ID A0A8I3N488_CANLF Unreviewed; 1135 AA.
AC A0A8I3N488;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=Platelet-derived growth factor receptor beta {ECO:0000256|ARBA:ARBA00020507, ECO:0000256|PIRNR:PIRNR500948};
DE Short=PDGF-R-beta {ECO:0000256|PIRNR:PIRNR500948};
DE Short=PDGFR-beta {ECO:0000256|PIRNR:PIRNR500948};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902, ECO:0000256|PIRNR:PIRNR500948};
DE AltName: Full=Beta platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500948};
DE AltName: Full=Beta-type platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500948};
GN Name=PDGFRB {ECO:0000313|Ensembl:ENSCAFP00845011249.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00845011249.1, ECO:0000313|Proteomes:UP000805418};
RN [1] {ECO:0000313|Ensembl:ENSCAFP00845011249.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Labrador retriever {ECO:0000313|Ensembl:ENSCAFP00845011249.1};
RA Eory L., Zhang W., Schoenebeck J.;
RT "Long-read based genome assembly of a Labrador retriever dog.";
RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCAFP00845011249.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845011249.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSCAFP00845011249.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845011249.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA
CC and PDGFB, and plays an essential role in the regulation of embryonic
CC development, cell proliferation, survival, differentiation, chemotaxis
CC and migration. Plays an essential role in blood vessel development by
CC promoting proliferation, migration and recruitment of pericytes and
CC smooth muscle cells to endothelial cells.
CC {ECO:0000256|PIRNR:PIRNR500948}.
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 ECO:0000256|PIRNR:PIRNR500948};
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|PIRNR:PIRNR500948};
CC Single-pass type I membrane protein {ECO:0000256|PIRNR:PIRNR500948}.
CC Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541,
CC ECO:0000256|PIRNR:PIRNR500948}. Lysosome lumen
CC {ECO:0000256|PIRNR:PIRNR500948}. 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|PIRNR:PIRNR500948, ECO:0000256|RuleBase:RU000311}.
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DR AlphaFoldDB; A0A8I3N488; -.
DR FunCoup; A0A8I3N488; 252.
DR Ensembl; ENSCAFT00845014520.1; ENSCAFP00845011249.1; ENSCAFG00845008241.1.
DR GeneTree; ENSGT00940000157138; -.
DR OrthoDB; 9936425at2759; -.
DR Reactome; R-CFA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CFA-186763; Downstream signal transduction.
DR Reactome; R-CFA-186797; Signaling by PDGF.
DR Reactome; R-CFA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-CFA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Proteomes; UP000805418; Chromosome 4.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0160185; F:phospholipase C activator activity; IEA:Ensembl.
DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IBA:GO_Central.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IBA:GO_Central.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IBA:GO_Central.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
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:000814; 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; IPR027288; PGFRB.
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; PF13927; Ig_3; 1.
DR Pfam; PF25305; Ig_PDGFR_d4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500948; Beta-PDGF_receptor; 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; 2.
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|PIRNR:PIRNR500948};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR500948};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PIRNR:PIRNR500948};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|PIRNR:PIRNR500948};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|PIRNR:PIRNR500948};
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR500948};
KW Lysosome {ECO:0000256|ARBA:ARBA00023228, ECO:0000256|PIRNR:PIRNR500948};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR500948};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR500948};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR500948};
KW Reference proteome {ECO:0000313|Proteomes:UP000805418};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR500948};
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 ECO:0000256|PIRNR:PIRNR500948};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 563..587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..132
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 245..338
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 631..993
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..13
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1107
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 857
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 610
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 637..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500948-2"
FT BINDING 638..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 713..719
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 861
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 862
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 875
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 1001
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1135 AA; 126303 MW; 8FB34CED9A6EA1AF CRC64;
MRGQRGGLPG GGDSPELRTV PTPEGISSKD TMQVPGTMPA PVLKGQALWL PLLLMLSPQA
SSGLVITPPG PELVLNISST FVLTCSGPAP VVWERLSQEP LQKMARTQDG TFSSTLTLTN
VTGLDTGEYF CTYKGSHGLE PDGRKRLYIF VPDPTMGFLP VDPEELFIFL TEITEITIPC
RVTDPRLVVT LHEKKVDIPL PIPYDHQRGF SGTFEDKTYV CKTTIGDKEV DSEAYYVYSL
QVSSINVSVN AVQTVVRQGE NITIMCIVTG NEVVNFEWTY PRMESGRLVE PVTDFLFNVP
SHIRSILHIP SAELGDSGTY ICNVSESVND HRDEKSINVT VVESGYVRLL GELDAVQFAE
LHRSRALQVV FEAYPPPTVV WFKDNRTLGD SSAGEIALST RNVSETRYVS ELTLVRVKVA
EAGYYTMRAF HEDAEAQLSF QLQVNVPVRV LELSESHPAS GEQTVRCRGR GMPQPHLTWS
TCSDLKRCPR ELPPTPLGNS SEEESQLETN VTYWPEDQEF EVVSTLRLRR VDQPLSVRCT
LHNLLGHDMQ EVTVVPHSLP FKVVVISAIL ALVVLTIISL IILIMLWQKK PRYEIRWKVI
ESVSSDGHEY IYVDPMQLPY DSTWELPRDQ LVLGRTLGSG AFGQVVEATA HGLSHSQATM
KVAVKMLKST ARSSEKQALM SELKIMSHLG PHLNVVNLLG ACTKGGPIYI ITEYCRYGDL
VDYLHRNKHT FLQLCSDKRR PPSAELYSNA LPAGLPLPSH VSLPGESDGG YMDMSKDESV
DYVPMLDMKG GVKYADIESS SYMAPYDNYV PTAPERTCRA TLINESPVLS YTDLVGFSYQ
VANGMEFLAS KNCVHRDLAA RNVLICEGKL VKICDFGLAR DIMRDSNYIS KGSTFLPLKW
MAPESIFNSL YTTLSDVWSF GILLWEIFTL GGTPYPELPM NEQFYNAIKR GYRMAQPAHA
SDEIYEIMQK CWEEKFEIRP PFSQLVLLLE RLLGEGYKKK YQQVDEEFLR SDHPAVLRSQ
ARLPGFPGLR SPLDTSSVLY TAVQPNEGDN DYIIPLPDPK PEVADDGPLE SSPSLASSTL
NEVNTSSTIS CDSPLEPQEE PEPEPEPQPE PQVVPEPPLD SSCPGPRAEA EDSFL
//
