ID Q4FJL1_MOUSE Unreviewed; 503 AA. AC Q4FJL1; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 170. 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|MGI:MGI:98728}; 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 {ECO:0000313|EMBL:CAJ18600.1}; RN [1] {ECO:0000313|EMBL:CAJ18600.1} RP NUCLEOTIDE SEQUENCE. RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., RA Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) 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}. 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; CT010393; CAJ18600.1; -; mRNA. DR RefSeq; NP_033396.1; NM_009370.3. DR AlphaFoldDB; Q4FJL1; -. DR SMR; Q4FJL1; -. DR SwissPalm; Q4FJL1; -. DR Antibodypedia; 29038; 723 antibodies from 43 providers. DR DNASU; 21812; -. DR GeneID; 21812; -. DR KEGG; mmu:21812; -. DR AGR; MGI:98728; -. DR CTD; 7046; -. DR MGI; MGI:98728; Tgfbr1. DR VEuPathDB; HostDB:ENSMUSG00000007613; -. DR OMA; VPHCCDK; -. DR OrthoDB; 3900892at2759; -. DR PhylomeDB; Q4FJL1; -. DR BioGRID-ORCS; 21812; 5 hits in 78 CRISPR screens. DR ChiTaRS; Tgfbr1; mouse. DR ExpressionAtlas; Q4FJL1; 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: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; IEA:Ensembl. 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:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase. DR GO; GO:0048870; P:cell motility; IEA:Ensembl. DR GO; GO:0042118; P:endothelial cell activation; ISS:AgBase. DR GO; GO:0007507; P:heart development; ISS:AgBase. DR GO; GO:0035556; P:intracellular signal transduction; ISS:AgBase. 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:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; 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:1901203; P:positive regulation of extracellular matrix 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:1904018; P:positive regulation of vasculature development; 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:0007179; P:transforming growth factor beta receptor signaling pathway; 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 2: Evidence at transcript level; 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 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}; 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..29 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 30..503 FT /note="TGF-beta receptor type-1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015097605" 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; 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 //