ID TGFR1_MOUSE Reviewed; 503 AA. AC Q64729; A2AJN0; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 212. DE RecName: Full=TGF-beta receptor type-1; DE Short=TGFR-1; DE EC=2.7.11.30; DE AltName: Full=ESK2; DE AltName: Full=Transforming growth factor-beta receptor type I; DE Short=TGF-beta receptor type I; DE Short=TbetaR-I; DE Flags: Precursor; GN Name=Tgfbr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain, and Testis; RX PubMed=8117261; DOI=10.1006/bbrc.1994.1150; RA Tomoda T., Kudoh T., Noma T., Nakazawa A., Muramatsu M.-A., Arai K.; RT "Molecular cloning of a mouse counterpart for human TGF-beta type I RT receptor."; RL Biochem. Biophys. Res. Commun. 198:1054-1062(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=8117262; DOI=10.1006/bbrc.1994.1151; RA Suzuki A., Shioda N., Maeda T., Tada M., Ueno N.; RT "A mouse TGF-beta type I receptor that requires type II receptor for ligand RT binding."; RL Biochem. Biophys. Res. Commun. 198:1063-1069(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF- CC beta type II serine/threonine kinase receptor, TGFBR2, the non- CC promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. CC Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to CC the cytoplasm and is thus regulating a plethora of physiological and CC pathological processes including cell cycle arrest in epithelial and CC hematopoietic cells, control of mesenchymal cell proliferation and CC differentiation, wound healing, extracellular matrix production, CC immunosuppression and carcinogenesis. The formation of the receptor CC complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound CC to the cytokine dimer results in the phosphorylation and the activation CC of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 CC phosphorylates SMAD2 which dissociates from the receptor and interacts CC with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the CC nucleus where it modulates the transcription of the TGF-beta-regulated CC genes. This constitutes the canonical SMAD-dependent TGF-beta signaling CC cascade. Also involved in non-canonical, SMAD-independent TGF-beta CC signaling pathways. For instance, TGFBR1 induces TRAF6 CC autoubiquitination which in turn results in MAP3K7 ubiquitination and CC activation to trigger apoptosis. Also regulates epithelial to CC mesenchymal transition through a SMAD-independent signaling pathway CC through PARD6A phosphorylation and activation (By similarity). CC {ECO:0000250|UniProtKB:P36897}. 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 -!- 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; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC -!- ACTIVITY REGULATION: Kept in an inactive conformation by FKBP1A CC preventing receptor activation in absence of ligand. CD109 is another CC inhibitor of the receptor (By similarity). CC {ECO:0000250|UniProtKB:P36897}. CC -!- SUBUNIT: Homodimer; in the endoplasmic reticulum but also at the cell CC membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands CC assemble a functional receptor composed of two TGFBR1 and TGFBR2 CC heterodimers to form a ligand-receptor heterohexamer. The respective CC affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics CC of assembly of the receptor and may explain the different biological CC activities of TGFB1, TGFB2 and TGFB3. Component of a complex composed CC of TSC22D1 (via N-terminus), TGFBR1 and TGFBR2; the interaction between CC TSC22D1 and TGFBR1 is inhibited by SMAD7 and promoted by TGFB1 (By CC similarity). Interacts with CD109; inhibits TGF-beta receptor CC activation in keratinocytes. Interacts with RBPMS. Interacts CC (unphosphorylated) with FKBP1A; prevents TGFBR1 phosphorylation by CC TGFBR2 and stabilizes it in the inactive conformation. Interacts with CC SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF- CC beta receptor. Interacts with TRAF6 and MAP3K7; induces MAP3K7 CC activation by TRAF6. Interacts with PARD6A; involved in TGF-beta CC induced epithelial to mesenchymal transition. Interacts with NEDD4L (By CC similarity). Interacts with SMAD7, SMURF1 and SMURF2; SMAD7 recruits CC NEDD4L, SMURF1 and SMURF2 to the TGF-beta receptor (By similarity). CC Interacts with USP15 and VPS39. Interacts with SDCBP (via C-terminus) CC (By similarity). Interacts with CAV1 and this interaction is impaired CC in the presence of SDCBP (By similarity). Interacts with APPL1; CC interaction is TGF beta dependent; mediates trafficking of the TGFBR1 CC from the endosomes to the nucleus via microtubules in a TRAF6-dependent CC manner (By similarity). Interacts with GPR50; this interaction promotes CC the constitutive activation of SMAD signaling pathway (By similarity). CC {ECO:0000250|UniProtKB:P36897}. CC -!- INTERACTION: CC Q64729; Q9DBG3: Ap2b1; NbExp=2; IntAct=EBI-2899393, EBI-775229; CC Q64729; P49817: Cav1; NbExp=4; IntAct=EBI-2899393, EBI-1161338; CC Q64729; P15379: Cd44; NbExp=4; IntAct=EBI-2899393, EBI-7565891; CC Q64729; P55284: Cdh5; NbExp=2; IntAct=EBI-2899393, EBI-7087433; CC Q64729; P05533: Ly6a; NbExp=2; IntAct=EBI-2899393, EBI-11600492; CC Q64729; P98083-2: Shc1; NbExp=7; IntAct=EBI-2899393, EBI-1019301; CC Q64729; Q62312: Tgfbr2; NbExp=3; IntAct=EBI-2899393, EBI-2899332; CC Q64729; P63010: AP2B1; Xeno; NbExp=3; IntAct=EBI-2899393, EBI-432924; CC Q64729; Q8TDM6: DLG5; Xeno; NbExp=3; IntAct=EBI-2899393, EBI-715138; CC Q64729; P84022: SMAD3; Xeno; NbExp=6; IntAct=EBI-2899393, EBI-347161; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P36897}; CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P36897}. CC Cell junction, tight junction {ECO:0000250|UniProtKB:P36897}. Membrane CC raft {ECO:0000250|UniProtKB:P36897}. Cell surface CC {ECO:0000250|UniProtKB:P36897}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q64729-1; Sequence=Displayed; CC Name=2; CC IsoId=Q64729-2; Sequence=VSP_021593; CC -!- PTM: Phosphorylated at basal levels in the absence of ligand. Activated CC upon phosphorylation by TGFBR2, mainly in the GS domain. CC Phosphorylation in the GS domain abrogates FKBP1A-binding (By CC similarity). {ECO:0000250|UniProtKB:P36897}. CC -!- PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P36897}. CC -!- PTM: Ubiquitinated; undergoes ubiquitination catalyzed by several E3 CC ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the CC proteasomal and/or lysosomal degradation of the receptor thereby CC negatively regulating its activity. Deubiquitinated by USP15, leading CC to stabilization of the protein and enhanced TGF-beta signal. Its CC ubiquitination and proteasome-mediated degradation is negatively CC regulated by SDCBP (By similarity). {ECO:0000250|UniProtKB:P36897}. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice CC site. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D28526; BAA05878.1; -; mRNA. DR EMBL; D25540; BAA05023.1; -; mRNA. DR EMBL; AL772150; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL772232; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC063260; AAH63260.1; -; mRNA. DR CCDS; CCDS18160.1; -. [Q64729-1] DR CCDS; CCDS84728.1; -. [Q64729-2] DR PIR; JC2061; JC2061. DR PIR; JC2062; JC2062. DR RefSeq; NP_001299797.1; NM_001312868.1. [Q64729-2] DR RefSeq; NP_001299798.1; NM_001312869.1. DR RefSeq; NP_033396.1; NM_009370.3. [Q64729-1] DR AlphaFoldDB; Q64729; -. DR SMR; Q64729; -. DR BioGRID; 204163; 28. DR ComplexPortal; CPX-823; TGF-beta-1-TGFR complex. DR ComplexPortal; CPX-826; TGF-beta-3-TGFR complex. DR ComplexPortal; CPX-836; TGF-beta-2-TGFR complex. DR CORUM; Q64729; -. DR DIP; DIP-42262N; -. DR IntAct; Q64729; 31. DR MINT; Q64729; -. DR STRING; 10090.ENSMUSP00000007757; -. DR BindingDB; Q64729; -. DR ChEMBL; CHEMBL2021750; -. DR GlyCosmos; Q64729; 1 site, No reported glycans. DR GlyGen; Q64729; 1 site. DR iPTMnet; Q64729; -. DR PhosphoSitePlus; Q64729; -. DR MaxQB; Q64729; -. DR PaxDb; 10090-ENSMUSP00000007757; -. DR ProteomicsDB; 258866; -. [Q64729-1] DR ProteomicsDB; 258867; -. [Q64729-2] DR Antibodypedia; 29038; 723 antibodies from 43 providers. DR DNASU; 21812; -. DR Ensembl; ENSMUST00000007757.15; ENSMUSP00000007757.9; ENSMUSG00000007613.16. [Q64729-1] DR Ensembl; ENSMUST00000044234.14; ENSMUSP00000048501.8; ENSMUSG00000007613.16. [Q64729-2] DR GeneID; 21812; -. DR KEGG; mmu:21812; -. DR UCSC; uc008sun.1; mouse. [Q64729-1] DR UCSC; uc008suo.1; mouse. [Q64729-2] DR AGR; MGI:98728; -. DR CTD; 7046; -. DR MGI; MGI:98728; Tgfbr1. DR VEuPathDB; HostDB:ENSMUSG00000007613; -. DR eggNOG; KOG2052; Eukaryota. DR GeneTree; ENSGT00940000156394; -. DR InParanoid; Q64729; -. DR OMA; VPHCCDK; -. DR OrthoDB; 3900892at2759; -. DR PhylomeDB; Q64729; -. DR TreeFam; TF314724; -. DR BRENDA; 2.7.10.2; 3474. DR Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling. DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs. DR Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition). DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR BioGRID-ORCS; 21812; 5 hits in 78 CRISPR screens. DR ChiTaRS; Tgfbr1; mouse. DR PRO; PR:Q64729; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q64729; Protein. DR Bgee; ENSMUSG00000007613; Expressed in metanephric cortical collecting duct and 279 other cell types or tissues. DR ExpressionAtlas; Q64729; baseline and differential. DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central. DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI. DR GO; GO:0005923; C:bicellular tight junction; ISO:MGI. DR GO; GO:0005901; C:caveola; ISO:MGI. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:AgBase. DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0043235; C:receptor complex; ISO:MGI. DR GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; ISO:MGI. DR GO; GO:0048185; F:activin binding; IBA:GO_Central. DR GO; GO:0016361; F:activin receptor activity, type I; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; ISO:MGI. DR GO; GO:0070411; F:I-SMAD binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; ISO:MGI. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0046332; F:SMAD binding; IDA:BHF-UCL. DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:MGI. DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IDA:UniProtKB. DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; ISS:AgBase. DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISO:MGI. DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISO:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:AgBase. DR GO; GO:0001525; P:angiogenesis; IMP:MGI. DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IMP:BHF-UCL. DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI. DR GO; GO:0006915; P:apoptotic process; IMP:MGI. DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI. DR GO; GO:0001824; P:blastocyst development; IDA:MGI. DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase. DR GO; GO:0048870; P:cell motility; ISO:MGI. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL. DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI. DR GO; GO:0060982; P:coronary artery morphogenesis; IMP:BHF-UCL. DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI. DR GO; GO:0042118; P:endothelial cell activation; ISS:AgBase. DR GO; GO:0043542; P:endothelial cell migration; IMP:MGI. DR GO; GO:0001935; P:endothelial cell proliferation; IGI:MGI. DR GO; GO:1905223; P:epicardium morphogenesis; IMP:BHF-UCL. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:MGI. DR GO; GO:0046847; P:filopodium assembly; IMP:MGI. DR GO; GO:0008354; P:germ cell migration; IMP:MGI. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0035556; P:intracellular signal transduction; ISS:AgBase. DR GO; GO:0001822; P:kidney development; IGI:MGI. DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI. DR GO; GO:0008584; P:male gonad development; IMP:MGI. DR GO; GO:0048762; P:mesenchymal cell differentiation; ISS:AgBase. DR GO; GO:0036446; P:myofibroblast differentiation; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI. DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:BHF-UCL. DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:MGI. DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IGI:MGI. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0048663; P:neuron fate commitment; IMP:MGI. DR GO; GO:0060017; P:parathyroid gland development; IMP:MGI. DR GO; GO:0060037; P:pharyngeal system development; IMP:MGI. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:BHF-UCL. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. 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:0010718; P:positive regulation of epithelial to mesenchymal transition; IGI:BHF-UCL. DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL. DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISO:MGI. DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase. DR GO; GO:1902462; P:positive regulation of mesenchymal stem cell proliferation; ISO:MGI. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI. DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IGI:BHF-UCL. DR GO; GO:1905075; P:positive regulation of tight junction disassembly; IGI:BHF-UCL. DR GO; GO:1904018; P:positive regulation of vasculature development; ISO:MGI. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; IMP:BHF-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISS:AgBase. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI. DR GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL. DR GO; GO:0043627; P:response to estrogen; ISO:MGI. DR GO; GO:0060021; P:roof of mouth development; IMP:MGI. DR GO; GO:0007165; P:signal transduction; ISO:MGI. DR GO; GO:0001501; P:skeletal system development; IGI:MGI. DR GO; GO:0048705; P:skeletal system morphogenesis; IGI:MGI. DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI. DR GO; GO:0048538; P:thymus development; IMP:MGI. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI. DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; IMP:BHF-UCL. DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL. DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL. 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. DR Genevisible; Q64729; MM. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; ATP-binding; Cell junction; Cell membrane; KW Differentiation; Disulfide bond; Glycoprotein; Growth regulation; KW Isopeptide bond; Kinase; Magnesium; Manganese; Membrane; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; KW Serine/threonine-protein kinase; Signal; Tight junction; Transferase; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1..29 FT /evidence="ECO:0000250" FT CHAIN 30..503 FT /note="TGF-beta receptor type-1" FT /id="PRO_0000024424" FT TOPO_DOM 30..126 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 127..147 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 148..503 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 175..204 FT /note="GS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585" FT DOMAIN 205..495 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOTIF 193..194 FT /note="FKBP1A-binding" FT ACT_SITE 333 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 211..219 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 232 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P36897" FT MOD_RES 185 FT /note="Phosphothreonine; by TGFBR2" FT /evidence="ECO:0000250|UniProtKB:P36897" FT MOD_RES 186 FT /note="Phosphothreonine; by TGFBR2" FT /evidence="ECO:0000250|UniProtKB:P36897" FT MOD_RES 187 FT /note="Phosphoserine; by TGFBR2" FT /evidence="ECO:0000250|UniProtKB:P36897" FT MOD_RES 189 FT /note="Phosphoserine; by TGFBR2" FT /evidence="ECO:0000250|UniProtKB:P36897" FT MOD_RES 191 FT /note="Phosphoserine; by TGFBR2" FT /evidence="ECO:0000250|UniProtKB:P36897" FT CARBOHYD 41 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 32..50 FT /evidence="ECO:0000250|UniProtKB:P36897" FT DISULFID 34..37 FT /evidence="ECO:0000250|UniProtKB:P36897" FT DISULFID 44..67 FT /evidence="ECO:0000250|UniProtKB:P36897" FT DISULFID 82..96 FT /evidence="ECO:0000250|UniProtKB:P36897" FT DISULFID 97..102 FT /evidence="ECO:0000250|UniProtKB:P36897" FT CROSSLNK 391 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250" FT VAR_SEQ 111..114 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8117262" FT /id="VSP_021593" SQ SEQUENCE 503 AA; 56179 MW; BB8BB6D2261793AF CRC64; MEAAAAAPRR PQLLIVLVAA ATLLPGAKAL QCFCHLCTKD NFTCETDGLC FVSVTETTDK VIHNSMCIAE IDLIPRDRPF VCAPSSKTGA VTTTYCCNQD HCNKIELPTT GPFSEKQSAG LGPVELAAVI AGPVCFVCIA 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 //