ID K9IKT9_DESRO Unreviewed; 498 AA.
AC K9IKT9;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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};
OS Desmodus rotundus (Vampire bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Phyllostomidae;
OC Desmodontinae; Desmodus.
OX NCBI_TaxID=9430 {ECO:0000313|EMBL:JAA47823.1};
RN [1] {ECO:0000313|EMBL:JAA47823.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:JAA47823.1};
RA Francischetti I.M.B., Assumpcao T.C.F., Ma D., Vicente E.C.,
RA Ribeiro J.M.C.;
RT "The Vampirome: Transcriptome and Proteome Analysis of the Submandibular
RT and Accessory Glands of the Vampire Bat and Vector of Human Rabies,
RT Desmodus rotundus.";
RL Submitted (NOV-2012) 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; GABZ01005702; JAA47823.1; -; mRNA.
DR AlphaFoldDB; K9IKT9; -.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
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: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:0010628; P:positive regulation of gene expression; ISS:AgBase.
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:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
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, ECO:0000256|RuleBase:RU000304};
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:JAA47823.1};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|RuleBase:RU000304};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427};
KW Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..498
FT /note="TGF-beta receptor type-1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003930789"
FT TRANSMEM 121..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 170..199
FT /note="GS"
FT /evidence="ECO:0000259|PROSITE:PS51256"
FT DOMAIN 200..490
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 498 AA; 55556 MW; 4B8E4545B0F8E738 CRC64;
MEAVAAAPRP RLFPLVLAAV TLVPGATALQ CFCHLCTKDN FTCVTDGLCF VSVTETTDKI
IHNSMCIAEI DLIPRDRPFV CAPSTKTGSV TTPYCCNQDH CNKIELPTAG KPSPGLGPVE
LAAVIAGPVC FVCISLMLMV YVCHNRAAIH HRVPNEEDPS LDRPFISEGT TLKDLIYDMT
TSGSGSGLPL LVQRTIARTI VLQESIGKGR FGEVWRGKWR GEEVAVKIFS SREERSWFRE
AEIYQTVMLR HENILGFIAA DNKDNGTWTQ LWLVSDYHEH GSLFDYLNRY TVTVEGMIKL
ALSTASGLAH LHMEIVGTQG KPAIAHRDLK SKNILVKKNG TCCIADLGLA VRHDSATDTI
DIAPNHRVGT KRYMAPEVLD DSINMKHFES FKRADIYAMG LVFWEIARRC SIGGIHEDYQ
LPYYDLVPSD PSVEEMRKVV CEQKLRPNIP NRWQSCEALR VMAKIMRECW YANGAARLTA
LRIKKTLSQL SQQEGIKM
//
