PGFRB_MOUSE
ID PGFRB_MOUSE Reviewed; 1098 AA.
AC P05622; E9QPE2;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 2.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Platelet-derived growth factor receptor beta;
DE Short=PDGF-R-beta;
DE Short=PDGFR-beta;
DE EC=2.7.10.1;
DE AltName: Full=Beta platelet-derived growth factor receptor;
DE AltName: Full=Beta-type platelet-derived growth factor receptor;
DE AltName: Full=CD140 antigen-like family member B;
DE AltName: Full=Platelet-derived growth factor receptor 1;
DE Short=PDGFR-1;
DE AltName: CD_antigen=CD140b;
DE Flags: Precursor;
GN Name=Pdgfrb; Synonyms=Pdgfr, Pdgfr1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fibroblast;
RX PubMed=3020426; DOI=10.1038/323226a0;
RA Yarden Y., Escobedo J.A., Kuang W.-J., Yang-Feng T.L., Daniel T.O.,
RA Tremble P.M., Chen E.Y., Ando M.E., Harkins R.N., Francke U., Fried V.A.,
RA Ullrich A., Williams L.T.;
RT "Structure of the receptor for platelet-derived growth factor helps define
RT a family of closely related growth factor receptors.";
RL Nature 323:226-232(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION AS RECEPTOR FOR PDGFA AND PDGFB, SUBUNIT, AND AUTOPHOSPHORYLATION.
RX PubMed=8440729; DOI=10.1016/s0021-9258(18)53633-4;
RA Seifert R.A., van Koppen A., Bowen-Pope D.F.;
RT "PDGF-AB requires PDGF receptor alpha-subunits for high-affinity, but not
RT for low-affinity, binding and signal transduction.";
RL J. Biol. Chem. 268:4473-4480(1993).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=7958864; DOI=10.1101/gad.8.16.1888;
RA Soriano P.;
RT "Abnormal kidney development and hematological disorders in PDGF beta-
RT receptor mutant mice.";
RL Genes Dev. 8:1888-1896(1994).
RN [5]
RP INTERACTION WITH GRB10.
RX PubMed=10454568; DOI=10.1128/mcb.19.9.6217;
RA Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
RA Swamy O.R., Leone M.E., Riedel H.;
RT "Grb10, a positive, stimulatory signaling adapter in platelet-derived
RT growth factor BB-, insulin-like growth factor I-, and insulin-mediated
RT mitogenesis.";
RL Mol. Cell. Biol. 19:6217-6228(1999).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=14514732; DOI=10.1097/01.asn.0000089828.73014.c8;
RA Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V.,
RA Truong L., Johnson R.J., Alpers C.E.;
RT "Obstructive uropathy in mice and humans: potential role for PDGF-D in the
RT progression of tubulointerstitial injury.";
RL J. Am. Soc. Nephrol. 14:2544-2555(2003).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF TYR-578; TYR-715; TYR-739; TYR-750; TYR-770;
RP TYR-1008 AND TYR-1020.
RX PubMed=14624252; DOI=10.1371/journal.pbio.0000052;
RA Tallquist M.D., French W.J., Soriano P.;
RT "Additive effects of PDGF receptor beta signaling pathways in vascular
RT smooth muscle cell development.";
RL PLoS Biol. 1:E52-E52(2003).
RN [8]
RP REVIEW ON FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15207813; DOI=10.1016/j.cytogfr.2004.03.005;
RA Betsholtz C.;
RT "Insight into the physiological functions of PDGF through genetic studies
RT in mice.";
RL Cytokine Growth Factor Rev. 15:215-228(2004).
RN [9]
RP MUTAGENESIS OF ASP-849, CATALYTIC ACTIVITY, FUNCTION, AND INTERACTION WITH
RP PIK3R1.
RX PubMed=15284236; DOI=10.1074/jbc.m406051200;
RA Chiara F., Goumans M.J., Forsberg H., Ahgren A., Rasola A., Aspenstrom P.,
RA Wernstedt C., Hellberg C., Heldin C.H., Heuchel R.;
RT "A gain of function mutation in the activation loop of platelet-derived
RT growth factor beta-receptor deregulates its kinase activity.";
RL J. Biol. Chem. 279:42516-42527(2004).
RN [10]
RP PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN2.
RX PubMed=14966296; DOI=10.1128/mcb.24.5.2190-2201.2004;
RA Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B.,
RA Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L.,
RA Ostman A., Hellberg C.;
RT "Site-selective regulation of platelet-derived growth factor beta receptor
RT tyrosine phosphorylation by T-cell protein tyrosine phosphatase.";
RL Mol. Cell. Biol. 24:2190-2201(2004).
RN [11]
RP FUNCTION, AND PHOSPHORYLATION AT TYR-685; TYR-933 AND TYR-969.
RX PubMed=14993293; DOI=10.1128/mcb.24.6.2573-2583.2004;
RA Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M.;
RT "Bidirectional signaling links the Abelson kinases to the platelet-derived
RT growth factor receptor.";
RL Mol. Cell. Biol. 24:2573-2583(2004).
RN [12]
RP INTERACTION WITH CBL, AND UBIQUITINATION.
RX PubMed=15753096; DOI=10.1074/jbc.m410265200;
RA Takayama Y., May P., Anderson R.G., Herz J.;
RT "Low density lipoprotein receptor-related protein 1 (LRP1) controls
RT endocytosis and c-CBL-mediated ubiquitination of the platelet-derived
RT growth factor receptor beta (PDGFR beta).";
RL J. Biol. Chem. 280:18504-18510(2005).
RN [13]
RP INTERACTION WITH CBL AND PLCG1, AND FUNCTION.
RX PubMed=17620338; DOI=10.1074/jbc.m701797200;
RA Reddi A.L., Ying G., Duan L., Chen G., Dimri M., Douillard P., Druker B.J.,
RA Naramura M., Band V., Band H.;
RT "Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived
RT growth factor receptor beta provides a dual mechanism of negative
RT regulation.";
RL J. Biol. Chem. 282:29336-29347(2007).
RN [14]
RP FUNCTION.
RX PubMed=18948621; DOI=10.1161/circresaha.108.176768;
RA Mellgren A.M., Smith C.L., Olsen G.S., Eskiocak B., Zhou B., Kazi M.N.,
RA Ruiz F.R., Pu W.T., Tallquist M.D.;
RT "Platelet-derived growth factor receptor beta signaling is required for
RT efficient epicardial cell migration and development of two distinct
RT coronary vascular smooth muscle cell populations.";
RL Circ. Res. 103:1393-1401(2008).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=18213589; DOI=10.1002/dvdy.21436;
RA Van den Akker N.M., Winkel L.C., Nisancioglu M.H., Maas S., Wisse L.J.,
RA Armulik A., Poelmann R.E., Lie-Venema H., Betsholtz C.,
RA Gittenberger-de Groot A.C.;
RT "PDGF-B signaling is important for murine cardiac development: its role in
RT developing atrioventricular valves, coronaries, and cardiac innervation.";
RL Dev. Dyn. 237:494-503(2008).
RN [16]
RP FUNCTION.
RX PubMed=19030102; DOI=10.1371/journal.pone.0003794;
RA Wu E., Palmer N., Tian Z., Moseman A.P., Galdzicki M., Wang X., Berger B.,
RA Zhang H., Kohane I.S.;
RT "Comprehensive dissection of PDGF-PDGFR signaling pathways in PDGFR
RT genetically defined cells.";
RL PLoS ONE 3:E3794-E3794(2008).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-306; ASN-467 AND ASN-478.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [18]
RP FUNCTION, AND INTERACTION WITH PIK3R1.
RX PubMed=19742316; DOI=10.1371/journal.pone.0006922;
RA Zhou L., Takayama Y., Boucher P., Tallquist M.D., Herz J.;
RT "LRP1 regulates architecture of the vascular wall by controlling PDGFRbeta-
RT dependent phosphatidylinositol 3-kinase activation.";
RL PLoS ONE 4:E6922-E6922(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [20]
RP FUNCTION.
RX PubMed=21664579; DOI=10.1016/j.devcel.2011.04.019;
RA Olson L.E., Soriano P.;
RT "PDGFRbeta signaling regulates mural cell plasticity and inhibits fat
RT development.";
RL Dev. Cell 20:815-826(2011).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1005-1015 IN COMPLEX WITH PTPN11,
RP AND INTERACTION WITH PTPN11.
RX PubMed=7521735; DOI=10.1016/s0969-2126(00)00044-7;
RA Lee C.-H., Kominos D., Jacques S., Margolis B., Schlessinger J.,
RA Shoelson S.E., Kuriyan J.;
RT "Crystal structures of peptide complexes of the amino-terminal SH2 domain
RT of the Syp tyrosine phosphatase.";
RL Structure 2:423-438(1994).
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. Plays a role in the migration
CC of vascular smooth muscle cells and the formation of neointima at
CC vascular injury sites. Required for normal development of the
CC cardiovascular system. Required for normal recruitment of pericytes
CC (mesangial cells) in the kidney glomerulus, and for normal formation of
CC a branched network of capillaries in kidney glomeruli. Promotes
CC rearrangement of the actin cytoskeleton and the formation of membrane
CC ruffles. Binding of its cognate ligands - homodimeric PDGFB,
CC heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to
CC the activation of several signaling cascades; the response depends on
CC the nature of the bound ligand and is modulated by the formation of
CC heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1,
CC PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the
CC production of the cellular signaling molecules diacylglycerol and
CC inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the
CC activation of protein kinase C. Phosphorylation of PIK3R1, the
CC regulatory subunit of phosphatidylinositol 3-kinase, leads to the
CC activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or
CC of the C-terminus of PTPN11, creates a binding site for GRB2, resulting
CC in the activation of HRAS, RAF1 and down-stream MAP kinases, including
CC MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation
CC of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and
CC STAM (By similarity). Receptor signaling is down-regulated by protein
CC phosphatases that dephosphorylate the receptor and its down-stream
CC effectors, and by rapid internalization of the activated receptor.
CC {ECO:0000250, ECO:0000269|PubMed:14624252, ECO:0000269|PubMed:14993293,
CC ECO:0000269|PubMed:15284236, ECO:0000269|PubMed:17620338,
CC ECO:0000269|PubMed:18948621, ECO:0000269|PubMed:19030102,
CC ECO:0000269|PubMed:19742316, ECO:0000269|PubMed:21664579,
CC ECO:0000269|PubMed:8440729}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:15284236};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization
CC and activation by autophosphorylation on tyrosine residues.
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 SLC9A3R1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P05622; P39688: Fyn; NbExp=3; IntAct=EBI-1554855, EBI-524514;
CC P05622; Q9JHL1: Slc9a3r2; NbExp=2; IntAct=EBI-1554855, EBI-538451;
CC P05622; Q91YD9: Wasl; NbExp=2; IntAct=EBI-1554855, EBI-642417;
CC P05622; C5IAU5: E5; Xeno; NbExp=2; IntAct=EBI-1554855, EBI-15646370;
CC P05622; P18031: PTPN1; Xeno; NbExp=3; IntAct=EBI-1554855, EBI-968788;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cytoplasmic vesicle {ECO:0000250}. Lysosome lumen
CC {ECO:0000250}. Note=After ligand binding, the autophosphorylated
CC receptor is ubiquitinated and internalized, leading to its degradation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P05622-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P05622-2; Sequence=VSP_060195;
CC -!- TISSUE SPECIFICITY: Weakly expressed in glomerular mesangial cells and
CC interstitial cells. Up-regulated in areas of renal fibrosis. In mice
CC with unilateral ureteral obstruction, increased expression in
CC interstitial cells at day 4 and expression is markedly elevated at day
CC 7 and is maximal at day 14. {ECO:0000269|PubMed:14514732}.
CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
CC receptor phosphorylates tyrosine residues on the other subunit.
CC Phosphorylation at Tyr-578, and to a lesser degree, Tyr-580 is
CC important for interaction with SRC. Phosphorylation at Tyr-715 is
CC important for interaction with GRB2. Phosphorylation at Tyr-739 and
CC Tyr-750 is important for interaction with PIK3R1. Phosphorylation at
CC Tyr-750 is important for interaction with NCK1. Phosphorylation at Tyr-
CC 770 and Tyr-856 is important for interaction with RASA1/GAP.
CC Phosphorylation at Tyr-856 is important for efficient phosphorylation
CC of PLCG1 and PTPN11, resulting in increased phosphorylation of AKT1,
CC MAPK1/ERK2 and/or MAPK3/ERK1, PDCD6IP/ALIX and STAM, and in increased
CC cell proliferation. Phosphorylation at Tyr-1008 is important for
CC interaction with PTPN11. Phosphorylation at Tyr-1008 and Tyr-1020 is
CC important for interaction with PLCG1. Dephosphorylated by PTPRJ at Tyr-
CC 750, Tyr-856, Tyr-1008 and Tyr-1020 (By similarity). Dephosphorylated
CC by PTPN2 at Tyr-578 and Tyr-1020. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
CC polyubiquitinated, leading to its degradation.
CC {ECO:0000269|PubMed:15753096}.
CC -!- DISRUPTION PHENOTYPE: No apparent phenotype up to 16 dpc. Lethality
CC late during gestation or at birth, due to widespread bleedings. This is
CC due to a severe shortage of vascular smooth muscle cells and pericytes,
CC especially in the central nervous system, skin, lung and heart. Mutants
CC suffer from hemorrhages, anemia, thrombocytopenia, and show defects in
CC the formation of kidney glomeruli, due to a lack of mesangial cells.
CC {ECO:0000269|PubMed:15207813, ECO:0000269|PubMed:18213589,
CC ECO:0000269|PubMed:7958864}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X04367; CAA27882.1; -; mRNA.
DR EMBL; AC124448; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50300.1; -. [P05622-2]
DR PIR; A25742; PFMSRB.
DR RefSeq; NP_001139740.1; NM_001146268.1. [P05622-2]
DR RefSeq; NP_032835.2; NM_008809.2. [P05622-1]
DR PDB; 1AYA; X-ray; 2.05 A; P/Q=1005-1015.
DR PDB; 1AYC; X-ray; 2.30 A; P=736-744.
DR PDBsum; 1AYA; -.
DR PDBsum; 1AYC; -.
DR AlphaFoldDB; P05622; -.
DR BMRB; P05622; -.
DR SMR; P05622; -.
DR BioGRID; 202089; 13.
DR ComplexPortal; CPX-2903; PDGF receptor alpha-beta - PDGF-AB complex.
DR ComplexPortal; CPX-2904; PDGF receptor beta - PDGF-AB complex.
DR ComplexPortal; CPX-2907; PDGF receptor alpha-beta - PDGF-BB complex.
DR ComplexPortal; CPX-2908; PDGF receptor beta - PDGF-BB complex.
DR ComplexPortal; CPX-2913; PDGF receptor alpha-beta - PDGF-CC complex.
DR ComplexPortal; CPX-2914; PDGF receptor beta - PDGF-CC complex.
DR ComplexPortal; CPX-2916; PDGF receptor alpha-beta - PDGF-DD complex.
DR ComplexPortal; CPX-2917; PDGF receptor beta - PDGF-DD complex.
DR CORUM; P05622; -.
DR DIP; DIP-39669N; -.
DR IntAct; P05622; 14.
DR MINT; P05622; -.
DR STRING; 10090.ENSMUSP00000025522; -.
DR BindingDB; P05622; -.
DR ChEMBL; CHEMBL2749; -.
DR DrugCentral; P05622; -.
DR GuidetoPHARMACOLOGY; 1804; -.
DR GlyGen; P05622; 11 sites.
DR iPTMnet; P05622; -.
DR PhosphoSitePlus; P05622; -.
DR jPOST; P05622; -.
DR MaxQB; P05622; -.
DR PaxDb; P05622; -.
DR PRIDE; P05622; -.
DR ProteomicsDB; 288051; -. [P05622-1]
DR ProteomicsDB; 311896; -.
DR ABCD; P05622; 3 sequenced antibodies.
DR Antibodypedia; 3424; 2229 antibodies from 49 providers.
DR DNASU; 18596; -.
DR Ensembl; ENSMUST00000025522; ENSMUSP00000025522; ENSMUSG00000024620. [P05622-2]
DR GeneID; 18596; -.
DR KEGG; mmu:18596; -.
DR UCSC; uc008fbk.2; mouse. [P05622-1]
DR CTD; 5159; -.
DR MGI; MGI:97531; Pdgfrb.
DR VEuPathDB; HostDB:ENSMUSG00000024620; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000157138; -.
DR HOGENOM; CLU_000288_49_0_1; -.
DR InParanoid; P05622; -.
DR OMA; PQPGCQE; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; P05622; -.
DR TreeFam; TF325768; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 18596; 5 hits in 76 CRISPR screens.
DR EvolutionaryTrace; P05622; -.
DR PRO; PR:P05622; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P05622; protein.
DR Bgee; ENSMUSG00000024620; Expressed in external carotid artery and 265 other tissues.
DR ExpressionAtlas; P05622; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IMP:MGI.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; ISS:UniProtKB.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0005017; F:platelet-derived growth factor receptor activity; IDA:MGI.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:MGI.
DR GO; GO:0030325; P:adrenal gland development; IGI:MGI.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0035909; P:aorta morphogenesis; IGI:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; IEP:UniProtKB.
DR GO; GO:0055003; P:cardiac myofibril assembly; IGI:UniProtKB.
DR GO; GO:0060947; P:cardiac vascular smooth muscle cell differentiation; TAS:DFLAT.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0060981; P:cell migration involved in coronary angiogenesis; IMP:UniProtKB.
DR GO; GO:0035441; P:cell migration involved in vasculogenesis; IMP:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IEP:UniProtKB.
DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0060437; P:lung growth; ISO:MGI.
DR GO; GO:0072277; P:metanephric glomerular capillary formation; IGI:UniProtKB.
DR GO; GO:0072262; P:metanephric glomerular mesangial cell proliferation involved in metanephros development; IMP:UniProtKB.
DR GO; GO:0072223; P:metanephric glomerular mesangium development; IEP:UniProtKB.
DR GO; GO:0035789; P:metanephric mesenchymal cell migration; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:MGI.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IMP:UniProtKB.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:BHF-UCL.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0106096; P:response to ceramide; IMP:MGI.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:UniProtKB.
DR GO; GO:0097178; P:ruffle assembly; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IDA:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0071670; P:smooth muscle cell chemotaxis; IGI:BHF-UCL.
DR GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
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; 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 Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; Chemotaxis;
KW Cytoplasmic vesicle; Developmental protein; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Lysosome;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..31
FT CHAIN 32..1098
FT /note="Platelet-derived growth factor receptor beta"
FT /id="PRO_0000016758"
FT TOPO_DOM 32..531
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..1098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..119
FT /note="Ig-like C2-type 1"
FT DOMAIN 128..209
FT /note="Ig-like C2-type 2"
FT DOMAIN 213..308
FT /note="Ig-like C2-type 3"
FT DOMAIN 330..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 415..523
FT /note="Ig-like C2-type 5"
FT DOMAIN 599..961
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1016..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 825
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 605..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 561
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 578
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 580
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 685
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000269|PubMed:14993293"
FT MOD_RES 715
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 739
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 750
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 762
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 770
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 774
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 777
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 856
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 933
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000269|PubMed:14993293"
FT MOD_RES 969
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000269|PubMed:14993293"
FT MOD_RES 1008
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT MOD_RES 1020
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09619"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT DISULFID 53..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 148..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 234..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 435..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 454
FT /note="K -> KS (in isoform 2)"
FT /id="VSP_060195"
FT MUTAGEN 578
FT /note="Y->F: Strongly reduced levels of vascular smooth
FT muscle cells and pericytes in developing blood vessels;
FT when associated with F-715; F-739; F-750; F-770; F-1008 and
FT F-1020."
FT /evidence="ECO:0000269|PubMed:14624252"
FT MUTAGEN 715
FT /note="Y->F: Strongly reduced levels of vascular smooth
FT muscle cells and pericytes in developing blood vessels;
FT when associated with F-578; F-739; F-750; F-770; F-1008 and
FT F-1020."
FT /evidence="ECO:0000269|PubMed:14624252"
FT MUTAGEN 739
FT /note="Y->F: Strongly reduced levels of vascular smooth
FT muscle cells and pericytes in developing blood vessels;
FT when associated with F-578; F-715; F-750; F-770; F-1008 and
FT F-1020."
FT /evidence="ECO:0000269|PubMed:14624252"
FT MUTAGEN 750
FT /note="Y->F: Strongly reduced levels of vascular smooth
FT muscle cells and pericytes in developing blood vessels;
FT when associated with F-578; F-715; F-739; F-770; F-1008 and
FT F-1020."
FT /evidence="ECO:0000269|PubMed:14624252"
FT MUTAGEN 770
FT /note="Y->F: Strongly reduced levels of vascular smooth
FT muscle cells and pericytes in developing blood vessels;
FT when associated with F-578; F-715; F-739; F-750; F-1008 and
FT F-1020."
FT /evidence="ECO:0000269|PubMed:14624252"
FT MUTAGEN 849
FT /note="D->N: Increased autophosphorylation in the absence
FT of PDGFB binding. Increased autophosphorylation in response
FT to PDGFB binding. Constitutive interaction with PIK3R1, and
FT constitutive AKT1 activation."
FT /evidence="ECO:0000269|PubMed:15284236"
FT MUTAGEN 1008
FT /note="Y->F: Strongly reduced levels of vascular smooth
FT muscle cells and pericytes in developing blood vessels;
FT when associated with F-578; F-715; F-739; F-750; F-770 and
FT F-1020."
FT /evidence="ECO:0000269|PubMed:14624252"
FT MUTAGEN 1020
FT /note="Y->F: Strongly reduced levels of vascular smooth
FT muscle cells and pericytes in developing blood vessels;
FT when associated with F-578; F-715; F-739; F-750; F-770 and
FT F-1008."
FT /evidence="ECO:0000269|PubMed:14624252"
FT CONFLICT 863
FT /note="F -> Y (in Ref. 1; CAA27882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1098 AA; 122790 MW; D08FC7C42B77B794 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 STFLPLKWMA PESIFNSLYT TLSDVWSFGI LLWEIFTLGG
TPYPELPMND QFYNAIKRGY RMAQPAHASD EIYEIMQKCW EEKFETRPPF SQLVLLLERL
LGEGYKKKYQ QVDEEFLRSD HPAILRSQAR FPGIHSLRSP LDTSSVLYTA VQPNESDNDY
IIPLPDPKPD VADEGLPEGS PSLASSTLNE VNTSSTISCD SPLELQEEPQ QAEPEAQLEQ
PQDSGCPGPL AEAEDSFL
