AIQAFGNGTD VNMSPKGPTF SATQAPRVEK TPSLPDDLSD STSLGTSVIT TCTSIQEQGL KANNSKELSM CFTELTTNIS PGSKKVIKLY SGSCRARLST ALTALPLLMV TLA // ID GSLG1_CRIGR STANDARD; PRT; 1160 AA. AC Q9Z1E9; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 03-OCT-2006, entry version 39. DE Golgi apparatus protein 1 precursor (Golgi sialoglycoprotein MG-160) DE (E-selectin ligand 1) (ESL-1) (Latent TGF-beta complexed protein 1) DE (LTCP-1). GN Name=GLG1; Synonyms=ESL1, MG160; OS Cricetulus griseus (Chinese hamster). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 80-87; 180-201; RP 215-223; 240-252; 266-273; 342-348; 442-448; 527-536; 632-645; RP 847-858; 930-937 AND 961-977. RC TISSUE=Ovary; RX MEDLINE=97307852; PubMed=9182700; RA Olofsson A., Hellman U., Ten Dijke P., Grimsby S., Ichijo H., RA Moren A., Miyazono K., Heldin C.-H.; RT "Latent transforming growth factor-beta complex in Chinese hamster RT ovary cells contains the multifunctional cysteine-rich fibroblast RT growth factor receptor, also termed E-selectin-ligand or MG-160."; RL Biochem. J. 324:427-434(1997). CC -!- FUNCTION: Binds fibroblast growth factor and E-selectin (cell- CC adhesion lectin on endothelial cells mediating the binding of CC neutrophils) (By similarity). CC -!- SUBCELLULAR LOCATION: Golgi apparatus; Golgi apparatus membrane; CC single-pass type I membrane protein (By similarity). CC -!- PTM: Fucosylation is essential for binding to E-selectin (By CC similarity). CC -!- PTM: N-glycosylated. Contains sialic acid residues (By CC similarity). CC -!- SIMILARITY: Contains 15 Cys-rich GLG1 repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U51162; AAD00079.1; -; mRNA. DR InterPro; IPR001893; Cys_rich_FGFR. DR Pfam; PF00839; Cys_rich_FGFR; 15. KW Direct protein sequencing; Glycoprotein; Golgi apparatus; Membrane; KW Repeat; Sialic acid; Signal; Transmembrane. FT SIGNAL 1 18 Potential. FT CHAIN 19 1160 Golgi apparatus protein 1. FT /FTId=PRO_0000011119. FT TOPO_DOM 19 1126 Extracellular (Potential). FT TRANSMEM 1127 1147 Potential. FT TOPO_DOM 1148 1160 Cytoplasmic (Potential). FT REPEAT 134 193 Cys-rich GLG1 1. FT REPEAT 195 259 Cys-rich GLG1 2. FT REPEAT 270 327 Cys-rich GLG1 3. FT REPEAT 330 394 Cys-rich GLG1 4. FT REPEAT 398 454 Cys-rich GLG1 5. FT REPEAT 459 518 Cys-rich GLG1 6. FT REPEAT 521 585 Cys-rich GLG1 7. FT REPEAT 593 649 Cys-rich GLG1 8. FT REPEAT 650 710 Cys-rich GLG1 9. FT REPEAT 713 769 Cys-rich GLG1 10. FT REPEAT 780 837 Cys-rich GLG1 11. FT REPEAT 838 893 Cys-rich GLG1 12. FT REPEAT 896 960 Cys-rich GLG1 13. FT REPEAT 963 1023 Cys-rich GLG1 14. FT REPEAT 1025 1082 Cys-rich GLG1 15. FT COMPBIAS 61 67 Poly-Gln. FT CARBOHYD 146 146 N-linked (GlcNAc...) (Potential). FT CARBOHYD 191 191 N-linked (GlcNAc...) (Potential). FT CARBOHYD 562 562 N-linked (GlcNAc...) (Potential). FT CARBOHYD 658 658 N-linked (GlcNAc...) (Potential). FT CARBOHYD 767 767 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 1160 AA; 132326 MW; 9D30E2D1DAAC03CB CRC64; MFRLSAALQL LLLAATGAQN NHGQVQVPGA NIGPLLGQAE GGSPAGQQLL QLSQQQKQPP QQQQQQQPAF PAGGPPARRG GAGPGGTGGG WKLAEEESCR EDVTRVCPKH TWSNNLAVLE CLQDVREPEN EISSDCNHLL WNYKLNLTTD PKFESVAREV CKSTISEIKE CAEEPVGKGY MVSCLVDHRG NITEYQCHQY ITKMTAIIFS DYRLICGFMD DCKNDINLLK CGSIRLGEKD AHSQGEVVSC LEKGLVKEAE EKEPKIQVSE LCKKAILRVA ELSSDDFHLD RHLYFACRDD RERFCENTQA GEGRVYKCLF NHKFEESMSE KCREALTTRQ KLIAQDYKVS YSLAKSCKSD LKKYRCNVEN LPRSREARLS YLLMCLESAV HRGRQVSSEC QGEMLDYRRM LMEDFSLSPE IILSCRGEIE HHCSGLHRKG RTLHCLMKVI RGEKGNLGMN CQQALQTLIQ ETDPGADYRI DRALNEACES VIQTACKHIR SGDPMILSCL MEHLYTEKMV EDCEHRLLEL QYFISRDWKL DPVLYRKCQG DASRLCHTHG WNETSELMPP GAVFSCLYRH AYRTEEQGRR LSRECRAEVQ RILHQRAMDV KLDPALQDKC LIDLGKWCSE KTETGQELEC LQDHLDDLAV ECRDIVGNLT ELESEDIQIE ALLMRACEPI IQNFCHDVAD NQIDSGDLME CLIQNKHQKD MNEKCAIGVT HFQLVQMKDF RFSYKFKMAC KEDVLKLCPN IKKKVDVVIC LSTTVRNDTL QEAKEHRVSL KCRKQLRVEE LEMTEDIRLE PDLYEACKSD IRGYCSTVQY GNAQIIECLK ENKKQLSTRC HQKVFKLQET EMMDPELDYT LMRVCKQMIK RFCPEADSKT MLQCLKQNKN SELMDPKCKQ MITKRQITQN TDYRLNPVLR KACKADIPKF CHGILTKAKD DSELEGQVIS CLKLRYADQR LSSDCEDQIR IIIQESALDY RLDPQLQLHC SDEIANLCAE EAAAQEQTGQ VEECLKVNLL KIRTELCKKE VLNMLKESKA DIFVDPVLHT ACALDIKHHC AAITPGRGRQ MSCLMEALED KRVRLQPECK KRLNDRIEMW SYAAKVAPAD GFSDLAMQVM TSPSKNYILS VISGSICILF LIGLMCGRIT KRVTRELKDR // ID IF32_ARATH STANDARD; PRT; 328 AA. AC Q38884; O82342; Q94K09; Q9C5Z0; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 2. DT 19-SEP-2006, entry version 42. DE Eukaryotic translation initiation factor 3 subunit 2 (eIF-3 beta) DE (eIF3 p36) (eIF3i) (TGF-beta receptor-interacting protein 1) (TRIP-1). GN Name=TIF3I1; OrderedLocusNames=At2g46280; ORFNames=T3F17.7; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=96013749; PubMed=7566156; DOI=10.1038/377548a0; RA Chen R.H., Miettinen P.J., Maruka E.M., Choy L., Derynck R.; RT "A WD-domain protein that is associated with and phosphorylated by the RT type II TGF-beta receptor."; RL Nature 377:548-552(1995). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=21125776; PubMed=11042177; DOI=10.1074/jbc.M007236200; RA Burks E.A., Bezerra P.P., Le H., Gallie D.R., Browning K.S.; RT "Plant initiation factor 3 subunit composition resembles mammalian RT initiation factor 3 and has a novel subunit."; RL J. Biol. Chem. 276:2122-2131(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). CC -!- FUNCTION: eIF-3 dissociates ribosomes, promotes initiator Met-tRNA CC and mRNA binding. CC -!- SUBUNIT: eIF-3 is composed of at least 12 different subunits. CC -!- SIMILARITY: Contains 5 WD repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U36765; AAC49079.1; -; mRNA. DR EMBL; AF285835; AAG53616.1; -; mRNA. DR EMBL; AC005397; AAC62878.1; -; Genomic_DNA. DR EMBL; AF370485; AAK43862.1; -; mRNA. DR EMBL; AY064633; AAL47346.1; -; mRNA. DR PIR; H84900; H84900. DR PIR; S60256; S60256. DR UniGene; At.21646; -. DR HSSP; P16649; 1ERJ. DR GenomeReviews; CT485783_GR; AT2G46280. DR KEGG; ath:At2g46280; -. DR GeneFarm; 2828; 267. DR TAIR; At2g46280; -. DR ArrayExpress; Q38884; -. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 3. DR SMART; SM00320; WD40; 4. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. KW Initiation factor; Protein biosynthesis; Repeat; WD repeat. FT CHAIN 1 328 Eukaryotic translation initiation factor FT 3 subunit 2. FT /FTId=PRO_0000051039. FT REPEAT 8 38 WD 1. FT REPEAT 50 80 WD 2. FT REPEAT 144 176 WD 3. FT REPEAT 189 221 WD 4. FT REPEAT 288 318 WD 5. FT CONFLICT 21 23 EGD -> QPH (in Ref. 2). FT CONFLICT 107 107 L -> F (in Ref. 2). FT CONFLICT 126 128 RIA -> AYC (in Ref. 1). FT CONFLICT 166 166 G -> C (in Ref. 1). FT CONFLICT 255 255 Q -> E (in Ref. 1). FT CONFLICT 275 275 Y -> C (in Ref. 1). FT CONFLICT 304 304 S -> G (in Ref. 4). FT CONFLICT 311 311 D -> G (in Ref. 1). SQ SEQUENCE 328 AA; 36388 MW; 4ABFE9866A09CFAF CRC64; MRPILMKGHE RPLTFLRYNR EGDLLFSCAK DHTPTLWFAD NGERLGTYRG HNGAVWCCDV SRDSSRLITG SADQTAKLWD VKSGKELFTF KFNAPTRSVD FAVGDRLAVI TTDHFVDRTA AIHVKRIAED PEEQDAESVL VLHCPDGKKR INRAVWGPLN QTIVSGGEDK VIRIWDAETG KLLKQSDEEV GHKKDITSLC KAADDSHFLT GSLDKTAKLW DMRTLTLLKT YTTVVPVNAV SLSPLLNHVV LGGGQDASAV TTTDHRAGKF EAKFYDKILQ EEIGGVKGHF GPINALAFNP DGKSFSSGGE DGYVRLHHFD SDYFNIKI // ID IF32_HUMAN STANDARD; PRT; 325 AA. AC Q13347; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 03-OCT-2006, entry version 61. DE Eukaryotic translation initiation factor 3 subunit 2 (eIF-3 beta) DE (eIF3 p36) (eIF3i) (TGF-beta receptor-interacting protein 1) (TRIP-1). GN Name=EIF3S2; Synonyms=TRIP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=97150873; PubMed=8995409; DOI=10.1074/jbc.272.28.17668; RA Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.; RT "Conservation and diversity of eukaryotic translation initiation RT factor eIF3."; RL J. Biol. Chem. 272:1101-1109(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96013749; PubMed=7566156; DOI=10.1038/377548a0; RA Chen R.H., Miettinen P.J., Maruka E.M., Choy L., Derynck R.; RT "A WD-domain protein that is associated with and phosphorylated by the RT type II TGF-beta receptor."; RL Nature 377:548-552(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASS RP SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). CC -!- FUNCTION: Binds to the 40S ribosome and promotes the binding of CC methionyl-tRNAi and mRNA. CC -!- SUBUNIT: eIF-3 is composed of at least 12 different subunits. CC -!- INTERACTION: CC Q9UMF9:-; NbExp=1; IntAct=EBI-354047, EBI-366696; CC -!- PTM: Phosphorylated by TGF-beta type II receptor. CC -!- SIMILARITY: Contains 5 WD repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U39067; AAC97144.1; -; mRNA. DR EMBL; U36764; AAC50224.1; -; mRNA. DR EMBL; BC000413; AAH00413.1; -; mRNA. DR EMBL; BC003140; AAH03140.1; -; mRNA. DR PIR; S60335; S60335. DR UniGene; Hs.530096; -. DR HSSP; P16649; 1ERJ. DR IntAct; Q13347; -. DR OGP; Q13347; -. DR PHCI-2DPAGE; Q13347; -. DR Ensembl; ENSG00000084623; Homo sapiens. DR KEGG; hsa:8668; -. DR H-InvDB; HIX0018823; -. DR HGNC; HGNC:3272; EIF3S2. DR MIM; 603911; gene. DR Reactome; Q13347; -. DR LinkHub; Q13347; -. DR ArrayExpress; Q13347; -. DR RZPD-ProtExp; I0376; -. DR RZPD-ProtExp; IOH3628; -. DR RZPD-ProtExp; RZPDo839H08121; -. DR RZPD-ProtExp; RZPDo839H08122; -. DR RZPD-ProtExp; T0377; -. DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 ...; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0008135; F:translation factor activity, nucleic acid b...; TAS. DR GO; GO:0006446; P:regulation of translational initiation; TAS. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 2. DR SMART; SM00320; WD40; 3. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. KW Initiation factor; Phosphorylation; Protein biosynthesis; Repeat; KW WD repeat. FT CHAIN 1 325 Eukaryotic translation initiation factor FT 3 subunit 2. FT /FTId=PRO_0000051036. FT REPEAT 8 47 WD 1. FT REPEAT 50 91 WD 2. FT REPEAT 144 183 WD 3. FT REPEAT 186 225 WD 4. FT REPEAT 283 324 WD 5. FT MOD_RES 308 308 Phosphotyrosine. SQ SEQUENCE 325 AA; 36502 MW; 02797BB72A752A96 CRC64; MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEA // ID IF32_MOUSE STANDARD; PRT; 325 AA. AC Q9QZD9; DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 03-OCT-2006, entry version 43. DE Eukaryotic translation initiation factor 3 subunit 2 (eIF-3 beta) DE (eIF3 p36) (eIF3i) (TGF-beta receptor-interacting protein 1) (TRIP-1). GN Name=Eif3s2; Synonyms=Trip1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhou A., Silverman R.H.; RT "Mouse TRIP-1 gene isolated from murine L-929 cells."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Joseph P., Fan L., Whong W.-Z., Ong T.-M.; RT "Mus musculus TGF-beta receptor interacting protein 1 (TRIP1)."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic stem cell, and Kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Binds to the 40S ribosome and promotes the binding of CC methionyl-tRNAi and mRNA (By similarity). CC -!- SUBUNIT: eIF-3 is composed of at least 12 different subunits. CC -!- PTM: Phosphorylated by TGF-beta type II receptor (By similarity). CC -!- SIMILARITY: Contains 5 WD repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF188297; AAF01455.1; -; mRNA. DR EMBL; AF271072; AAF76199.1; -; mRNA. DR EMBL; AK012375; BAB28197.1; -; mRNA. DR EMBL; AK002896; BAB22440.1; -; mRNA. DR EMBL; AK010781; BAB27177.1; -; mRNA. DR EMBL; BC029625; AAH29625.1; -; mRNA. DR UniGene; Mm.250874; -. DR HSSP; P16649; 1ERJ. DR Ensembl; ENSMUSG00000028798; Mus musculus. DR KEGG; mmu:54709; -. DR MGI; MGI:1860763; Eif3s2. DR ArrayExpress; Q9QZD9; -. DR InterPro; IPR001680; WD40. DR InterPro; IPR011046; WD40_like. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 2. DR SMART; SM00320; WD40; 3. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. KW Initiation factor; Phosphorylation; Protein biosynthesis; Repeat; KW WD repeat. FT CHAIN 1 325 Eukaryotic translation initiation factor FT 3 subunit 2. FT /FTId=PRO_0000051037. FT REPEAT 8 47 WD 1. FT REPEAT 50 91 WD 2. FT REPEAT 144 183 WD 3. FT REPEAT 186 225 WD 4. FT REPEAT 283 324 WD 5. FT MOD_RES 308 308 Phosphotyrosine (By similarity). SQ SEQUENCE 325 AA; 36461 MW; 2B29405772675CC0 CRC64; MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC FVSFFDLRDP SQIDSNEPYM KIPCNDSKIT SAVWGPLGEC VIAGHESGEL NQYSAKSGEV LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY SSGGEDGYVR IHYFDPQYFE FEFEA // ID LTBP1_RAT STANDARD; PRT; 1712 AA. AC Q00918; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 05-SEP-2006, entry version 60. DE Latent-transforming growth factor beta-binding protein 1 precursor DE (LTBP-1) (Transforming growth factor beta-1-binding protein 1) (TGF- DE beta-1-BP-1) (Transforming growth factor beta-1-masking protein, large DE subunit). GN Name=Ltbp1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=91062373; PubMed=2247454; RA Tsuji T., Okada F., Yamaguchi K., Nakamura T.; RT "Molecular cloning of the large subunit of transforming growth factor RT type beta masking protein and expression of the mRNA in various rat RT tissues."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8835-8839(1990). RN [2] RP FUNCTION. RX PubMed=7593177; DOI=10.1083/jcb.131.2.539; RA Dallas S.L., Miyazono K., Skerry T.M., Mundy G.R., Bonewald L.F.; RT "Dual role for the latent transforming growth factor-beta binding RT protein in storage of latent TGF-beta in the extracellular matrix and RT as a structural matrix protein."; RL J. Cell Biol. 131:539-549(1995). RN [3] RP REVIEW. RX MEDLINE=20207905; PubMed=10743502; DOI=10.1016/S1359-6101(99)00010-6; RA Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.; RT "Latent transforming growth factor-beta binding proteins (LTBPs) -- RT structural extracellular matrix proteins for targeting TGF-beta RT action."; RL Cytokine Growth Factor Rev. 10:99-117(1999). RN [4] RP REVIEW. RX MEDLINE=20558065; PubMed=11104663; DOI=10.1042/0264-6021:3520601; RA Oklu R., Hesketh R.; RT "The latent transforming growth factor beta binding protein (LTBP) RT family."; RL Biochem. J. 352:601-610(2000). CC -!- FUNCTION: May be involved in the assembly, secretion and targeting CC of TGFB1 to sites at which it is stored and/or activated. May play CC critical roles in controlling and directing the activity of TGFB1. CC May have a structural role in the extra cellular matrix (ECM). CC -!- SUBUNIT: The large latent complex of TGFB1 from platelets is CC composed of the TGFB1 molecule non-covalently associated with a CC disulfide-bonded complex of a dimer of the N-terminal propeptide CC of the TGFB1 precursor and LTBP1. LTBP1 does not bind directly to CC active TGFB1. Binds to FBN1 and FBN2. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- DOMAIN: Associates covalently with small latent TGF-beta complex CC via Repeat C (By similarity). CC -!- SIMILARITY: Belongs to the LTBP family. CC -!- SIMILARITY: Contains 18 EGF-like domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M55431; AAA42235.1; -; mRNA. DR PIR; A38261; A38261. DR UniGene; Rn.40942; -. DR HSSP; P08709; 1BF9. DR SMR; Q00918; 1332-1403. DR Ensembl; ENSRNOG00000033090; Rattus norvegicus. DR RGD; 68379; Ltbp1. DR ArrayExpress; Q00918; -. DR InterPro; IPR000152; Asx_hydroxyl_S. DR InterPro; IPR006210; EGF. DR InterPro; IPR000742; EGF_3. DR InterPro; IPR001881; EGF_Ca_bd. DR InterPro; IPR013091; EGF_Ca_bd_2. DR InterPro; IPR006209; EGF_like. DR InterPro; IPR013032; EGF_like_reg. DR InterPro; IPR002212; Fibril-assoc. DR Pfam; PF00008; EGF; 5. DR Pfam; PF07645; EGF_CA; 12. DR Pfam; PF00683; TB; 4. DR SMART; SM00181; EGF; 18. DR SMART; SM00179; EGF_CA; 13. DR PROSITE; PS00010; ASX_HYDROXYL; 13. DR PROSITE; PS00022; EGF_1; 2. DR PROSITE; PS01186; EGF_2; 10. DR PROSITE; PS50026; EGF_3; 14. DR PROSITE; PS01187; EGF_CA; 15. KW Direct protein sequencing; EGF-like domain; Glycoprotein; KW Growth factor binding; Hydroxylation; Repeat; Signal. FT SIGNAL 1 20 Potential. FT PROPEP 21 736 Potential. FT /FTId=PRO_0000007639. FT CHAIN 737 1577 Latent-transforming growth factor beta- FT binding protein 1. FT /FTId=PRO_0000007640. FT PROPEP 1578 1712 Potential. FT /FTId=PRO_0000007641. FT DOMAIN 181 213 EGF-like 1. FT DOMAIN 391 423 EGF-like 2. FT REPEAT 551 604 Repeat A. FT DOMAIN 618 658 EGF-like 3; calcium-binding (Potential). FT REPEAT 671 721 Repeat B. FT DOMAIN 865 906 EGF-like 4; calcium-binding (Potential). FT DOMAIN 907 948 EGF-like 5; calcium-binding (Potential). FT DOMAIN 949 989 EGF-like 6; calcium-binding (Potential). FT DOMAIN 990 1029 EGF-like 7; calcium-binding (Potential). FT DOMAIN 1030 1070 EGF-like 8; calcium-binding (Potential). FT DOMAIN 1071 1111 EGF-like 9; calcium-binding (Potential). FT DOMAIN 1112 1152 EGF-like 10; calcium-binding (Potential). FT DOMAIN 1153 1193 EGF-like 11; calcium-binding (Potential). FT DOMAIN 1194 1235 EGF-like 12; calcium-binding (Potential). FT DOMAIN 1236 1277 EGF-like 13; calcium-binding (Potential). FT DOMAIN 1278 1320 EGF-like 14; calcium-binding (Potential). FT REPEAT 1340 1392 Repeat C. FT DOMAIN 1415 1457 EGF-like 15; calcium-binding (Potential). FT DOMAIN 1458 1498 EGF-like 16; calcium-binding (Potential). FT REPEAT 1517 1568 Repeat D. FT DOMAIN 1612 1652 EGF-like 17. FT DOMAIN 1653 1697 EGF-like 18; calcium-binding (Potential). FT SITE 734 736 Cleavage (Potential). FT SITE 1575 1577 Cleavage (Potential). FT CARBOHYD 339 339 N-linked (GlcNAc...) (Potential). FT CARBOHYD 370 370 N-linked (GlcNAc...) (Potential). FT CARBOHYD 416 416 N-linked (GlcNAc...) (Potential). FT CARBOHYD 612 612 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1042 1042 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1242 1242 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1357 1357 N-linked (GlcNAc...) (Potential). FT DISULFID 185 195 By similarity. FT DISULFID 189 201 By similarity. FT DISULFID 203 212 By similarity. FT DISULFID 395 405 By similarity. FT DISULFID 399 411 By similarity. FT DISULFID 413 422 By similarity. FT DISULFID 622 633 By similarity. FT DISULFID 628 642 By similarity. FT DISULFID 644 657 By similarity. FT DISULFID 869 881 By similarity. FT DISULFID 876 890 By similarity. FT DISULFID 892 905 By similarity. FT DISULFID 911 923 By similarity. FT DISULFID 918 932 By similarity. FT DISULFID 934 947 By similarity. FT DISULFID 953 964 By similarity. FT DISULFID 959 973 By similarity. FT DISULFID 976 988 By similarity. FT DISULFID 994 1005 By similarity. FT DISULFID 1000 1014 By similarity. FT DISULFID 1017 1028 By similarity. FT DISULFID 1034 1045 By similarity. FT DISULFID 1040 1054 By similarity. FT DISULFID 1056 1069 By similarity. FT DISULFID 1075 1086 By similarity. FT DISULFID 1081 1095 By similarity. FT DISULFID 1097 1110 By similarity. FT DISULFID 1116 1127 By similarity. FT DISULFID 1122 1136 By similarity. FT DISULFID 1138 1151 By similarity. FT DISULFID 1157 1169 By similarity. FT DISULFID 1164 1178 By similarity. FT DISULFID 1180 1192 By similarity. FT DISULFID 1198 1210 By similarity. FT DISULFID 1204 1219 By similarity. FT DISULFID 1221 1234 By similarity. FT DISULFID 1240 1252 By similarity. FT DISULFID 1246 1261 By similarity. FT DISULFID 1263 1276 By similarity. FT DISULFID 1282 1294 By similarity. FT DISULFID 1289 1303 By similarity. FT DISULFID 1305 1319 By similarity. FT DISULFID 1419 1432 By similarity. FT DISULFID 1427 1441 By similarity. FT DISULFID 1443 1456 By similarity. FT DISULFID 1462 1473 By similarity. FT DISULFID 1468 1482 By similarity. FT DISULFID 1484 1497 By similarity. FT DISULFID 1616 1627 By similarity. FT DISULFID 1622 1636 By similarity. FT DISULFID 1638 1651 By similarity. FT DISULFID 1657 1672 By similarity. FT DISULFID 1667 1681 By similarity. FT DISULFID 1683 1696 By similarity. SQ SEQUENCE 1712 AA; 186599 MW; 650BCEAA691FD134 CRC64; MAGAWLRWGL LLWAGLLAWS AHGRVRRITY VVRPGPGLPA GTLPLAGPPR TFNVALDARY SRSSTATSSR SLAGPPAERT RRTSQPGGAA LPGLRSPLPP EPARPGAPSR QLHSKAGAQT AVTRFAKHGR QVVRSKVQQD TQSSGGSRLQ VQQKQQLQGI NVCGGQCCHG WSKAPGSQRC TKPSCVPPCQ NGGMCLRPQF CVCKPGTKGK ACEITAAQDT MSPVFGGQNP GSSWVPPEPA AKRTSTKKAD TLPRVSPVAQ MTLTLKPKPS MGLSQQIHSQ VAPLSSQNVM IRHGQTQEYV LKPKYFPAPK VVSGEQSTEG SFSLRYGQEQ GTAPFQVSNH TGRIKVVFTP SICKVTCTKG NCHNSCQKGN TTTLISENGH AADTLTATNF RVVICHLPCM NGGQCSSRDK CQCPPNFTGK LCQIPVLGAS MPKLYQHAQQ PGKALGSHVI HSTHTLPLTM TNQQGVKVKF PPNIVNIHVK HPPEASVQIH QVSRIDGPVG QRVKEVQPGQ SQVSYQGLPV QKTQTVHSTY SHQQVIPHVY PVAAKTQLGR CFQETIGSQC GKALPGLSKQ EDCCGTVGTS WGFNKCQKCP KKQSYHGYTQ MMECLQGYKR VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCSCKMGFGP DPTFSSCVPD PPMISEEKGP CYRLVSPGRQ CMHPLSVHLT KQICCCSVGK AWGPQCEKCP LPGTAAFKEI CPGGMGYTVS GIHRRRPIHQ HIGKEAVFVK PKNTQPVAKS THPPPLPAKE EPVEALTSSR EHGPGVAEPE VVTAPPEKEI PSLDQEKTRL EPGQPQLSPG VSTIHLHPQF PVVVEKTSPP VPVEVAPEGS TSSASQVIAP TQVTEINECT VNPDICGAGH CINLPVRYTC ICYEGYKFSE QQRKCIDIDE CAQAQHLCSQ GRCENTEGSF LCICPAGFIA SEEGSNCIDV DECLRPDVCR DGRCINTAGA FRCEYCDSGY RMSRRGHCED IDECLTPSTC PEEQCVNSPG SYQCVPCTEG FRGWNGQCLD VDECLQPKVC TNGSCTNLEG SYMCSCHKGY SPTPDHRHCQ DIDECQQGNL CMNGQCKNTD GSFRCTCGQG YQLSAAKDQC EDIDECEHRH LCSHGQCRNT EGSFQCLCNQ GYRASVLGDH CEDINECLED SSVCQGGDCI NTAGSYDCTC PDGLQLNDNK GCQDINECAQ PGLCAPHGEC LNTQGSFHCV CEQGFSISAD GRTCEDIDEC VNNTVCDSHG FCDNTAGSFR CLCYQGFQAP QDGQGCVDVN ECELLSGVCG EAFCENVEGS FLCVCADENQ EYSPMTGQCR SRATEDSGVD RQPKEEKKEC YYNLNDASLC DNVLAPNVTK QECCCTSGAG WGDNCEIFPC PVQGTAEFSE MCPRGKGFVP AGESSYETGG ENYKDADECL LFGEEICKNG YCLNTQPGYE CYCKEGTYYD PVKLQCFDMD ECQDPNSCID GQCVNTEGSY NCFCTHPMVL DASEKRCVQP TESNEQIEET DVYQDLCWEH LSEEYVCSRP LVGKQTTYTE CCCLYGEAWG MQCALCPMKD SDDYAQLCNI PVTGRRRPYG RDALVDFSEQ YGPETDPYFI QDRFLNSFEE LQAEECGILN GCENGRCVRV QEGYTCDCFD GYHLDMAKMT CVDVNECSEL NNRMSLCKNA KCINTEGSYK CVCLPGYVPS DKPNYCTPLN TALNLDKDSD LE // ID M3K7_DROME STANDARD; PRT; 678 AA. AC Q9V3Q6; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 19-SEP-2006, entry version 41. DE Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (TGF- DE beta-activated kinase 1) (dTAK1). GN Name=Tak1; ORFNames=CG18492; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Ovary; RX MEDLINE=20221548; PubMed=10757786; RX DOI=10.1128/MCB.20.9.3015-3026.2000; RA Takatsu Y., Nakamura M., Stapleton M., Danos M.C., Matsumoto K., RA O'Connor M.B., Shibuya H., Ueno N.; RT "TAK1 participates in c-Jun N-terminal kinase signaling during RT Drosophila development."; RL Mol. Cell. Biol. 20:3015-3026(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [5] RP FUNCTION. RX PubMed=14519762; DOI=10.1074/jbc.M304802200; RA Silverman N., Zhou R., Erlich R.L., Hunter M., Bernstein E., RA Schneider D., Maniatis T.; RT "Immune activation of NF-kappaB and JNK requires Drosophila TAK1."; RL J. Biol. Chem. 278:48928-48934(2003). RN [6] RP FUNCTION. RX PubMed=15037551; DOI=10.1101/gad.1168104; RA Park J.M., Brady H., Ruocco M.G., Sun H., Williams D., Lee S.J., RA Kato T. Jr., Richards N., Chan K., Mercurio F., Karin M., RA Wasserman S.A.; RT "Targeting of TAK1 by the NF-kappa B protein Relish regulates the JNK- RT mediated immune response in Drosophila."; RL Genes Dev. 18:584-594(2004). CC -!- FUNCTION: Component of a protein kinase signal transduction CC cascade. Mediator of TGF-beta signal transduction. Responsible for CC activation of the JNK MAPK pathway (basket, bsk and hemipterous, CC hep) in response to LPS. Component of the NF-kappa-B pathway; CC relish-mediated JNK inhibition involves proteasomal degradation of CC Tak1; certain targets of Relish that are induced during immune CC responses may facilitate destruction of Tak1 and switch off the CC JNK cascade. Participates in diverse roles such as control of cell CC shape and regulation of apoptosis. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- COFACTOR: Magnesium (By similarity). CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. MAP CC kinase kinase kinase subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF199466; AAF06815.1; -; mRNA. DR EMBL; AE003571; AAF50895.1; -; Genomic_DNA. DR EMBL; AY051953; AAK93377.1; -; mRNA. DR UniGene; Dm.6425; -. DR HSSP; Q62838; 1LUF. DR Ensembl; CG18492; Drosophila melanogaster. DR KEGG; dme:CG18492-PA; -. DR FlyBase; FBgn0026323; Tak1. DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IMP. DR GO; GO:0007256; P:activation of JNKK activity; IMP. DR GO; GO:0006963; P:antibacterial polypeptide induction; TAS. DR GO; GO:0006915; P:apoptosis; IGI. DR GO; GO:0007391; P:dorsal closure; IMP. DR GO; GO:0007456; P:eye development (sensu Endopterygota); IMP. DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; IMP. DR GO; GO:0006955; P:immune response; IMP. DR GO; GO:0007477; P:notum development; IMP. DR GO; GO:0016318; P:ommatidial rotation; IMP. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW ATP-binding; Complete proteome; Immune response; Innate immunity; KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 678 Mitogen-activated protein kinase kinase FT kinase 7. FT /FTId=PRO_0000086254. FT DOMAIN 19 271 Protein kinase. FT NP_BIND 25 33 ATP (By similarity). FT COMPBIAS 621 644 His-rich. FT ACT_SITE 140 140 Proton acceptor (By similarity). FT BINDING 46 46 ATP (By similarity). SQ SEQUENCE 678 AA; 75675 MW; 87EBA80CDB8CDE45 CRC64; MATASLDALQ AAYVDFSEIT LREKVGHGSY GVVCKAVWRD KLVAVKEFFA SAEQKDIEKE VKQLSRVKHP NIIALHGISS YQQATYLIME FAEGGSLHNF LHGKVKPAYS LAHAMSWARQ CAEGLAYLHA MTPKPLIHRD VKPLNLLLTN KGRNLKICDF GTVADKSTMM TNNRGSAAWM APEVFEGSKY TEKCDIFSWA IVLWEVLSRK QPFKGIDNAY TIQWKIYKGE RPPLLTTCPK RIEDLMTACW KTVPEDRPSM QYIVGVMHEI VKDYTGADKA LEYTFVNQQI VTKESDGTVA AQPDSLSSQE GELSPSSTQL TPTTAANANV NAIAISKTTT SSMTENTSST SSDITPTNSG QLDNNPLFYM VTNRWDAIPE EESNESRNDS FNLTSSAEAT QRLETIRNGM ILMACKPMEQ LTLDVEANGF DLSPSESSSS STNAKSDGRE RLTVTDTKPV MMTTDLSNNN GGIHAHSNGL LSHANGWQAR DEELQEQEHE QEIVNSLDVD VDPDEDENDG TEQSLAEILD PELQPEPPIP NDAESQLIYR DHRHMAKEYL SVDTNLYYAQ DFKDKLIVQM DRTEREQKQE LLRKMKDKEG LQSLYNNLQQ QYASRQLAAG HHPQPHPHPH PNQLQHPHSH PPMHFLQDEG CGLLPGSVCG GSESVEEGWV VIPPHHNA // ID M3K7_HUMAN STANDARD; PRT; 606 AA. AC O43318; O43317; O43319; Q5TDN2; Q5TDN3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 03-OCT-2006, entry version 68. DE Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) DE (Transforming growth factor-beta-activated kinase 1) (TGF-beta- DE activated kinase 1). GN Name=MAP3K7; Synonyms=TAK1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C). RC TISSUE=Lung; RX MEDLINE=98153801; PubMed=9480845; DOI=10.1006/bbrc.1998.8124; RA Sakurai H., Shigemori N., Hasegawa K., Sugita T.; RT "TGF-beta-activated kinase 1 stimulates NF-kappa B activation by an RT NF-kappa B-inducing kinase-independent mechanism."; RL Biochem. Biophys. Res. Commun. 243:545-549(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RSnG); RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A). RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH MAP3K7IP1. RX MEDLINE=96216294; PubMed=8638164; RA Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., RA Ueno N., Irie K., Nishida E., Matsumoto K.; RT "TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal RT transduction."; RL Science 272:1179-1182(1996). RN [6] RP INTERACTION WITH PELI1 AND PELI2. RX MEDLINE=22689054; PubMed=12804775; DOI=10.1016/S0014-5793(03)00533-7; RA Jensen L.E., Whitehead A.S.; RT "Pellino2 activates the mitogen activated protein kinase pathway."; RL FEBS Lett. 545:199-202(2003). RN [7] RP INTERACTION WITH PELI3. RX MEDLINE=22756745; PubMed=12874243; RA Jensen L.E., Whitehead A.S.; RT "Pellino3, a novel member of the Pellino protein family, promotes RT activation of c-Jun and Elk-1 and may act as a scaffolding protein."; RL J. Immunol. 171:1500-1506(2003). RN [8] RP FUNCTION, INTERACTION WITH SMAD7; MAP2K3 AND P38 KINASE, AND RP MUTAGENESIS OF LYS-63. RX MEDLINE=22477345; PubMed=12589052; DOI=10.1091/mbc.02-03-0037; RA Edlund S., Bu S., Schuster N., Aspenstrom P., Heuchel R., Heldin N.E., RA ten Dijke P., Heldin C.H., Landstrom M.; RT "Transforming growth factor-beta1 (TGF-beta)-induced apoptosis of RT prostate cancer cells involves Smad7-dependent activation of p38 by RT TGF-beta-activated kinase 1 and mitogen-activated protein kinase RT kinase 3."; RL Mol. Biol. Cell 14:529-544(2003). CC -!- FUNCTION: Component of a protein kinase signal transduction CC cascade. Mediator of TGF-beta signal transduction. Stimulates NF- CC kappa-B activation and the p38 MAPK pathway. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- COFACTOR: Magnesium. CC -!- SUBUNIT: Binds both upstream activators and downstream substrates CC in multimolecular complexes. Interacts with MAP3K7IP1 and CC MAP3K7IP2. Interacts with PPM1L. CC -!- INTERACTION: CC O95163:IKBKAP; NbExp=1; IntAct=EBI-358684, EBI-347559; CC Q99558:MAP3K14; NbExp=1; IntAct=EBI-358704, EBI-358011; CC Q8N2H9-1:MGC35521; NbExp=1; IntAct=EBI-358684, EBI-448466; CC Q8N2H9-2:MGC35521; NbExp=1; IntAct=EBI-358684, EBI-448472; CC P40763:STAT3; NbExp=1; IntAct=EBI-358684, EBI-518675; CC P42227:Stat3 (xeno); NbExp=1; IntAct=EBI-358684, EBI-602878; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1B; CC IsoId=O43318-1; Sequence=Displayed; CC Name=1A; CC IsoId=O43318-2; Sequence=VSP_004886; CC Name=1C; CC IsoId=O43318-3; Sequence=VSP_004887, VSP_004888; CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. MAP CC kinase kinase kinase subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB009357; BAA25026.1; -; mRNA. DR EMBL; AB009356; BAA25025.1; -; mRNA. DR EMBL; AB009358; BAA25027.2; -; mRNA. DR EMBL; DQ314875; ABC40734.1; -; Genomic_DNA. DR EMBL; AL121964; CAI19611.1; -; Genomic_DNA. DR EMBL; AL121837; CAI19611.1; JOINED; Genomic_DNA. DR EMBL; AL121964; CAI19612.1; -; Genomic_DNA. DR EMBL; AL121837; CAI19612.1; JOINED; Genomic_DNA. DR EMBL; AL121837; CAI23532.1; -; Genomic_DNA. DR EMBL; AL121964; CAI23532.1; JOINED; Genomic_DNA. DR EMBL; AL121837; CAI23533.1; -; Genomic_DNA. DR EMBL; AL121964; CAI23533.1; JOINED; Genomic_DNA. DR EMBL; BC017715; AAH17715.1; -; mRNA. DR PIR; JC5955; JC5955. DR PIR; JC5956; JC5956. DR UniGene; Hs.590889; -. DR PDB; 2EVA; X-ray; A=31-328. DR IntAct; O43318; -. DR Ensembl; ENSG00000135341; Homo sapiens. DR KEGG; hsa:6885; -. DR H-InvDB; HIX0006075; -. DR HGNC; HGNC:6859; MAP3K7. DR MIM; 602614; gene. DR ArrayExpress; O43318; -. DR GO; GO:0004709; F:MAP kinase kinase kinase activity; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0007179; P:transforming growth factor beta receptor si...; TAS. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW 3D-structure; Alternative splicing; ATP-binding; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1 606 Mitogen-activated protein kinase kinase FT kinase 7. FT /FTId=PRO_0000086252. FT DOMAIN 36 291 Protein kinase. FT NP_BIND 42 50 ATP (By similarity). FT COMPBIAS 8 14 Poly-Ser. FT ACT_SITE 156 156 Proton acceptor (By similarity). FT BINDING 63 63 ATP. FT VAR_SEQ 404 430 Missing (in isoform 1A). FT /FTId=VSP_004886. FT VAR_SEQ 509 518 PLAPCPNSKE -> ARTSCRTGPG (in isoform 1C). FT /FTId=VSP_004887. FT VAR_SEQ 519 606 Missing (in isoform 1C). FT /FTId=VSP_004888. FT MUTAGEN 63 63 K->W: Loss of kinase activity. SQ SEQUENCE 606 AA; 67196 MW; 3D8F8147CD174013 CRC64; MSTASAASSS SSSSAGEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIA ATTAYSKPKR GHRKTASFGN ILDVPEIVIS GNGQPRRRSI QDLTVTGTEP GQVSSRSSSP SVRMITTSGP TSEKPTRSHP WTPDDSTDTN GSDNSIPMAY LTLDHQLQPL APCPNSKESM AVFEQHCKMA QEYMKVQTEI ALLLQRKQEL VAELDQDEKD QQNTSRLVQE HKKLLDENKS LSTYYQQCKK QLEVIRSQQQ KRQGTS // ID M3K7_MOUSE STANDARD; PRT; 579 AA. AC Q62073; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 19-SEP-2006, entry version 55. DE Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) DE (Transforming growth factor-beta-activated kinase 1) (TGF-beta- DE activated kinase 1). GN Name=Map3k7; Synonyms=Tak1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RX MEDLINE=96123277; PubMed=8533096; RA Yamaguchi K., Shirakabe K., Shibuya H., Irie K., Ohishi I., Ueno N., RA Taniguchi T., Nishida E., Matsumoto K.; RT "Identification of a member of the MAPKKK family as a potential RT mediator of TGF-beta signal transduction."; RL Science 270:2008-2011(1995). RN [2] RP INTERACTION WITH PPM1L. RX MEDLINE=22552457; PubMed=12556533; DOI=10.1074/jbc.M211474200; RA Li M.G., Katsura K., Nomiyama H., Komaki K., Ninomiya-Tsuji J., RA Matsumoto K., Kobayashi T., Tamura S.; RT "Regulation of the interleukin-1-induced signaling pathways by a novel RT member of the protein phosphatase 2C family (PP2Cepsilon)."; RL J. Biol. Chem. 278:12013-12021(2003). CC -!- FUNCTION: Component of a protein kinase signal transduction CC cascade. Mediator of TGF-beta signal transduction. Stimulates NF- CC kappa-B activation and the p38 MAPK pathway. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- COFACTOR: Magnesium. CC -!- SUBUNIT: Binds both upstream activators and downstream substrates CC in multimolecular complexes. Interacts with MAP3K7IP1 and CC MAP3K7IP2 (By similarity). Interacts with PPM1L. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. MAP CC kinase kinase kinase subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D76446; BAA11184.1; -; mRNA. DR UniGene; Mm.258589; -. DR UniGene; Mm.392292; -. DR HSSP; P36897; 1IAS. DR Ensembl; ENSMUSG00000028284; Mus musculus. DR KEGG; mmu:26409; -. DR MGI; MGI:1346877; Map3k7. DR ArrayExpress; Q62073; -. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0001525; P:angiogenesis; IMP. DR GO; GO:0007252; P:I-kappaB phosphorylation; IGI. DR GO; GO:0000165; P:MAPKKK cascade; IDA. DR GO; GO:0043066; P:negative regulation of apoptosis; IGI. DR GO; GO:0001841; P:neural tube formation; IMP. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-k...; IGI. DR GO; GO:0046330; P:positive regulation of JNK cascade; IGI. DR GO; GO:0007179; P:transforming growth factor beta receptor si...; IMP. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR001245; Tyr_pkinase. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 579 Mitogen-activated protein kinase kinase FT kinase 7. FT /FTId=PRO_0000086253. FT DOMAIN 36 291 Protein kinase. FT NP_BIND 42 50 ATP (By similarity). FT COMPBIAS 8 16 Poly-Ser. FT ACT_SITE 156 156 Proton acceptor (By similarity). FT BINDING 63 63 ATP (By similarity). SQ SEQUENCE 579 AA; 64228 MW; 97C8F6F3C8E283EE CRC64; MSTASAASSS SSSSASEMIE APSQVLNFEE IDYKEIEVEE VVGRGAFGVV CKAKWRAKDV AIKQIESESE RKAFIVELRQ LSRVNHPNIV KLYGACLNPV CLVMEYAEGG SLYNVLHGAE PLPYYTAAHA MSWCLQCSQG VAYLHSMQPK ALIHRDLKPP NLLLVAGGTV LKICDFGTAC DIQTHMTNNK GSAAWMAPEV FEGSNYSEKC DVFSWGIILW EVITRRKPFD EIGGPAFRIM WAVHNGTRPP LIKNLPKPIE SLMTRCWSKD PSQRPSMEEI VKIMTHLMRY FPGADEPLQY PCQYSDEGQS NSATSTGSFM DIASTNTSNK SDTNMEQVPA TNDTIKRLES KLLKNQAKQQ SESGRLSLGA SRGSSVESLP PTSEGKRMSA DMSEIEARIV ATAGNGQPRR RSIQDLTVTG TEPGQVSSRS SSPSVRMITT SGPTSEKPAR SHPWTPDDST DTNGSDNSIP MAYLTLDHQL QPLAPCPNSK ESMAVFEQHC KMAQEYMKVQ TEIALLLQRK QELVAELDQD EKDQQNTSRL VQEHKKLLDE NKSLSTYYQQ CKKQLEVIRS QQQKRQGTS // ID PP16B_BOVIN STANDARD; PRT; 568 AA. AC Q95N27; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-SEP-2006, entry version 31. DE Protein phosphatase 1 regulatory inhibitor subunit 16B (TGF-beta- DE inhibited membrane-associated protein) (bTIMAP) (CAAX box protein DE TIMAP). GN Name=PPP1R16B; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=22049828; PubMed=12055102; DOI=10.1152/ajpcell.00442.2001; RA Cao W., Mattagajasingh S.N., Xu H., Kim K., Fierlbeck W., Deng J., RA Lowenstein C.J., Ballermann B.J.; RT "TIMAP, a novel CAAX box protein regulated by TGF-beta1 and expressed RT in endothelial cells."; RL Am. J. Physiol. 283:C327-C337(2002). CC -!- FUNCTION: May be a downstream target for TGF-beta1 signaling CC cascade in endothelial cells. CC -!- SUBUNIT: Binds PP1 (Probable). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor (Potential). CC -!- INDUCTION: Inhibited by TGF-beta1. CC -!- SIMILARITY: Contains 5 ANK repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF362909; AAK52795.1; -; mRNA. DR UniGene; Bt.8543; -. DR HSSP; P09959; 1SW6. DR KEGG; bta:282091; -. DR GO; GO:0005886; C:plasma membrane; ISS. DR GO; GO:0019903; F:protein phosphatase binding; ISS. DR GO; GO:0007165; P:signal transduction; ISS. DR InterPro; IPR002110; ANK. DR Pfam; PF00023; Ank; 5. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 4. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. KW ANK repeat; Coiled coil; Lipoprotein; Membrane; Prenylation; Repeat. FT CHAIN 1 568 Protein phosphatase 1 regulatory FT inhibitor subunit 16B. FT /FTId=PRO_0000067042. FT REPEAT 100 129 ANK 1. FT REPEAT 133 162 ANK 2. FT REPEAT 228 257 ANK 3. FT REPEAT 261 290 ANK 4. FT REPEAT 531 560 ANK 5. FT COILED 15 55 Potential. FT LIPID 565 565 S-farnesyl cysteine (Potential). SQ SEQUENCE 568 AA; 63643 MW; 61C10899462B0334 CRC64; MASHVDLLTE LQLLEKVPTL ERLRAAQKRR AQQLKKWAQY EQDLQHRKRK HERKRSTGGR RKKVSFEASV ALLEASLRND AEEVRYFLKN KVSPDLCNED GLTALHQCCI DNFEEIVKLL LSHGANVNAK DNELWTPLHA AATCGHINLV KILVQYGADL LAVNSDGNMP YDLCEDEPTL DVIETCMAYQ GITQEKINEM RAAPEQQMIS DIHCMIAAGQ DLDWVDAQGA TLLHIAGANG YLRAAELLLD HGVRVDVKDW DGWEPLHAAA FWGQMQMAEL LVSHGASLSA RTSMDEMPID LCEEEEFKVL LLELKHKHDV IMKSQLRHKS SLSRRTSSAG SRGKVVRRAS LSDRTNLYRK EYEGEAILWQ QRSASEDQRN STYNGDIRET RTDQENKDPN PRLEKPVLLS EFPTKIPHSD MDMPVENGLR APVSTYQYAL CNGDVWKVHE VPDYSMAYGN PGVADATPSW SGYKEQSPQT LLELKRQRAA AKLLSHPFLS THLGSGVSRT GEGSSEGKAP LIGGRTSPYS SNGTSVYYTV TSGDPPLLKF KAPIEEMEEK VHGCCRIS // ID PP16B_HUMAN STANDARD; PRT; 567 AA. AC Q96T49; O94912; Q9NQG4; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 19-SEP-2006, entry version 40. DE Protein phosphatase 1 regulatory inhibitor subunit 16B (TGF-beta- DE inhibited membrane-associated protein) (hTIMAP) (CAAX box protein DE TIMAP) (Ankyrin repeat domain protein 4). GN Name=PPP1R16B; Synonyms=ANKRD4, KIAA0823; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=22049828; PubMed=12055102; DOI=10.1152/ajpcell.00442.2001; RA Cao W., Mattagajasingh S.N., Xu H., Kim K., Fierlbeck W., Deng J., RA Lowenstein C.J., Ballermann B.J.; RT "TIMAP, a novel CAAX box protein regulated by TGF-beta1 and expressed RT in endothelial cells."; RL Am. J. Physiol. 283:C327-C337(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=99156230; PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP SEQUENCE REVISION. RX MEDLINE=22158633; PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). CC -!- FUNCTION: May be a downstream target for TGF-beta1 signaling CC cascade in endothelial cells. CC -!- SUBUNIT: Binds PP1 (Probable). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor (Potential). CC -!- TISSUE SPECIFICITY: Highly expressed in vascular endothelium, CNS, CC lung, spleen, kidney and testis. CC -!- INDUCTION: Inhibited by TGF-beta1. CC -!- SIMILARITY: Contains 5 ANK repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF362910; AAK52796.1; -; mRNA. DR EMBL; AB020630; BAA74846.2; ALT_INIT; mRNA. DR EMBL; AL031657; CAI20058.1; -; Genomic_DNA. DR EMBL; AL121889; CAI20058.1; JOINED; Genomic_DNA. DR EMBL; AL121889; CAI19080.1; -; Genomic_DNA. DR EMBL; AL031657; CAI19080.1; JOINED; Genomic_DNA. DR UniGene; Hs.45719; -. DR HSSP; P09959; 1SW6. DR Ensembl; ENSG00000101445; Homo sapiens. DR KEGG; hsa:26051; -. DR H-InvDB; HIX0015811; -. DR HGNC; HGNC:15850; PPP1R16B. DR ArrayExpress; Q96T49; -. DR RZPD-ProtExp; IOH37988; -. DR RZPD-ProtExp; W1225; -. DR GO; GO:0005886; C:plasma membrane; NAS. DR GO; GO:0019903; F:protein phosphatase binding; NAS. DR GO; GO:0007165; P:signal transduction; NAS. DR InterPro; IPR002110; ANK. DR Pfam; PF00023; Ank; 5. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 4. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. KW ANK repeat; Coiled coil; Lipoprotein; Membrane; Prenylation; Repeat. FT CHAIN 1 567 Protein phosphatase 1 regulatory FT inhibitor subunit 16B. FT /FTId=PRO_0000067043. FT REPEAT 100 129 ANK 1. FT REPEAT 133 162 ANK 2. FT REPEAT 228 257 ANK 3. FT REPEAT 261 290 ANK 4. FT REPEAT 530 559 ANK 5. FT COILED 15 55 Potential. FT LIPID 564 564 S-farnesyl cysteine (Potential). SQ SEQUENCE 567 AA; 63551 MW; 8418CE26D0035CF1 CRC64; MASHVDLLTE LQLLEKVPTL ERLRAAQKRR AQQLKKWAQY EQDLQHRKRK HERKRSTGGR RKKVSFEASV ALLEASLRND AEEVRYFLKN KVSPDLCNED GLTALHQCCI DNFEEIVKLL LSHGANVNAK DNELWTPLHA AATCGHINLV KILVQYGADL LAVNSDGNMP YDLCEDEPTL DVIETCMAYQ GITQEKINEM RVAPEQQMIA DIHCMIAAGQ DLDWIDAQGA TLLHIAGANG YLRAAELLLD HGVRVDVKDW DGWEPLHAAA FWGQMQMAEL LVSHGASLSA RTSMDEMPID LCEEEEFKVL LLELKHKHDV IMKSQLRHKS SLSRRTSSAG SRGKVVRRAS LSDRTNLYRK EYEGEAILWQ RSAAEDQRTS TYNGDIRETR TDQENKDPNP RLEKPVLLSE FPTKIPRGEL DMPVENGLRA PVSAYQYALA NGDVWKVHEV PDYSMAYGNP GVADATPPWS SYKEQSPQTL LELKRQRAAA KLLSHPFLST HLGSSMARTG ESSSEGKAPL IGGRTSPYSS NGTSVYYTVT SGDPPLLKFK APIEEMEEKV HGCCRIS // ID PP16B_MOUSE STANDARD; PRT; 568 AA. AC Q8VHQ3; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 03-OCT-2006, entry version 37. DE Protein phosphatase 1 regulatory inhibitor subunit 16B (TGF-beta- DE inhibited membrane-associated protein) (CAAX box protein TIMAP). GN Name=Ppp1r16b; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/c; TISSUE=Cerebellum; RX MEDLINE=22525552; PubMed=12638124; DOI=10.1016/S1567-133X(02)00010-8; RA Magdaleno S., Northcutt G.M., Curran T., Kurschner C.; RT "mPPP1R16B is a novel mouse protein phosphatase 1 targeting subunit RT whose mRNA is located in cell bodies and dendrites of neurons in four RT distinct regions of the brain."; RL Gene Expr. Patterns 1:143-149(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: May be a downstream target for TGF-beta1 signaling CC cascade in endothelial cells (By similarity). CC -!- SUBUNIT: Binds PP1 (Probable). CC -!- SUBCELLULAR LOCATION: Cell membrane; lipid-anchor (By similarity). CC -!- MISCELLANEOUS: Repressed by TGF-beta1 which requires denovo CC protein synthesis and histone deacetylase (By similarity). CC -!- SIMILARITY: Contains 5 ANK repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF423761; AAL62093.1; -; mRNA. DR EMBL; BC054764; AAH54764.1; -; mRNA. DR EMBL; BC057542; AAH57542.1; -; mRNA. DR UniGene; Mm.150540; -. DR UniGene; Mm.392660; -. DR HSSP; P09959; 1SW6. DR Ensembl; ENSMUSG00000037754; Mus musculus. DR MGI; MGI:2151841; Ppp1r16b. DR ArrayExpress; Q8VHQ3; -. DR GO; GO:0005886; C:plasma membrane; ISS. DR GO; GO:0019903; F:protein phosphatase binding; ISS. DR GO; GO:0007165; P:signal transduction; ISS. DR InterPro; IPR002110; ANK. DR Pfam; PF00023; Ank; 5. DR PRINTS; PR01415; ANKYRIN. DR SMART; SM00248; ANK; 4. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 4. KW ANK repeat; Coiled coil; Lipoprotein; Membrane; Prenylation; Repeat. FT CHAIN 1 568 Protein phosphatase 1 regulatory FT inhibitor subunit 16B. FT /FTId=PRO_0000067044. FT REPEAT 100 129 ANK 1. FT REPEAT 133 162 ANK 2. FT REPEAT 228 257 ANK 3. FT REPEAT 261 290 ANK 4. FT REPEAT 531 560 ANK 5. FT COILED 15 55 Potential. FT LIPID 565 565 S-farnesyl cysteine (Potential). SQ SEQUENCE 568 AA; 63571 MW; 5D8446C81DEBA3D1 CRC64; MASHVDLLTE LQLLEKVPTL ERLRAAQKRR AQQLKKWAQY EQDLLHRKRK HERKRSTGGR RKKVSFEASV ALLEASLRND AEEVRYFLKN KVSPDLCNED GLTALHQCCI DNFEEIVKLL LSHGANVNAK DNELWTPLHA AATCGHINLV KILVQYGADL LAVNSDGNMP YDLCEDEPTL DVIETCMAYQ GITQEKINEM RAAPEQKMIS DIHCMIAAGQ DLDWIDGQGA TLLHIAGANG YLRAAELLLD HGVRVDVKDW DGWEPLHAAA FWGQMPMAEL LVSHGASLSA RTSMDEMPID LCEEEEFKVL LLELKHKHDV IMKSQLRHKS SLSRRTSSAG SRGKVVRRAS LSDRTNLYRK EYEGEAILWQ QRSAAEDQRT STYNGDIRET RTDQENKDPN PRLEKPVLLS EFSTKISRGE LDGPVENGLR APVSTYQYAL ANGDIWKMHE MPDYSMAYGN PGVADVPPPW SGFKEQSPQT LLELKRQRAA AKLLSHPFLS THLGSSVARS GESSSEGKAP LIGGRTSPYS SNGTSVYYTV TSGDPPLLKF KAPMEEMEEK VHGCCRIS // ID SPB10_RAT STANDARD; PRT; 397 AA. AC Q8K3K4; Q6P7C1; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 03-OCT-2006, entry version 24. DE Serpin B10 (Transforming growth factor beta repressible serpin) (TGF- DE beta-repressible serine proteinase inhibitor) (Trespin). GN Name=Serpinb10; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC STRAIN=Wistar; RX MEDLINE=22113007; PubMed=11986314; DOI=10.1074/jbc.M201244200; RA Chipuk J.E., Stewart L.V., Ranieri A., Song K., Danielpour D.; RT "Identification and characterization of a novel rat ov-serpin family RT member, trespin."; RL J. Biol. Chem. 277:26412-26421(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Inhibits plasmin. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including brain, CC heart, kidney, liver, lung, prostate, skin, spleen and stomach. CC -!- SIMILARITY: Belongs to the serpin family. Ov-serpin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY075037; AAL78042.1; -; mRNA. DR EMBL; BC061735; AAH61735.1; -; mRNA. DR HSSP; P05120; 1BY7. DR MEROPS; I04.015; -. DR Ensembl; ENSRNOG00000002417; Rattus norvegicus. DR RGD; 628853; Serpinb10. DR GO; GO:0030414; F:protease inhibitor activity; IDA. DR GO; GO:0045861; P:negative regulation of proteolysis; IDA. DR InterPro; IPR000215; Prot_inh_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Protease inhibitor; Serine protease inhibitor. FT CHAIN 1 397 Serpin B10. FT /FTId=PRO_0000094116. FT SITE 362 363 Reactive bond (By similarity). FT CONFLICT 88 88 M -> I (in Ref. 2). FT CONFLICT 164 164 D -> G (in Ref. 2). FT CONFLICT 288 288 R -> Q (in Ref. 2). FT CONFLICT 391 391 D -> Y (in Ref. 2). SQ SEQUENCE 397 AA; 45387 MW; 19E7BF371A9D2F4C CRC64; MASLAVSINQ FAVEFSKKLA ESAEGRNIFF SPWGISTSLA MVYLGTKGTT AAQMSQVLHF GSIQDFKFGP DSEKKRKMEC HSGKSEEMQS DFQTLTAKIL KHGNSYVLKI ANRIYVEKTY LFHNKYLEDM KTYFGAEPQS VNFVEASGQI RKEINSWVGS QTGDKIPNLL PDDAVDNKTT MVLVNALYFK GTWEHQFSVQ NTTERPFRIN KTTSKPVQMM SMKQSLQVFH IEELQTIGVQ LHYQNREFSL LLLLPEEVEG LKQLERAITY EKLDKWTSAD MMDTYEVRLY LPKFKMEESY DLQSALRDMG MTDAFNQGKA NFSNMTSERN LFLSNVFHKT FLEINEEGTE AAAGTGSEVN FRIKAPSIEL NADHPFLFLI RHNVTNTILF DGRFYSP // ID STK16_HUMAN STANDARD; PRT; 304 AA. AC O75716; Q96KI2; Q9UEN3; Q9UP78; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2004, sequence version 3. DT 03-OCT-2006, entry version 63. DE Serine/threonine-protein kinase 16 (EC 2.7.11.1) (Protein kinase DE PKL12) (Myristoylated and palmitoylated serine/threonine-protein DE kinase) (MPSK) (TGF-beta-stimulated factor 1) (TSF-1) (hPSK). GN Name=STK16; Synonyms=MPSK1, PKL12, TSF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98380270; PubMed=9712705; DOI=10.1006/bbrc.1998.9163; RA Ligos J.M., Gerwin N., Fernandez P., Gutierrez-Ramos J.C., Bernad A.; RT "Cloning, expression analysis, and functional characterization of RT PKL12, a member of a new subfamily of ser/thr kinases."; RL Biochem. Biophys. Res. Commun. 249:380-384(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], MYRISTOYLATION AT GLY-1, AND RP PALMITOYLATION AT CYS-5 AND CYS-7. RX MEDLINE=99294623; PubMed=10364453; DOI=10.1006/bbrc.1999.0811; RA Berson A.E., Young C., Morrison S.L., Fujii G.H., Sheung J., Wu B., RA Bolen J.B., Burkhardt A.L.; RT "Identification and characterization of a myristylated and RT palmitylated serine/threonine protein kinase."; RL Biochem. Biophys. Res. Commun. 259:533-538(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RA Wabakken T.K., Aasheim H.C.; RT "Characterization of a ubiquitous expressed human serine/threonine RT kinase."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=20407116; PubMed=10947953; DOI=10.1042/0264-6021:3500395; RA Ohta S., Takeuchi M., Deguchi M., Tsuji T., Gahara Y., Nagata K.; RT "A novel transcriptional factor with Ser/Thr kinase activity involved RT in the transforming growth factor (TGF)-beta signalling pathway."; RL Biochem. J. 350:395-404(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Stairs D.B., Ha S.I., Chodosh L.A.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Protein kinase that act on both serine and threonine CC residues. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBCELLULAR LOCATION: Membrane; lipid-anchor (Probable). CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at very low levels. CC -!- PTM: Autophosphorylated on serine and threonine residues. CC -!- PTM: It is uncertain whether palmitoylation is on Cys-5 and/or CC Cys-7. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ005791; CAA06700.1; -; mRNA. DR EMBL; AF060798; AAC28337.1; -; mRNA. DR EMBL; AJ010