ID A0A8M1FSJ6_URSMA Unreviewed; 1048 AA.
AC A0A8M1FSJ6;
DT 03-AUG-2022, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
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|RefSeq:XP_040486348.1};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_040486348.1};
RN [1] {ECO:0000313|RefSeq:XP_040486348.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_040486348.1};
RG RefSeq;
RL Submitted (AUG-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 RefSeq; XP_040486348.1; XM_040630414.1.
DR AlphaFoldDB; A0A8M1FSJ6; -.
DR GeneID; 103664600; -.
DR CTD; 5159; -.
DR Proteomes; UP000261680; Unplaced.
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:InterPro.
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: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:UP000261680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
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 SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1048
FT /note="Platelet-derived growth factor receptor beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035462523"
FT TRANSMEM 532..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..101
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 214..307
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 600..962
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1019..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 826
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 579
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 606..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500948-2"
FT BINDING 607..614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 682..688
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 830
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 831
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 844
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 970
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1048 AA; 117552 MW; 59A2EA7F3F12208D CRC64;
MQLPSAVPAP VLKGQVLLLP LLLLLGPQAS WGLVISPPGP ELILNVSSNF VLTCSGPAPV
VWERMSQEPL QKMAKTQDGT FSSTLTLTNV SGIDTGEYFC TYKGSHGLEP GERKRLYIFV
PDPLMGFLPV DPEELFIFLT EITEITIPCR VTDPRLVVTL HEKKVDIPLP IPYDHQRGFS
GTFEDKTYVC KTTIGDKEVD SEAYYVYSLQ VSSINVSVNA VQTVVRQGEN ITIMCIVTGN
EVVNFEWTYP RMESGRLVEP VTDFLFNMPS HIRSILHIPS AELGDSGTYI CNVSESVNEH
RDEKSINVTV VESGYVRLLG ELDAIQFAEL HRSRTLQVVF EAYPPPTVMW FKDNRTLGDS
SAGEISLSTR NVSETRYVSE LTLVRVKVAE AGCYTMRAFH EDAEAQLSFQ LQVNVPVRVL
ELSENHPASG EQTVRCRGRG MPQPHLTWST CSDLKRCPRE LPPTPLGNSS EEESQLETNV
TYWPEEQEFE VVSTLRLRRV DQPLSVRCTL HNLLGHDMQE VTVVPHSLPF KVVVISAILA
LVVLTIISLI ILVMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL
VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS ELKIMSHLGP
HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF LQRCPDKRRP PSAELYSNAL
PGDLPLPSHV SLPRESDGGY MDMSKDESVD YVPMLAMKGG VKYADIESSS YMAPYDNYVP
TAPERTCRAT LINESPVLSY TDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV
KICDFGLARD IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG
GTPYPELPMN DQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP FSQLVLLLER
LLGEGYKKKY QQVDEEFLRS DHPAVLRSQA RLPGFHGLRS PLDTSSVLYT AVQPNEGDND
YIIPLPDPKP EVADEGPLES SPSLARLQ
//
