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Database: UniProt
Entry: G3WW65_SARHA
LinkDB: G3WW65_SARHA
Original site: G3WW65_SARHA 
ID   G3WW65_SARHA            Unreviewed;       556 AA.
AC   G3WW65;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 74.
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|Ensembl:ENSSHAP00000019670.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000019670.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000019670.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000019670.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; G3WW65; -.
DR   STRING; 9305.ENSSHAP00000019670; -.
DR   Ensembl; ENSSHAT00000019827.2; ENSSHAP00000019670.2; ENSSHAG00000016699.2.
DR   eggNOG; KOG2052; Eukaryota.
DR   GeneTree; ENSGT00940000156394; -.
DR   HOGENOM; CLU_000288_8_1_1; -.
DR   InParanoid; G3WW65; -.
DR   TreeFam; TF314724; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
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:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0070021; C:transforming growth factor beta ligand-receptor complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070411; F:I-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:0005114; F:type II transforming growth factor beta receptor binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
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:0036446; P:myofibroblast differentiation; IEA:Ensembl.
DR   GO; GO:0030336; P:negative regulation of cell migration; 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:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; 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:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0030335; P:positive regulation of cell migration; 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:1901203; P:positive regulation of extracellular matrix assembly; 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:1902462; P:positive regulation of mesenchymal stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
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:1904018; P:positive regulation of vasculature development; 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:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
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:0000256|ARBA:ARBA00022527};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        179..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          228..257
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          258..548
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         285
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   556 AA;  61735 MW;  09625BEE2A2FE930 CRC64;
     MGGPPPSSYK GAERGRGARR GSRVPRGGGS ETRPRPLERT GRGGRRGTME AAAAAAAVAG
     KATVPPRYQM FLLLAATGLV PGAAGLQCYC HLCIKENYTC VTDGICFVAV TQNADKVIYN
     SMCIPEVDLI PRDRPFVCAP SLRDGFLMSP FCCSKDHCNK IEFPTGTPMK PSNLGPVELA
     AVIAGPVCLV CISLMLMIYI CHNRTVIHHR VPNEEDPSLD RPFISEGTTL KDLIYDMTTS
     GSGSGLPLLV QRTIARTIVL QESIGKGRFG EVWRGKWRGE EVAVKIFSSR EERSWFREAE
     IYQTVMLRHE NILGFIAADN KDNGTWTQLW LVSDYHEHGS LFDYLNRYTV TVEGMIKLAL
     STASGLAHLH MEIVGTQGKP AIAHRDLKSK NILVKKNGTC CIADLGLAVR HDSATDTIDI
     APNHRVGTKR YMAPEVLDDS INMKHFESFK RADIYAMGLV FWEIARRCSI GGIHEDYQLP
     YYDLVPSDPS VDEMRKVVCE QKLRPNIPNR WQSCEALRVM AKIMRECWYA NGAARLTALR
     IKKTLSQLSQ QEGIKM
//
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