ID A0A6P5C6N9_BOSIN Unreviewed; 1117 AA.
AC A0A6P5C6N9;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 2.
DT 28-JAN-2026, entry version 25.
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|ARBA:ARBA00029696, ECO:0000256|PIRNR:PIRNR500948};
DE AltName: Full=Beta-type platelet-derived growth factor receptor {ECO:0000256|ARBA:ARBA00032009, ECO:0000256|PIRNR:PIRNR500948};
GN Name=PDGFRB {ECO:0000313|RefSeq:XP_019820792.2,
GN ECO:0000313|RefSeq:XP_070649943.1};
OS Bos indicus (Zebu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9915 {ECO:0000313|Proteomes:UP001652663, ECO:0000313|RefSeq:XP_019820792.2};
RN [1] {ECO:0000313|RefSeq:XP_019820792.2, ECO:0000313|RefSeq:XP_070649943.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_019820792.2,
RC ECO:0000313|RefSeq:XP_070649943.1};
RG RefSeq;
RL Submitted (MAY-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.
CC {ECO:0000256|PIRNR:PIRNR500948}.
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_019820792.2; XM_019965233.2.
DR RefSeq; XP_070649943.1; XM_070793842.1.
DR AlphaFoldDB; A0A6P5C6N9; -.
DR GeneID; 109562197; -.
DR CTD; 5159; -.
DR Proteomes; UP001652663; Chromosome 7.
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 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; 1.
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:UP001652663};
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..1117
FT /note="Platelet-derived growth factor receptor beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5045019517"
FT TRANSMEM 545..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..306
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 613..975
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1031..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 839
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 619..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR500948-2"
FT BINDING 620..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 695..701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 843
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-2"
FT BINDING 844
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 857
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT SITE 983
FT /note="Important for interaction with phosphotyrosine-
FT binding proteins"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-4"
SQ SEQUENCE 1117 AA; 125203 MW; BAE616967C929866 CRC64;
MWLPSAMQAV VLKGRVLLLP LLFLLGPQAS WGLAIIPPGP ELVLNLSSTF VLTCSGPAPV
VWERMSQKPP QEMTETQDGT FSSVLTLVNV TGLDTGEYFC GYKRSHGLEA SERKRLYIFV
PDPSVGFLPV DPEELFIFLT EITETTIPCR VTDPRLVVML HEKKVDVPLP IAYDPQRGFS
GTFEDKTYIC KTTIGDREVD SDAYHVYSLQ VSSINVSVNA VQTVVRQGEN ITIMCIVTGN
EVVNFEWTYP RMESGRLVEP VTDFLFEMPH IRSILHIPSA ELGDSGTYIC NVSESVSDHR
DEKAINVTVV ENGYVRLLGE LDPVQFAELH RSRTLQVVFE AYPPPTVMWF KDNRTLGDSS
AGEIVLSTRN VSETRYVSEL TLVRVKVAEA GYYTMRAFHE DAEAQLSFQL QVNVPVRVLE
LSESHPANGE QTVRCRGRGM PQPHLTWSTC SDLKRVGRDW KSTWPVLGRC PRELPPTPLG
NSSEEESQLE TNVTYWAEEQ EFEVVSTLRL RHVDQPLSVR CTLHNLLGYD VQEVTVVPHS
LPFKVVVISA ILALVVLTII SLIILIMLWQ KKPRYEIRWK VIESVSSDGH EYIYVDPMQL
PYDSTWELPR DQLVLGRTLG SGAFGQVVEA TAHGLSHSQA TMKVAVKMLK STARSSEKQA
LMSELKIMSH LGPHLNVVNL LGACTKGGPI YIITEYCRYG DLVDYLHRNK HTFLQRCSDK
RRPPSAELYS NALPVGLPLP SHVSLPGESD GGYMDMSKDE SVDYVPMLDM KGDVKYADIE
SSNYMAPYDN YVPSAPERTC RVTLINESPV LSYTDLVGFS YQVANGMEFL ASKNCVHRDL
AARNVLICEG KLVKICDFGL ARDIMRDSNY ISKGSTFLPL KWMAPESIFN SLYTTLSDVW
SFGILLWEIF TLGGTPYPEL PMNEQFYNAI KRGYRMAQPA HASDEIYEIM QKCWEEKFEI
RPPFSQLVLL LERLLGEGYK KKYQQVDEEF LRSDHPAILR SQARLPGFNG LRSPLDSSSV
LYTAVQPNEG DNDYIIPLPD PKPEVADEGP LEGSPSLASS TLNEVNTSST ISCDSPLEPQ
EEPEPELQPA SQVEPEPKWP PDSSCPGPRA EAEDSFL
//
