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Platelet-derived growth factor receptor beta (PDGF-R-beta) (PDGFR-beta) (EC 2.7.10.1) (Beta platelet-derived growth factor receptor) (Beta-type platelet-derived growth factor receptor) (CD140 antigen-like family member B) (Platelet-derived growth factor receptor 1) (PDGFR-1) (CD antigen CD140b)

 PGFRB_CANLF             Reviewed;        1103 AA.
Q6QNF3;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
07-APR-2021, entry version 131.
RecName: Full=Platelet-derived growth factor receptor beta;
Short=PDGF-R-beta;
Short=PDGFR-beta;
EC=2.7.10.1;
AltName: Full=Beta platelet-derived growth factor receptor;
AltName: Full=Beta-type platelet-derived growth factor receptor;
AltName: Full=CD140 antigen-like family member B;
AltName: Full=Platelet-derived growth factor receptor 1;
Short=PDGFR-1;
AltName: CD_antigen=CD140b;
Flags: Precursor;
Name=PDGFRB; Synonyms=PDGFR, PDGFR1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Liao A.T., Chien M.B., London C.A.;
"Characterization of PDGFb on the histiocytic sarcoma.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA
and PDGFB, and plays an essential role in the regulation of embryonic
development, cell proliferation, survival, differentiation, chemotaxis
and migration. Plays an essential role in blood vessel development by
promoting proliferation, migration and recruitment of pericytes and
smooth muscle cells to endothelial cells. Plays a role in the migration
of vascular smooth muscle cells and the formation of neointima at
vascular injury sites. Required for normal development of the
cardiovascular system. Required for normal recruitment of pericytes
(mesangial cells) in the kidney glomerulus, and for normal formation of
a branched network of capillaries in kidney glomeruli. Promotes
rearrangement of the actin cytoskeleton and the formation of membrane
ruffles. Binding of its cognate ligands - homodimeric PDGFB,
heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to
the activation of several signaling cascades; the response depends on
the nature of the bound ligand and is modulated by the formation of
heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1,
PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the
production of the cellular signaling molecules diacylglycerol and
inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the
activation of protein kinase C. Phosphorylation of PIK3R1, the
regulatory subunit of phosphatidylinositol 3-kinase, leads to the
activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or
of the C-terminus of PTPN11, creates a binding site for GRB2, resulting
in the activation of HRAS, RAF1 and down-stream MAP kinases, including
MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation
of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and
STAM. Receptor signaling is down-regulated by protein phosphatases that
dephosphorylate the receptor and its down-stream effectors, and by
rapid internalization of the activated receptor (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
-!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization
and activation by autophosphorylation on tyrosine residues (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
heterodimers formed by PDGFA and PDGFB. May also interact with
homodimeric PDGFC. Monomer in the absence of bound ligand. Interaction
with homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
homodimeric PDGFD, leads to receptor dimerization, where both PDGFRA
homodimers and heterodimers with PDGFRB are observed. Interacts with
SH2B2/APS. Interacts directly (tyrosine phosphorylated) with SHB.
Interacts (tyrosine phosphorylated) with PIK3R1 and RASA1. Interacts
(tyrosine phosphorylated) with CBL. Interacts (tyrosine phosphorylated)
with SRC and SRC family kinases. Interacts (tyrosine phosphorylated)
with PIK3C2B, maybe indirectly. Interacts (tyrosine phosphorylated)
with SHC1, GRB7, GRB10 and NCK1. Interaction with GRB2 is mediated by
SHC1. Interacts (via C-terminus) with SLC9A3R1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}.
Lysosome lumen {ECO:0000250}. Note=After ligand binding, the
autophosphorylated receptor is ubiquitinated and internalized, leading
to its degradation. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
polyubiquitinated, leading to its degradation (By similarity).
{ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
receptor phosphorylates tyrosine residues on the other subunit.
Phosphorylation at Tyr-579, and to a lesser degree, Tyr-581 is
important for interaction with SRC. Phosphorylation at Tyr-716 is
important for interaction with GRB2. Phosphorylation at Tyr-740 and
Tyr-751 is important for interaction with PIK3R1. Phosphorylation at
Tyr-751 is important for interaction with NCK1. Phosphorylation at Tyr-
771 and Tyr-857 is important for interaction with RASA1/GAP.
Phosphorylation at Tyr-857 is important for efficient phosphorylation
of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1,
MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased
cell proliferation. Phosphorylation at Tyr-1009 is important for
interaction with PTPN11. Phosphorylation at Tyr-1009 and Tyr-1021 is
important for interaction with PLCG1. Dephosphorylated by PTPRJ at Tyr-
751, Tyr-857, Tyr-1009 and Tyr-1021 (By similarity). Dephosphorylated
by PTPN2 at Tyr-579 and Tyr-1021 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
---------------------------------------------------------------------------
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EMBL; AY532634; AAS48371.1; -; mRNA.
RefSeq; NP_001003382.1; NM_001003382.1.
RefSeq; XP_005618929.1; XM_005618872.2.
RefSeq; XP_005618930.1; XM_005618873.2.
BMRB; Q6QNF3; -.
BioGRID; 140028; 1.
STRING; 9612.ENSCAFP00000000714; -.
PaxDb; Q6QNF3; -.
PRIDE; Q6QNF3; -.
GeneID; 442985; -.
KEGG; cfa:442985; -.
CTD; 5159; -.
eggNOG; KOG0200; Eukaryota.
InParanoid; Q6QNF3; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB.
GO; GO:0048407; F:platelet-derived growth factor binding; IBA:GO_Central.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0060981; P:cell migration involved in coronary angiogenesis; ISS:UniProtKB.
GO; GO:0035441; P:cell migration involved in vasculogenesis; ISS:UniProtKB.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0046488; P:phosphatidylinositol metabolic process; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027288; PGFRB.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF07679; I-set; 1.
Pfam; PF00047; ig; 1.
Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Chemotaxis; Cytoplasmic vesicle;
Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
Kinase; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1..31
/evidence="ECO:0000255"
CHAIN 32..1103
/note="Platelet-derived growth factor receptor beta"
/id="PRO_0000041843"
TOPO_DOM 33..532
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 533..553
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 554..1103
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 33..120
/note="Ig-like C2-type 1"
DOMAIN 129..210
/note="Ig-like C2-type 2"
DOMAIN 214..309
/note="Ig-like C2-type 3"
DOMAIN 331..403
/note="Ig-like C2-type 4"
DOMAIN 416..524
/note="Ig-like C2-type 5"
DOMAIN 600..962
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 606..614
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
COMPBIAS 1062..1094
/note="Pro-rich"
ACT_SITE 826
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
BINDING 634
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 562
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 579
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 581
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 686
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000250|UniProtKB:P05622"
MOD_RES 716
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 740
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 751
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 763
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 771
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 775
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 778
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 857
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 934
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000250|UniProtKB:P05622"
MOD_RES 970
/note="Phosphotyrosine; by ABL1 and ABL2"
/evidence="ECO:0000250|UniProtKB:P05622"
MOD_RES 1009
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
MOD_RES 1021
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P09619"
CARBOHYD 45
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 89
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 215
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 230
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 292
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 307
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 354
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 371
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 468
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 479
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 54..100
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 149..190
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 235..291
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
DISULFID 436..508
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SEQUENCE 1103 AA; 123022 MW; A3D66E78A34C5FE0 CRC64;
MQVPGTMPAP VLKGQALWLP LLLMLSPQAS GGLVITPPGP ELVLNISSTF VLTCSGPAPV
VWERLSQEPL QKMARTQDGT FSSTLTLTNV TGLDTGEYFC TYKGSHGLEP DGRKRLYIFV
PDPTMGFLPV DPEELFIFLT EITEITIPCR VTDPRLVVTL HEKKVDIPLP IPYDHQRGFS
GTFEDKTYVC KTTIGDKEVD SEAYYVYSLQ VSSINVSVNA VQTVVRQGEN ITIMCIVTGN
EVVNFEWTYP RMESGRLVEP VTDFLFNVPS HIRSILHIPS AELGDSGTYI CNVSESVNDH
RDEKSINVTV VESGYVRLLG ELDAVQFAEL HRSRALQVVF EAYPPPTVVW FKDNRTLGDS
SAGEIALSTR NVSETRYVSE LTLVRVKVAE AGYYTMRAFH EDAEAQLSFQ LQVNVPVRVL
ELSESHPASG EQTVRCRGRG MPQPHLTWST CSDLKRCPRE LPPTPLGNSS EEESQLETNV
TYWPEDQEFE VVSTLRLRRV DQPLSVRCTL HNLLGHDMQE VTVVPHSLPF KVVVISAILA
LVVLTIISLI ILIMLWQKKP RYEIRWKVIE SVSSDGHEYI YVDPMQLPYD STWELPRDQL
VLGRTLGSGA FGQVVEATAH GLSHSQATMK VAVKMLKSTA RSSEKQALMS ELKIMSHLGP
HLNVVNLLGA CTKGGPIYII TEYCRYGDLV DYLHRNKHTF LQLCSDKRRP PSAELYSNAL
PAGLPLPSHV SLPGESDGGY MDMSKDESVD YVPMLDMKGG VKYADIESSS YMAPYDNYVP
TAPERTCRAT LINESPVLSY TDLVGFSYQV ANGMEFLASK NCVHRDLAAR NVLICEGKLV
KICDFGLARD IMRDSNYISK GSTFLPLKWM APESIFNSLY TTLSDVWSFG ILLWEIFTLG
GTPYPELPMN EQFYNAIKRG YRMAQPAHAS DEIYEIMQKC WEEKFEIRPP FSQLVLLLER
LLGEGYKKKY QQVDEEFLRS DHPAVLRSQA RLPGFPGLRS PLDTSSVLYT AVQPNEGDND
YIIPLPDPKP EVADGPLESS PSLASSTLNE VNTSSTISCD SPLEPQEEPE PEPEPQPEPQ
VVPEPPLDSS CPGPRAEAED SFL


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