TGFR1_RAT
ID TGFR1_RAT Reviewed; 501 AA.
AC P80204;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=TGF-beta receptor type-1;
DE Short=TGFR-1;
DE EC=2.7.11.30;
DE AltName: Full=Serine/threonine-protein kinase receptor R4;
DE Short=SKR4;
DE AltName: Full=TGF-beta type I receptor;
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Urogenital ridge;
RX PubMed=8395914; DOI=10.1002/aja.1001960207;
RA He W.-W., Gustafson M.L., Hirobe S., Donahoe P.K.;
RT "Developmental expression of four novel serine/threonine kinase receptors
RT homologous to the activin/transforming growth factor-beta type II receptor
RT family.";
RL Dev. Dyn. 196:133-142(1993).
RN [2]
RP INTERACTION WITH FKBP1A, AND ACTIVITY REGULATION.
RX PubMed=8756725; DOI=10.1016/s0092-8674(00)80116-6;
RA Wang T., Li B.Y., Danielson P.D., Shah P.C., Rockwell S., Lechleider R.J.,
RA Martin J., Manganaro T., Donahoe P.K.;
RT "The immunophilin FKBP12 functions as a common inhibitor of the TGF beta
RT family type I receptors.";
RL Cell 86:435-444(1996).
RN [3]
RP SUMOYLATION AT LYS-389.
RX PubMed=18469808; DOI=10.1038/ncb1728;
RA Kang J.S., Saunier E.F., Akhurst R.J., Derynck R.;
RT "The type I TGF-beta receptor is covalently modified and regulated by
RT sumoylation.";
RL Nat. Cell Biol. 10:654-664(2008).
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. {ECO:0000269|PubMed:8756725}.
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. Interacts with CD109; inhibits
CC TGF-beta receptor activation in keratinocytes. Interacts with RBPMS.
CC Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3
CC to the TGF-beta receptor. Interacts with TRAF6 and MAP3K7; induces
CC MAP3K7 activation by TRAF6. Interacts with PARD6A; involved in TGF-beta
CC induced epithelial to mesenchymal transition. Interacts with SMAD7,
CC NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1 and SMURF2 to
CC the TGF-beta receptor (By similarity). Interacts with USP15 and VPS39
CC (By similarity). Interacts (unphosphorylated) with FKBP1A; prevents
CC TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive
CC conformation. Interacts with SDCBP (via C-terminus). Interacts with
CC CAV1 and this interaction is impaired in the presence of SDCBP (By
CC similarity). Interacts with APPL1; interaction is TGF beta dependent;
CC mediates trafficking of the TGFBR1 from the endosomes to the nucleus
CC via microtubules in a TRAF6-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P36897, ECO:0000269|PubMed:8756725}.
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 -!- TISSUE SPECIFICITY: Urogenital ridge, testis, ovary, brain and lungs.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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DR EMBL; L26110; AAA83216.1; -; mRNA.
DR RefSeq; XP_006238092.2; XM_006238030.3.
DR AlphaFoldDB; P80204; -.
DR SMR; P80204; -.
DR BioGRID; 248223; 2.
DR CORUM; P80204; -.
DR IntAct; P80204; 4.
DR MINT; P80204; -.
DR STRING; 10116.ENSRNOP00000009452; -.
DR ChEMBL; CHEMBL4523265; -.
DR GlyGen; P80204; 1 site.
DR PhosphoSitePlus; P80204; -.
DR PaxDb; P80204; -.
DR PRIDE; P80204; -.
DR GeneID; 29591; -.
DR UCSC; RGD:3852; rat.
DR CTD; 7046; -.
DR RGD; 3852; Tgfbr1.
DR eggNOG; KOG2052; Eukaryota.
DR HOGENOM; CLU_000288_8_1_1; -.
DR InParanoid; P80204; -.
DR OrthoDB; 776697at2759; -.
DR PhylomeDB; P80204; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 5301.
DR BRENDA; 2.7.11.30; 5301.
DR Reactome; R-RNO-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR PRO; PR:P80204; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P80204; RN.
DR GO; GO:0048179; C:activin receptor complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005901; C:caveola; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0070411; F:I-SMAD binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0050431; F:transforming growth factor beta binding; IDA:RGD.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; ISO:RGD.
DR GO; GO:0005025; F:transforming growth factor beta receptor activity, type I; IMP:RGD.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0032924; P:activin receptor signaling pathway; ISS:AgBase.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0048870; P:cell motility; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0060982; P:coronary artery morphogenesis; ISO:RGD.
DR GO; GO:0048565; P:digestive tract development; IEP:RGD.
DR GO; GO:0007566; P:embryo implantation; IEP:RGD.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
DR GO; GO:0042118; P:endothelial cell activation; ISS:AgBase.
DR GO; GO:0043542; P:endothelial cell migration; ISO:RGD.
DR GO; GO:1905223; P:epicardium morphogenesis; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0008354; P:germ cell migration; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISS:AgBase.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:AgBase.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISO:RGD.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IMP:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0048663; P:neuron fate commitment; ISO:RGD.
DR GO; GO:0060017; P:parathyroid gland development; ISO:RGD.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0060037; P:pharyngeal system development; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1905007; P:positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation; ISO:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:RGD.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:1905075; P:positive regulation of tight junction disassembly; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:AgBase.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP:RGD.
DR GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; ISO:RGD.
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:0043393; P:regulation of protein binding; ISO:RGD.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0070723; P:response to cholesterol; ISO:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0034695; P:response to prostaglandin E; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:RGD.
DR GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISO:RGD.
DR GO; GO:0060412; P:ventricular septum morphogenesis; ISO:RGD.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISO:RGD.
DR Gene3D; 2.10.60.10; -; 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; PTHR23255; 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; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 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 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell junction; Cell membrane; Differentiation;
KW Disulfide bond; Glycoprotein; Growth regulation; Isopeptide bond; Kinase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW 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..501
FT /note="TGF-beta receptor type-1"
FT /id="PRO_0000024425"
FT TOPO_DOM 30..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 173..202
FT /note="GS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00585"
FT DOMAIN 203..493
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 191..192
FT /note="FKBP1A-binding"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P36897"
FT MOD_RES 183
FT /note="Phosphothreonine; by TGFBR2"
FT /evidence="ECO:0000250|UniProtKB:P36897"
FT MOD_RES 184
FT /note="Phosphothreonine; by TGFBR2"
FT /evidence="ECO:0000250|UniProtKB:P36897"
FT MOD_RES 185
FT /note="Phosphoserine; 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 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..94
FT /evidence="ECO:0000250|UniProtKB:P36897"
FT DISULFID 95..100
FT /evidence="ECO:0000250|UniProtKB:P36897"
FT CROSSLNK 389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
SQ SEQUENCE 501 AA; 56000 MW; EAD7F8D37E456102 CRC64;
MEAASAALRR CLLLIVLVAA ATLLPGAKAL QCFCHLCTKD NFTCETDGLC FVSVTETTDK
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGA VTYCCNQDHC NKIELPTTGP FSEKQSAGLG
PVELAAVIAG PVCFVCIALM LMVYICHNRT VIHHRVPNEE DPSLDRPFIS EGTTLKDLIY
DMTTSGSGSG LPLLVQRTIA RTIVLQESIG KGRFGEVWRG KWRGEEVAVK IFSSREERSW
FREAEIYQTV MLRHENILGF IAADNKDNGT WTQLWLVSDY HEHGSLFDYL NRYTVTVEGM
IKLALSTASG LAHLHMEIVG TQGKPAIAHR DLKSKNILVK KNGTCCIADL GLAVRHDSAT
DTIDIAPNHR VGTKRYMAPE VLDDSINMKH FESFKRADIY AMGLVFWEIA RRCSIGGIHE
DYQLPYYDLV PSDPSVEEMR KVVCEQKLRP NIPNRWQSCE ALRVMAKIMR ECWYANGAAR
LTALRIKKTL SQLSQQEGIK M
