PGFRA_MOUSE
ID PGFRA_MOUSE Reviewed; 1089 AA.
AC P26618; Q3TQ37; Q62046; Q7TSJ3; Q8C4N3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Platelet-derived growth factor receptor alpha;
DE Short=PDGF-R-alpha;
DE Short=PDGFR-alpha;
DE EC=2.7.10.1;
DE AltName: Full=Alpha platelet-derived growth factor receptor;
DE AltName: Full=Alpha-type platelet-derived growth factor receptor;
DE AltName: Full=CD140 antigen-like family member A;
DE AltName: Full=Platelet-derived growth factor alpha receptor;
DE AltName: CD_antigen=CD140a;
DE Flags: Precursor;
GN Name=Pdgfra;
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).
RX PubMed=2174116; DOI=10.1128/mcb.10.12.6781-6784.1990;
RA Stiles C.D., Wang C.;
RT "Retinoic acid promotes transcription of the platelet-derived growth factor
RT alpha-receptor gene.";
RL Mol. Cell. Biol. 10:6781-6784(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1321404;
RA Do M.S., Fitzer-Attas C., Gubbay J., Greenfeld L., Feldman M.,
RA Eisenbach L.;
RT "Mouse platelet-derived growth factor alpha receptor: sequence, tissue-
RT specific expression and correlation with metastatic phenotype.";
RL Oncogene 7:1567-1575(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Colon, Embryonic head, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9226440; DOI=10.1242/dev.124.14.2691;
RA Soriano P.;
RT "The PDGF alpha receptor is required for neural crest cell development and
RT for normal patterning of the somites.";
RL Development 124:2691-2700(1997).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=10903171; DOI=10.1242/dev.127.16.3457;
RA Karlsson L., Lindahl P., Heath J.K., Betsholtz C.;
RT "Abnormal gastrointestinal development in PDGF-A and PDGFR-(alpha)
RT deficient mice implicates a novel mesenchymal structure with putative
RT instructive properties in villus morphogenesis.";
RL Development 127:3457-3466(2000).
RN [7]
RP INTERACTION WITH SHB.
RX PubMed=10837138; DOI=10.1006/excr.2000.4896;
RA Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M.;
RT "Platelet-derived growth factor-mediated signaling through the Shb adaptor
RT protein: effects on cytoskeletal organization.";
RL Exp. Cell Res. 257:245-254(2000).
RN [8]
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 [9]
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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 [12]
RP FUNCTION.
RX PubMed=20110689; DOI=10.1159/000276562;
RA Schneider L., Cammer M., Lehman J., Nielsen S.K., Guerra C.F., Veland I.R.,
RA Stock C., Hoffmann E.K., Yoder B.K., Schwab A., Satir P., Christensen S.T.;
RT "Directional cell migration and chemotaxis in wound healing response to
RT PDGF-AA are coordinated by the primary cilium in fibroblasts.";
RL Cell. Physiol. Biochem. 25:279-292(2010).
RN [13]
RP UBIQUITINATION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29237719; DOI=10.1083/jcb.201611050;
RA Schmid F.M., Schou K.B., Vilhelm M.J., Holm M.S., Breslin L., Farinelli P.,
RA Larsen L.A., Andersen J.S., Pedersen L.B., Christensen S.T.;
RT "IFT20 modulates ciliary PDGFRalpha signaling by regulating the stability
RT of Cbl E3 ubiquitin ligases.";
RL J. Cell Biol. 217:151-161(2018).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC for PDGFA, PDGFB and PDGFC and plays an essential role in the
CC regulation of embryonic development, cell proliferation, survival and
CC chemotaxis. Depending on the context, promotes or inhibits cell
CC proliferation and cell migration. Plays an important role in the
CC differentiation of bone marrow-derived mesenchymal stem cells. Required
CC for normal skeleton development and cephalic closure during embryonic
CC development. Required for normal development of the mucosa lining the
CC gastrointestinal tract, and for recruitment of mesenchymal cells and
CC normal development of intestinal villi. Plays a role in cell migration
CC and chemotaxis in wound healing. Plays a role in platelet activation,
CC secretion of agonists from platelet granules, and in thrombin-induced
CC platelet aggregation. Binding of its cognate ligands - homodimeric
CC PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
CC homodimeric PDGFC -leads to the activation of several signaling
CC cascades; the response depends on the nature of the bound ligand and is
CC modulated by the formation of heterodimers between PDGFRA and PDGFRB.
CC Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to
CC the 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. Phosphorylates PIK3R1, the regulatory
CC subunit of phosphatidylinositol 3-kinase, and thereby mediates
CC activation of the AKT1 signaling pathway. Mediates activation of HRAS
CC and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes
CC activation of STAT family members STAT1, STAT3 and STAT5A and/or
CC STAT5B. Receptor signaling is down-regulated by protein phosphatases
CC that dephosphorylate the receptor and its down-stream effectors, and by
CC rapid internalization of the activated receptor.
CC {ECO:0000269|PubMed:10903171, ECO:0000269|PubMed:19030102,
CC ECO:0000269|PubMed:20110689, ECO:0000269|PubMed:9226440}.
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 -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Binding of PDGFA and/or PDGFB leads to dimerization
CC and activation by autophosphorylation on tyrosine residues. Inhibited
CC by imatinib, nilotinib and sorafenib (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and with
CC heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound
CC ligand. Interaction with dimeric PDGFA, PDGFB and/or PDGFC leads to
CC receptor dimerization, where both PDGFRA homodimers and heterodimers
CC with PDGFRB are observed. Interacts (tyrosine phosphorylated) with SHB
CC (via SH2 domain). Interacts (tyrosine phosphorylated) with SHF (via SH2
CC domain). Interacts (tyrosine phosphorylated) with SRC (via SH2 domain).
CC Interacts (tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine
CC phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine
CC phosphorylated) with CRK, GRB2 and GRB7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16234};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16234}.
CC Cell projection, cilium {ECO:0000269|PubMed:29237719}. Golgi apparatus
CC {ECO:0000269|PubMed:29237719}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P26618-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P26618-2; Sequence=VSP_031877, VSP_031878;
CC -!- TISSUE SPECIFICITY: Focally expressed in cortical interstitial cells
CC and highly expressed in the interstitium of the papillary region. Also
CC expressed by adventitial cells in arterial vessels. Up-regulated in
CC areas of renal fibrosis. In mice with unilateral ureteral obstruction,
CC expression in cortical interstitial cells becomes prominent at day 4
CC which increases progressively until day 14.
CC {ECO:0000269|PubMed:14514732}.
CC -!- INDUCTION: Up-regulated by growth arrest.
CC {ECO:0000269|PubMed:29237719}.
CC -!- PTM: Ubiquitinated, leading to its internalization and degradation.
CC {ECO:0000269|PubMed:29237719}.
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-731 and Tyr-742 is important for interaction
CC with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is important for
CC interaction with PTPN11. Phosphorylation at Tyr-762 is important for
CC interaction with CRK. Phosphorylation at Tyr-572 and Tyr-574 is
CC important for interaction with SRC and SRC family members.
CC Phosphorylation at Tyr-988 and Tyr-1018 is important for interaction
CC with PLCG1 (By similarity). {ECO:0000250|UniProtKB:P16234}.
CC -!- DISRUPTION PHENOTYPE: Embryonically lethal. Most embryos survive up to
CC 13 dpc, but display important defects in skeleton development,
CC including spina bifida, fusions of cervical vertebrae and ribs, and
CC incomplete fusion of the skull parietal bone. Embryos display also
CC abnormal mucosa lining the gastrointestinal tract, including fewer and
CC misshapen villi and loss of pericryptal mesenchyme. At about 16 dpc,
CC embryos display extensive hemorrhaging. {ECO:0000269|PubMed:10903171,
CC ECO:0000269|PubMed:15207813, ECO:0000269|PubMed:9226440}.
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; M57683; AAA39733.1; -; mRNA.
DR EMBL; M84607; AAA39904.1; -; mRNA.
DR EMBL; AK081664; BAC38283.1; -; mRNA.
DR EMBL; AK136490; BAE23004.1; -; mRNA.
DR EMBL; AK147267; BAE27808.1; -; mRNA.
DR EMBL; AK163952; BAE37548.1; -; mRNA.
DR EMBL; BC053036; AAH53036.1; -; mRNA.
DR CCDS; CCDS19351.1; -. [P26618-1]
DR CCDS; CCDS89929.1; -. [P26618-2]
DR PIR; I57511; S33727.
DR RefSeq; NP_001076785.1; NM_001083316.2. [P26618-1]
DR RefSeq; NP_001334647.1; NM_001347718.1. [P26618-2]
DR RefSeq; NP_001334648.1; NM_001347719.1. [P26618-2]
DR RefSeq; NP_035188.2; NM_011058.3. [P26618-1]
DR RefSeq; XP_006504324.1; XM_006504261.3. [P26618-1]
DR RefSeq; XP_006504325.1; XM_006504262.3. [P26618-1]
DR RefSeq; XP_006504326.1; XM_006504263.3. [P26618-1]
DR AlphaFoldDB; P26618; -.
DR SMR; P26618; -.
DR BioGRID; 202088; 6.
DR ComplexPortal; CPX-2899; PDGF receptor alpha - PDGF-AA complex.
DR ComplexPortal; CPX-2901; PDGF receptor alpha - PDGF-AB complex.
DR ComplexPortal; CPX-2903; PDGF receptor alpha-beta - PDGF-AB complex.
DR ComplexPortal; CPX-2906; PDGF receptor alpha - PDGF-BB complex.
DR ComplexPortal; CPX-2907; PDGF receptor alpha-beta - PDGF-BB complex.
DR ComplexPortal; CPX-2912; PDGF receptor alpha - PDGF-CC complex.
DR ComplexPortal; CPX-2913; PDGF receptor alpha-beta - PDGF-CC complex.
DR ComplexPortal; CPX-2916; PDGF receptor alpha-beta - PDGF-DD complex.
DR IntAct; P26618; 2.
DR MINT; P26618; -.
DR STRING; 10090.ENSMUSP00000127173; -.
DR BindingDB; P26618; -.
DR ChEMBL; CHEMBL3466; -.
DR GuidetoPHARMACOLOGY; 1803; -.
DR GlyGen; P26618; 10 sites.
DR iPTMnet; P26618; -.
DR PhosphoSitePlus; P26618; -.
DR SwissPalm; P26618; -.
DR jPOST; P26618; -.
DR MaxQB; P26618; -.
DR PaxDb; P26618; -.
DR PeptideAtlas; P26618; -.
DR PRIDE; P26618; -.
DR ProteomicsDB; 301800; -. [P26618-1]
DR ProteomicsDB; 301801; -. [P26618-2]
DR ABCD; P26618; 4 sequenced antibodies.
DR Antibodypedia; 1381; 2189 antibodies from 46 providers.
DR DNASU; 18595; -.
DR Ensembl; ENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231. [P26618-1]
DR Ensembl; ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231. [P26618-1]
DR Ensembl; ENSMUST00000201711; ENSMUSP00000143891; ENSMUSG00000029231. [P26618-2]
DR Ensembl; ENSMUST00000202681; ENSMUSP00000143906; ENSMUSG00000029231. [P26618-2]
DR GeneID; 18595; -.
DR KEGG; mmu:18595; -.
DR UCSC; uc008xub.1; mouse. [P26618-2]
DR UCSC; uc008xuc.1; mouse. [P26618-1]
DR CTD; 5156; -.
DR MGI; MGI:97530; Pdgfra.
DR VEuPathDB; HostDB:ENSMUSG00000029231; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000156021; -.
DR HOGENOM; CLU_000288_49_0_1; -.
DR InParanoid; P26618; -.
DR OMA; CFLTGPF; -.
DR OrthoDB; 236292at2759; -.
DR PhylomeDB; P26618; -.
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; 18595; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Pdgfra; mouse.
DR PRO; PR:P26618; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P26618; protein.
DR Bgee; ENSMUSG00000029231; Expressed in ureter smooth muscle and 346 other tissues.
DR ExpressionAtlas; P26618; baseline and differential.
DR Genevisible; P26618; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0062063; F:BBSome binding; IDA:MGI.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:UniProtKB.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:MGI.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IGI:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0055003; P:cardiac myofibril assembly; IGI:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:UniProtKB.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:UniProtKB.
DR GO; GO:0008210; P:estrogen metabolic process; IGI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0008585; P:female gonad development; IGI:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0060437; P:lung growth; ISO:MGI.
DR GO; GO:0001553; P:luteinization; IMP:MGI.
DR GO; GO:0030539; P:male genitalia development; IMP:MGI.
DR GO; GO:0072277; P:metanephric glomerular capillary formation; IGI:UniProtKB.
DR GO; GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0035790; P:platelet-derived growth factor receptor-alpha signaling pathway; IDA:UniProtKB.
DR GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0050920; P:regulation of chemotaxis; ISO:MGI.
DR GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IGI:UniProtKB.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0050872; P:white fat cell differentiation; IMP:MGI.
DR GO; GO:0042060; P:wound healing; IMP:UniProtKB.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027290; PDGFRA.
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; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
DR SMART; SM00409; IG; 4.
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 Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW Chemotaxis; Developmental protein; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Immunoglobulin domain; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1089
FT /note="Platelet-derived growth factor receptor alpha"
FT /id="PRO_0000016761"
FT TOPO_DOM 25..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..1089
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..113
FT /note="Ig-like C2-type 1"
FT DOMAIN 117..201
FT /note="Ig-like C2-type 2"
FT DOMAIN 202..306
FT /note="Ig-like C2-type 3"
FT DOMAIN 319..410
FT /note="Ig-like C2-type 4"
FT DOMAIN 414..517
FT /note="Ig-like C2-type 5"
FT DOMAIN 593..954
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1018..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 818
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 599..607
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 572
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 574
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 720
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234, ECO:0000305"
FT MOD_RES 731
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 742
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 754
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 762
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 768
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 849
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 988
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT MOD_RES 1018
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P16234"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 150..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 235..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 435..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 775..790
FT /note="DSEVKNLLSDDDSEGL -> GKSAHAHSGKYDLSVV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031877"
FT VAR_SEQ 791..1089
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031878"
FT CONFLICT 65
FT /note="D -> E (in Ref. 1; AAA39733 and 2; AAA39904)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="T -> A (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="E -> A (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="E -> G (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="L -> V (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="G -> S (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> P (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..440
FT /note="GT -> EG (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="I -> V (in Ref. 3; BAE37548)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="A -> E (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="A -> D (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 849
FT /note="Y -> D (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="E -> D (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 950
FT /note="V -> L (in Ref. 1; AAA39733)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="G -> S (in Ref. 2; AAA39904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1089 AA; 122683 MW; 07AAFD2BAA12533A CRC64;
MGTSHQVFLV LSCLLTGPGL ISCQLLLPSI LPNENEKIVQ LNSSFSLRCV GESEVSWQHP
MSEEDDPNVE IRSEENNSGL FVTVLEVVNA SAAHTGWYTC YYNHTQTDES EIEGRHIYIY
VPDPDMAFVP LGMTDSLVIV EEDDSAIIPC RTTDPETQVT LHNNGRLVPA SYDSRQGFNG
TFSVGPYICE ATVKGRTFKT SEFNVYALKA TSELNLEMDA RQTVYKAGET IVVTCAVFNN
EVVDLQWTYP GEVRNKGITM LEEIKLPSIK LVYTLTVPKA TVKDSGEYEC AARQATKEVK
EMKRVTISVH EKGFVEIEPT FGQLEAVNLH EVREFVVEVQ AYPTPRISWL KDNLTLIENL
TEITTDVQKS QETRYQSKLK LIRAKEEDSG HYTIIVQNED DVKSYTFELS TLVPASILDL
VDDHHGSGGG QTVRCTAEGT PLPEIDWMIC KHIKKCNNDT SWTVLASNVS NIITELPRRG
RSTVEGRVSF AKVEETIAVR CLAKNNLSVV ARELKLVAPT LRSELTVAAA VLVLLVIVIV
SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFMSQHPEK PKKDLDIFGL NPADESTRSY
VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN
LLSDDDSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV QCWNSEPEKR PSFYHLSEIV ENLLPGQYKK
SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII
PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS
SDLVEDSFL
