ID Q5T7S2_HUMAN Unreviewed; 503 AA.
AC Q5T7S2;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 179.
DE RecName: Full=TGF-beta receptor type-1 {ECO:0000256|ARBA:ARBA00040150};
DE EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
DE AltName: Full=Transforming growth factor-beta receptor type I {ECO:0000256|ARBA:ARBA00043075};
GN Name=TGFBR1 {ECO:0000313|EMBL:ACZ58375.1};
GN ORFNames=hCG_30154 {ECO:0000313|EMBL:EAW58905.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ACZ58375.1};
RN [1] {ECO:0000313|EMBL:EAW58905.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11181995; DOI=10.1126/science.1058040;
RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT "The sequence of the human genome.";
RL Science 291:1304-1351(2001).
RN [2] {ECO:0000313|EMBL:EAW58905.1}
RP NUCLEOTIDE SEQUENCE.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABD46753.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17319955; DOI=10.1186/1471-2350-8-5;
RA McKnight A.J., Savage D.A., Patterson C.C., Sadlier D., Maxwell A.P.;
RT "Resequencing of genes for transforming growth factor beta1 (TGFB1) type 1
RT and 2 receptors (TGFBR1, TGFBR2), and association analysis of variants with
RT diabetic nephropathy.";
RL BMC Med. Genet. 8:5-5(2007).
RN [4] {ECO:0000313|EMBL:ACZ58375.1}
RP NUCLEOTIDE SEQUENCE.
RA Rieder M.J., Bertucci C., Stanaway I.B., Johnson E.J., Swanson J.E.,
RA Siegel D.L., da Ponte S.H., Igartua C., Patterson K., Nickerson D.A.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30; Evidence={ECO:0000256|ARBA:ARBA00023945};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC Evidence={ECO:0000256|ARBA:ARBA00023948};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251}. Cell surface
CC {ECO:0000256|ARBA:ARBA00004241}. Membrane raft
CC {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605}.
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DR EMBL; AH015633; ABD46753.1; -; Genomic_DNA.
DR EMBL; DQ383416; ABD46753.1; JOINED; Genomic_DNA.
DR EMBL; DQ383417; ABD46753.1; JOINED; Genomic_DNA.
DR EMBL; DQ383418; ABD46753.1; JOINED; Genomic_DNA.
DR EMBL; DQ383419; ABD46753.1; JOINED; Genomic_DNA.
DR EMBL; DQ383421; ABD46753.1; JOINED; Genomic_DNA.
DR EMBL; DQ383422; ABD46753.1; JOINED; Genomic_DNA.
DR EMBL; DQ383424; ABD46753.1; JOINED; Genomic_DNA.
DR EMBL; GU143401; ACZ58375.1; -; Genomic_DNA.
DR EMBL; CH471105; EAW58905.1; -; Genomic_DNA.
DR RefSeq; NP_004603.1; NM_004612.3.
DR SMR; Q5T7S2; -.
DR Antibodypedia; 29038; 723 antibodies from 43 providers.
DR DNASU; 7046; -.
DR GeneID; 7046; -.
DR KEGG; hsa:7046; -.
DR UCSC; uc004azc.4; human.
DR CTD; 7046; -.
DR PharmGKB; PA36485; -.
DR VEuPathDB; HostDB:ENSG00000106799; -.
DR OMA; VPHCCDK; -.
DR OrthoDB; 3900892at2759; -.
DR BioGRID-ORCS; 7046; 59 hits in 1182 CRISPR screens.
DR ChiTaRS; TGFBR1; human.
DR GenomeRNAi; 7046; -.
DR ExpressionAtlas; Q5T7S2; baseline and differential.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098802; C:plasma membrane signaling receptor complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:AgBase.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; ISS:AgBase.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:AgBase.
DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IEA:Ensembl.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
DR GO; GO:0060982; P:coronary artery morphogenesis; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR GO; GO:0042118; P:endothelial cell activation; ISS:AgBase.
DR GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:1905223; P:epicardium morphogenesis; IEA:Ensembl.
DR GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; ISS:AgBase.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:AgBase.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0002088; P:lens development in camera-type eye; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0048663; P:neuron fate commitment; IEA:Ensembl.
DR GO; GO:0060017; P:parathyroid gland development; IEA:Ensembl.
DR GO; GO:0060037; P:pharyngeal system development; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:AgBase.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:AgBase.
DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IEA:Ensembl.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1905075; P:positive regulation of tight junction disassembly; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0010468; P:regulation of gene expression; ISS:AgBase.
DR GO; GO:0070723; P:response to cholesterol; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IEA:Ensembl.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IEA:Ensembl.
DR CDD; cd14143; STKc_TGFbR1_ACVR1b_ACVR1c; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR003605; GS_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF61; TGF-BETA RECEPTOR TYPE-1; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08515; TGF_beta_GS; 1.
DR SMART; SM00467; GS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 1.
DR PROSITE; PS51256; GS; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Kinase {ECO:0000313|EMBL:EAW58905.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:ACZ58375.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transferase {ECO:0000256|ARBA:ARBA00022527};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..503
FT /note="TGF-beta receptor type-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014309963"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 175..204
FT /note="GS"
FT /evidence="ECO:0000259|PROSITE:PS51256"
FT DOMAIN 205..495
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 503 AA; 55960 MW; 179F11404725DDCB CRC64;
MEAAVAAPRP RLLLLVLAAA AAAAAALLPG ATALQCFCHL CTKDNFTCVT DGLCFVSVTE
TTDKVIHNSM CIAEIDLIPR DRPFVCAPSS KTGSVTTTYC CNQDHCNKIE LPTTVKSSPG
LGPVELAAVI AGPVCFVCIS LMLMVYICHN RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL
IYDMTTSGSG SGLPLLVQRT IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER
SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE
GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA DLGLAVRHDS
ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD IYAMGLVFWE IARRCSIGGI
HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL RPNIPNRWQS CEALRVMAKI MRECWYANGA
ARLTALRIKK TLSQLSQQEG IKM
//
