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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_MOUSE             Reviewed;        1098 AA.
P05622;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
30-AUG-2017, entry version 190.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Fibroblast;
PubMed=3020426; DOI=10.1038/323226a0;
Yarden Y., Escobedo J.A., Kuang W.-J., Yang-Feng T.L., Daniel T.O.,
Tremble P.M., Chen E.Y., Ando M.E., Harkins R.N., Francke U.,
Fried V.A., Ullrich A., Williams L.T.;
"Structure of the receptor for platelet-derived growth factor helps
define a family of closely related growth factor receptors.";
Nature 323:226-232(1986).
[2]
FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBUNIT, AND
AUTOPHOSPHORYLATION.
PubMed=8440729;
Seifert R.A., van Koppen A., Bowen-Pope D.F.;
"PDGF-AB requires PDGF receptor alpha-subunits for high-affinity, but
not for low-affinity, binding and signal transduction.";
J. Biol. Chem. 268:4473-4480(1993).
[3]
DISRUPTION PHENOTYPE.
PubMed=7958864; DOI=10.1101/gad.8.16.1888;
Soriano P.;
"Abnormal kidney development and hematological disorders in PDGF beta-
receptor mutant mice.";
Genes Dev. 8:1888-1896(1994).
[4]
INTERACTION WITH GRB10.
PubMed=10454568; DOI=10.1128/MCB.19.9.6217;
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
Swamy O.R., Leone M.E., Riedel H.;
"Grb10, a positive, stimulatory signaling adapter in platelet-derived
growth factor BB-, insulin-like growth factor I-, and insulin-mediated
mitogenesis.";
Mol. Cell. Biol. 19:6217-6228(1999).
[5]
TISSUE SPECIFICITY.
PubMed=14514732; DOI=10.1097/01.ASN.0000089828.73014.C8;
Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G.,
Ophascharoensuk V., Truong L., Johnson R.J., Alpers C.E.;
"Obstructive uropathy in mice and humans: potential role for PDGF-D in
the progression of tubulointerstitial injury.";
J. Am. Soc. Nephrol. 14:2544-2555(2003).
[6]
FUNCTION, AND MUTAGENESIS OF TYR-578; TYR-715; TYR-739; TYR-750;
TYR-770; TYR-1008 AND TYR-1020.
PubMed=14624252; DOI=10.1371/journal.pbio.0000052;
Tallquist M.D., French W.J., Soriano P.;
"Additive effects of PDGF receptor beta signaling pathways in vascular
smooth muscle cell development.";
PLoS Biol. 1:E52-E52(2003).
[7]
REVIEW ON FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15207813; DOI=10.1016/j.cytogfr.2004.03.005;
Betsholtz C.;
"Insight into the physiological functions of PDGF through genetic
studies in mice.";
Cytokine Growth Factor Rev. 15:215-228(2004).
[8]
MUTAGENESIS OF ASP-849, CATALYTIC ACTIVITY, FUNCTION, AND INTERACTION
WITH PIK3R1.
PubMed=15284236; DOI=10.1074/jbc.M406051200;
Chiara F., Goumans M.J., Forsberg H., Ahgren A., Rasola A.,
Aspenstrom P., Wernstedt C., Hellberg C., Heldin C.H., Heuchel R.;
"A gain of function mutation in the activation loop of platelet-
derived growth factor beta-receptor deregulates its kinase activity.";
J. Biol. Chem. 279:42516-42527(2004).
[9]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
PubMed=14966296; DOI=10.1128/MCB.24.5.2190-2201.2004;
Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B.,
Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H.,
Roennstrand L., Ostman A., Hellberg C.;
"Site-selective regulation of platelet-derived growth factor beta
receptor tyrosine phosphorylation by T-cell protein tyrosine
phosphatase.";
Mol. Cell. Biol. 24:2190-2201(2004).
[10]
FUNCTION, AND PHOSPHORYLATION AT TYR-685; TYR-933 AND TYR-969.
PubMed=14993293; DOI=10.1128/MCB.24.6.2573-2583.2004;
Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
"Bidirectional signaling links the Abelson kinases to the platelet-
derived growth factor receptor.";
Mol. Cell. Biol. 24:2573-2583(2004).
[11]
INTERACTION WITH CBL, AND UBIQUITINATION.
PubMed=15753096; DOI=10.1074/jbc.M410265200;
Takayama Y., May P., Anderson R.G., Herz J.;
"Low density lipoprotein receptor-related protein 1 (LRP1) controls
endocytosis and c-CBL-mediated ubiquitination of the platelet-derived
growth factor receptor beta (PDGFR beta).";
J. Biol. Chem. 280:18504-18510(2005).
[12]
INTERACTION WITH CBL AND PLCG1, AND FUNCTION.
PubMed=17620338; DOI=10.1074/jbc.M701797200;
Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P.,
Druker B.J., Naramura M., Band V., Band H.;
"Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-
derived growth factor receptor beta provides a dual mechanism of
negative regulation.";
J. Biol. Chem. 282:29336-29347(2007).
[13]
FUNCTION.
PubMed=18948621; DOI=10.1161/CIRCRESAHA.108.176768;
Mellgren A.M., Smith C.L., Olsen G.S., Eskiocak B., Zhou B.,
Kazi M.N., Ruiz F.R., Pu W.T., Tallquist M.D.;
"Platelet-derived growth factor receptor beta signaling is required
for efficient epicardial cell migration and development of two
distinct coronary vascular smooth muscle cell populations.";
Circ. Res. 103:1393-1401(2008).
[14]
DISRUPTION PHENOTYPE.
PubMed=18213589; DOI=10.1002/dvdy.21436;
Van den Akker N.M., Winkel L.C., Nisancioglu M.H., Maas S.,
Wisse L.J., Armulik A., Poelmann R.E., Lie-Venema H., Betsholtz C.,
Gittenberger-de Groot A.C.;
"PDGF-B signaling is important for murine cardiac development: its
role in developing atrioventricular valves, coronaries, and cardiac
innervation.";
Dev. Dyn. 237:494-503(2008).
[15]
FUNCTION.
PubMed=19030102; DOI=10.1371/journal.pone.0003794;
Wu E., Palmer N., Tian Z., Moseman A.P., Galdzicki M., Wang X.,
Berger B., Zhang H., Kohane I.S.;
"Comprehensive dissection of PDGF-PDGFR signaling pathways in PDGFR
genetically defined cells.";
PLoS ONE 3:E3794-E3794(2008).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-306; ASN-312; ASN-467 AND
ASN-478.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[17]
FUNCTION, AND INTERACTION WITH PIK3R1.
PubMed=19742316; DOI=10.1371/journal.pone.0006922;
Zhou L., Takayama Y., Boucher P., Tallquist M.D., Herz J.;
"LRP1 regulates architecture of the vascular wall by controlling
PDGFRbeta-dependent phosphatidylinositol 3-kinase activation.";
PLoS ONE 4:E6922-E6922(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[19]
FUNCTION.
PubMed=21664579; DOI=10.1016/j.devcel.2011.04.019;
Olson L.E., Soriano P.;
"PDGFRbeta signaling regulates mural cell plasticity and inhibits fat
development.";
Dev. Cell 20:815-826(2011).
[20]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1005-1015 IN COMPLEX WITH
PTPN11, AND INTERACTION WITH PTPN11.
PubMed=7521735; DOI=10.1016/S0969-2126(00)00044-7;
Lee C.-H., Kominos D., Jacques S., Margolis B., Schlessinger J.,
Shoelson S.E., Kuriyan J.;
"Crystal structures of peptide complexes of the amino-terminal SH2
domain of the Syp tyrosine phosphatase.";
Structure 2:423-438(1994).
-!- 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 (By similarity). 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. {ECO:0000250,
ECO:0000269|PubMed:14624252, ECO:0000269|PubMed:14993293,
ECO:0000269|PubMed:15284236, ECO:0000269|PubMed:17620338,
ECO:0000269|PubMed:18948621, ECO:0000269|PubMed:19030102,
ECO:0000269|PubMed:19742316, ECO:0000269|PubMed:21664579,
ECO:0000269|PubMed:8440729}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:15284236}.
-!- 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.
-!- 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}.
-!- INTERACTION:
P39688:Fyn; NbExp=3; IntAct=EBI-1554855, EBI-524514;
P18031:PTPN1 (xeno); NbExp=3; IntAct=EBI-1554855, EBI-968788;
Q9JHL1:Slc9a3r2; NbExp=2; IntAct=EBI-1554855, EBI-538451;
Q91YD9:Wasl; NbExp=2; IntAct=EBI-1554855, EBI-642417;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cytoplasmic vesicle {ECO:0000250}. Lysosome lumen
{ECO:0000250}. Note=After ligand binding, the autophosphorylated
receptor is ubiquitinated and internalized, leading to its
degradation.
-!- TISSUE SPECIFICITY: Weakly expressed in glomerular mesangial cells
and interstitial cells. Up-regulated in areas of renal fibrosis.
In mice with unilateral ureteral obstruction, increased expression
in interstitial cells at day 4 and expression is markedly elevated
at day 7 and is maximal at day 14. {ECO:0000269|PubMed:14514732}.
-!- 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-578, and to a lesser degree, Tyr-
580 is important for interaction with SRC. Phosphorylation at Tyr-
715 is important for interaction with GRB2. Phosphorylation at
Tyr-739 and Tyr-750 is important for interaction with PIK3R1.
Phosphorylation at Tyr-750 is important for interaction with NCK1.
Phosphorylation at Tyr-770 and Tyr-856 is important for
interaction with RASA1/GAP. Phosphorylation at Tyr-856 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-1008 is important for
interaction with PTPN11. Phosphorylation at Tyr-1008 and Tyr-1020
is important for interaction with PLCG1. Dephosphorylated by PTPRJ
at Tyr-750, Tyr-856, Tyr-1008 and Tyr-1020 (By similarity).
Dephosphorylated by PTPN2 at Tyr-578 and Tyr-1020. {ECO:0000250}.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
polyubiquitinated, leading to its degradation.
{ECO:0000269|PubMed:15753096}.
-!- DISRUPTION PHENOTYPE: No apparent phenotype up to 16 dpc.
Lethality late during gestation or at birth, due to widespread
bleedings. This is due to a severe shortage of vascular smooth
muscle cells and pericytes, especially in the central nervous
system, skin, lung and heart. Mutants suffer from hemorrhages,
anemia, thrombocytopenia, and show defects in the formation of
kidney glomeruli, due to a lack of mesangial cells.
{ECO:0000269|PubMed:15207813, ECO:0000269|PubMed:18213589,
ECO:0000269|PubMed:7958864}.
-!- 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; X04367; CAA27882.1; -; mRNA.
PIR; A25742; PFMSRB.
RefSeq; NP_001139740.1; NM_001146268.1.
RefSeq; NP_032835.2; NM_008809.2.
UniGene; Mm.4146; -.
PDB; 1AYA; X-ray; 2.05 A; P/Q=1005-1015.
PDB; 1AYC; X-ray; 2.30 A; P=736-744.
PDBsum; 1AYA; -.
PDBsum; 1AYC; -.
ProteinModelPortal; P05622; -.
SMR; P05622; -.
BioGrid; 202089; 5.
DIP; DIP-39669N; -.
IntAct; P05622; 13.
MINT; MINT-2832882; -.
STRING; 10090.ENSMUSP00000025522; -.
BindingDB; P05622; -.
ChEMBL; CHEMBL2749; -.
GuidetoPHARMACOLOGY; 1804; -.
iPTMnet; P05622; -.
PhosphoSitePlus; P05622; -.
MaxQB; P05622; -.
PaxDb; P05622; -.
PRIDE; P05622; -.
GeneID; 18596; -.
KEGG; mmu:18596; -.
UCSC; uc008fbk.2; mouse.
CTD; 5159; -.
MGI; MGI:97531; Pdgfrb.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
HOVERGEN; HBG004335; -.
InParanoid; P05622; -.
KO; K05089; -.
PhylomeDB; P05622; -.
BRENDA; 2.7.10.1; 3474.
EvolutionaryTrace; P05622; -.
PRO; PR:P05622; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; ISO:MGI.
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:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; IMP:MGI.
GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB.
GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IDA:MGI.
GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:MGI.
GO; GO:0030325; P:adrenal gland development; IGI:MGI.
GO; GO:0035909; P:aorta morphogenesis; IGI:BHF-UCL.
GO; GO:0001568; P:blood vessel development; IEP:UniProtKB.
GO; GO:0055003; P:cardiac myofibril assembly; IGI:UniProtKB.
GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISO:MGI.
GO; GO:0060981; P:cell migration involved in coronary angiogenesis; IMP:UniProtKB.
GO; GO:0035441; P:cell migration involved in vasculogenesis; IMP:UniProtKB.
GO; GO:0048568; P:embryonic organ development; IEP:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0072277; P:metanephric glomerular capillary formation; IGI:UniProtKB.
GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; IMP:UniProtKB.
GO; GO:0072223; P:metanephric glomerular mesangium development; IEP:UniProtKB.
GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:MGI.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
GO; GO:0090280; P:positive regulation of calcium ion import; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:BHF-UCL.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:UniProtKB.
GO; GO:0007165; P:signal transduction; IDA:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0071670; P:smooth muscle cell chemotaxis; IGI:BHF-UCL.
GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom.
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; 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; 4.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 3.
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.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell membrane; Chemotaxis;
Complete proteome; Cytoplasmic vesicle; Developmental protein;
Direct protein sequencing; 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
CHAIN 32 1098 Platelet-derived growth factor receptor
beta.
/FTId=PRO_0000016758.
TOPO_DOM 32 531 Extracellular. {ECO:0000255}.
TRANSMEM 532 552 Helical. {ECO:0000255}.
TOPO_DOM 553 1098 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 119 Ig-like C2-type 1.
DOMAIN 128 209 Ig-like C2-type 2.
DOMAIN 213 308 Ig-like C2-type 3.
DOMAIN 330 402 Ig-like C2-type 4.
DOMAIN 415 523 Ig-like C2-type 5.
DOMAIN 599 961 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 605 613 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 825 825 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 633 633 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 561 561 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 578 578 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 580 580 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 685 685 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000269|PubMed:14993293}.
MOD_RES 715 715 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 739 739 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 750 750 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 762 762 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 770 770 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 774 774 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 777 777 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 856 856 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 933 933 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000269|PubMed:14993293}.
MOD_RES 969 969 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000269|PubMed:14993293}.
MOD_RES 1008 1008 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
MOD_RES 1020 1020 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P09619}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 312 312 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19656770}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 467 467 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
DISULFID 53 99 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 148 189 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 234 290 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 435 507 {ECO:0000255|PROSITE-ProRule:PRU00114}.
MUTAGEN 578 578 Y->F: Strongly reduced levels of vascular
smooth muscle cells and pericytes in
developing blood vessels; when associated
with F-715; F-739; F-750; F-770; F-1008
and F-1020.
{ECO:0000269|PubMed:14624252}.
MUTAGEN 715 715 Y->F: Strongly reduced levels of vascular
smooth muscle cells and pericytes in
developing blood vessels; when associated
with F-578; F-739; F-750; F-770; F-1008
and F-1020.
{ECO:0000269|PubMed:14624252}.
MUTAGEN 739 739 Y->F: Strongly reduced levels of vascular
smooth muscle cells and pericytes in
developing blood vessels; when associated
with F-578; F-715; F-750; F-770; F-1008
and F-1020.
{ECO:0000269|PubMed:14624252}.
MUTAGEN 750 750 Y->F: Strongly reduced levels of vascular
smooth muscle cells and pericytes in
developing blood vessels; when associated
with F-578; F-715; F-739; F-770; F-1008
and F-1020.
{ECO:0000269|PubMed:14624252}.
MUTAGEN 770 770 Y->F: Strongly reduced levels of vascular
smooth muscle cells and pericytes in
developing blood vessels; when associated
with F-578; F-715; F-739; F-750; F-1008
and F-1020.
{ECO:0000269|PubMed:14624252}.
MUTAGEN 849 849 D->N: Increased autophosphorylation in
the absence of PDGFB binding. Increased
autophosphorylation in response to PDGFB
binding. Constitutive interaction with
PIK3R1, and constitutive AKT1 activation.
{ECO:0000269|PubMed:15284236}.
MUTAGEN 1008 1008 Y->F: Strongly reduced levels of vascular
smooth muscle cells and pericytes in
developing blood vessels; when associated
with F-578; F-715; F-739; F-750; F-770
and F-1020.
{ECO:0000269|PubMed:14624252}.
MUTAGEN 1020 1020 Y->F: Strongly reduced levels of vascular
smooth muscle cells and pericytes in
developing blood vessels; when associated
with F-578; F-715; F-739; F-750; F-770
and F-1008.
{ECO:0000269|PubMed:14624252}.
SEQUENCE 1098 AA; 122806 MW; 8D391CAFAC3FC31D CRC64;
MGLPGVIPAL VLRGQLLLSV LWLLGPQTSR GLVITPPGPE FVLNISSTFV LTCSGSAPVM
WEQMSQVPWQ EAAMNQDGTF SSVLTLTNVT GGDTGEYFCV YNNSLGPELS ERKRIYIFVP
DPTMGFLPMD SEDLFIFVTD VTETTIPCRV TDPQLEVTLH EKKVDIPLHV PYDHQRGFTG
TFEDKTYICK TTIGDREVDS DTYYVYSLQV SSINVSVNAV QTVVRQGESI TIRCIVMGND
VVNFQWTYPR MKSGRLVEPV TDYLFGVPSR IGSILHIPTA ELSDSGTYTC NVSVSVNDHG
DEKAINISVI ENGYVRLLET LGDVEIAELH RSRTLRVVFE AYPMPSVLWL KDNRTLGDSG
AGELVLSTRN MSETRYVSEL ILVRVKVSEA GYYTMRAFHE DDEVQLSFKL QVNVPVRVLE
LSESHPANGE QTIRCRGRGM PQPNVTWSTC RDLKRCPRKL SPTPLGNSSK EESQLETNVT
FWEEDQEYEV VSTLRLRHVD QPLSVRCMLQ NSMGGDSQEV TVVPHSLPFK VVVISAILAL
VVLTVISLII LIMLWQKKPR YEIRWKVIES VSSDGHEYIY VDPVQLPYDS TWELPRDQLV
LGRTLGSGAF GQVVEATAHG LSHSQATMKV AVKMLKSTAR SSEKQALMSE LKIMSHLGPH
LNVVNLLGAC TKGGPIYIIT EYCRYGDLVD YLHRNKHTFL QRHSNKHCPP SAELYSNALP
VGFSLPSHLN LTGESDGGYM DMSKDESIDY VPMLDMKGDI KYADIESPSY MAPYDNYVPS
APERTYRATL INDSPVLSYT DLVGFSYQVA NGMDFLASKN CVHRDLAARN VLICEGKLVK
ICDFGLARDI MRDSNYISKG STYLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL
LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR FPGIHSLRSP LDTSSVLYTA VQPNESDNDY
IIPLPDPKPD VADEGLPEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ QAEPEAQLEQ
PQDSGCPGPL AEAEDSFL


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