UniProt: A0A851IR79

Database: UniProt
Entry: A0A851IR79_9PASS

LinkDB:  A0A851IR79_9PASS 
Original site:  A0A851IR79_9PASS

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Ontology (13)   
   GO (13)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (29)   
   InterPro (15)   
   Pfam (6)   
   PROSITE (5)   
   SMART (3)   
All databases (44)   

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ID   A0A851IR79_9PASS        Unreviewed;      1029 AA.
AC   A0A851IR79;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   28-JAN-2026, entry version 20.
DE   RecName: Full=Platelet-derived growth factor receptor beta {ECO:0000256|ARBA:ARBA00020507};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE   AltName: Full=Beta platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00029696};
DE   AltName: Full=Beta-type platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00032009};
DE   AltName: Full=CD140 antigen-like family member B {ECO:0000256|ARBA:ARBA00075975};
DE   AltName: Full=Platelet-derived growth factor receptor 1 {ECO:0000256|ARBA:ARBA00075984};
DE   Flags: Fragment;
GN   Name=Pdgfrb {ECO:0000313|EMBL:NXB69559.1};
GN   ORFNames=DONATR_R07609 {ECO:0000313|EMBL:NXB69559.1};
OS   Donacobius atricapilla.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Mimidae; Donacobius.
OX   NCBI_TaxID=237420 {ECO:0000313|EMBL:NXB69559.1, ECO:0000313|Proteomes:UP000660704};
RN   [1] {ECO:0000313|EMBL:NXB69559.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B10K-DU-001-63 {ECO:0000313|EMBL:NXB69559.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXB69559.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00051243};
CC   -!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
CC       heterodimers formed by PDGFA and PDGFB. May also interact with
CC       homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction
CC       with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
CC       homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA
CC       homodimers and heterodimers with PDGFRB are observed. Interacts with
CC       SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB.
CC       Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts
CC       (tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated)
CC       with SRC and SRC family kinases. Interacts (tyrosine phosphorylated)
CC       with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated)
CC       with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by
CC       SHC1. Interacts (via C-terminus) with NHERF1.
CC       {ECO:0000256|ARBA:ARBA00066051}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Lysosome lumen
CC       {ECO:0000256|ARBA:ARBA00004227}. Membrane
CC       {ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC       {ECO:0000256|RuleBase:RU000311}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSF-1/PDGF receptor subfamily.
CC       {ECO:0000256|RuleBase:RU000311}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NXB69559.1}.
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DR   EMBL; WBMY01000389; NXB69559.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A851IR79; -.
DR   Proteomes; UP000660704; Unassembled WGS sequence.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043235; C:receptor complex; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IEA:TreeGrafter.
DR   GO; GO:0048407; F:platelet-derived growth factor binding; IEA:TreeGrafter.
DR   GO; GO:0001525; P:angiogenesis; IEA:TreeGrafter.
DR   GO; GO:0060326; P:cell chemotaxis; IEA:TreeGrafter.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR   GO; GO:1902533; P:positive regulation of intracellular signal transduction; IEA:UniProtKB-ARBA.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:TreeGrafter.
DR   CDD; cd00096; Ig; 1.
DR   FunFam; 3.30.200.20:FF:000025; Platelet-derived growth factor receptor alpha; 1.
DR   FunFam; 1.10.510.10:FF:000140; Platelet-derived growth factor receptor beta; 1.
DR   FunFam; 2.60.40.10:FF:000223; Platelet-derived growth factor receptor beta; 1.
DR   FunFam; 2.60.40.10:FF:000572; Platelet-derived growth factor receptor beta; 1.
DR   FunFam; 2.60.40.10:FF:000715; Platelet-derived growth factor receptor beta; 1.
DR   FunFam; 2.60.40.10:FF:000982; Platelet-derived growth factor receptor beta; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR   PANTHER; PTHR24416:SF53; PLATELET-DERIVED GROWTH FACTOR RECEPTOR BETA; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13895; Ig_2; 1.
DR   Pfam; PF25305; Ig_PDGFR_d4; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000615; TyrPK_CSF1-R; 1.
DR   PRINTS; PR01832; VEGFRECEPTOR.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000615-
KW   2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW   ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR000615-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW   Reference proteome {ECO:0000313|Proteomes:UP000660704};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000311};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   TRANSMEM        514..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..97
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          193..288
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          304..389
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          397..504
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          582..945
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        808
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT   BINDING         561
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         589..596
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         664..670
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         812
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT   BINDING         813
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   BINDING         826
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT   SITE            952
FT                   /note="Important for interaction with phosphotyrosine-
FT                   binding proteins"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXB69559.1"
FT   NON_TER         1029
FT                   /evidence="ECO:0000313|EMBL:NXB69559.1"
SQ   SEQUENCE   1029 AA;  116097 MW;  3D657BBEE0C474A6 CRC64;
     LSGLLEVTFG DSSLHIEPRD TELVLSLHST FSLLCYGDRE LVWEREGQPL AASLEHRDGV
     FVSNLTLRNV TGHHTGEYTC TYSREQAPEP GERRALYIYV PDPSLVFLPA VTSEEVFIFI
     TGYTEAVIPC RVTNPQMQVT LYEKKVENPI PATYDPQQGF KGFFEDKTYF CRTFVDDQEV
     DSDTFYVYRI QVSSVNVSIS AVQTMVRQGE NVTVMCTVSG NELVNFNWDY PRKQAGKAVE
     PVTDFLPGST HEIRSILVIQ NAELEDSGTY VCNVSEGYHE KTDRKDITVQ VIERGFVHFP
     THLPSTVYAE VHKSHTIQVE VEAYPQPSIV WLKNNKTLTM ESSSEFTITS RNLSETRYQT
     ALVLVRVKQE EGGFYTIRAS NEDDEQELSF HLQINVPAKV VDLKENSSAS SGEQTVTCSA
     EGMPQPEISW STCSDIKWCS TKGQPTRLLG NESAEIGVQT NASYHAERQL YRVNSTLQLH
     RVHEPLLLRC TVQNFLGTSS QDITLVPHAL PFKVVIISVI LALLVLTVIS LIILIVLWQK
     KPRYEIRWKV IESVSSDGHE YIYVDPMQLP YDSTWEVPRD KLVLGRTLGS GAFGRVVEAT
     AHGLSHSRST MKVAVKMLKS TARSSEKQAL MSELKIMSHL GPHLNIVNLL GACTKGGPIY
     IITEYCRYGD LVDYLHRNKH TFLQSYGDKA RQEAELYGNT PEEDHVHSHL SMSVESDGGY
     MDMSKDDSLD YVPMSDMKGE VKYADIESSN YGTPYELDSY SPSAPERTDR VTLINESPLL
     SYMDLVGFSF QVANGMEFLA SKNCVHRDLA ARNVLICEGK LVKICDFGLA RDIMRDSNYI
     SKGSTFLPLK WMAPESIFNN LYTTLSDVWS FGILLWEIFT LGGTPYPELP MNEQFYNAIK
     RGYRMSKPTH ASDEIYNIMQ KCWEEKFEIR PSFSQLVVLM GNLLVDCYRK RYQQVDEEFM
     KSDHPAVVRT RPTIPVLNNA RLAASSPSSS ILYTAVHQNG GENDYIIPLP DPKPEANCDL
     PQEASISRA
//

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