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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.
22-NOV-2017, entry version 114.
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: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME 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.
UniGene; Cfa.3909; -.
ProteinModelPortal; Q6QNF3; -.
SMR; Q6QNF3; -.
BioGrid; 140028; 1.
STRING; 9615.ENSCAFP00000000714; -.
PaxDb; Q6QNF3; -.
GeneID; 442985; -.
KEGG; cfa:442985; -.
CTD; 5159; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000112009; -.
HOVERGEN; HBG004335; -.
InParanoid; Q6QNF3; -.
KO; K05089; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB.
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: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 proliferation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
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.
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; Pkinase_Tyr; 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; 2.
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; Complete proteome;
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 {ECO:0000255}.
CHAIN 32 1103 Platelet-derived growth factor receptor
beta.
/FTId=PRO_0000041843.
TOPO_DOM 33 532 Extracellular. {ECO:0000255}.
TRANSMEM 533 553 Helical. {ECO:0000255}.
TOPO_DOM 554 1103 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 120 Ig-like C2-type 1.
DOMAIN 129 210 Ig-like C2-type 2.
DOMAIN 214 309 Ig-like C2-type 3.
DOMAIN 331 403 Ig-like C2-type 4.
DOMAIN 416 524 Ig-like C2-type 5.
DOMAIN 600 962 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 606 614 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 1062 1094 Pro-rich.
ACT_SITE 826 826 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 634 634 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 562 562 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 579 579 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 581 581 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 686 686 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000250|UniProtKB:P05622}.
MOD_RES 716 716 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 740 740 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 751 751 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 763 763 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 771 771 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 775 775 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 778 778 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 857 857 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 934 934 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000250|UniProtKB:P05622}.
MOD_RES 970 970 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000250|UniProtKB:P05622}.
MOD_RES 1009 1009 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 1021 1021 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
CARBOHYD 45 45 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 371 371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 479 479 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 100 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 149 190 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 235 291 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 436 508 {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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