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Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (Platelet-derived growth factor alpha receptor) (CD antigen CD140a)

 PGFRA_MOUSE             Reviewed;        1089 AA.
P26618; Q3TQ37; Q62046; Q7TSJ3; Q8C4N3;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 3.
28-FEB-2018, entry version 183.
RecName: Full=Platelet-derived growth factor receptor alpha;
Short=PDGF-R-alpha;
Short=PDGFR-alpha;
EC=2.7.10.1;
AltName: Full=Alpha platelet-derived growth factor receptor;
AltName: Full=Alpha-type platelet-derived growth factor receptor;
AltName: Full=CD140 antigen-like family member A;
AltName: Full=Platelet-derived growth factor alpha receptor;
AltName: CD_antigen=CD140a;
Flags: Precursor;
Name=Pdgfra;
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] (ISOFORM 1).
PubMed=2174116; DOI=10.1128/MCB.10.12.6781;
Stiles C.D., Wang C.;
"Retinoic acid promotes transcription of the platelet-derived growth
factor alpha-receptor gene.";
Mol. Cell. Biol. 10:6781-6784(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1321404;
Do M.S., Fitzer-Attas C., Gubbay J., Greenfeld L., Feldman M.,
Eisenbach L.;
"Mouse platelet-derived growth factor alpha receptor: sequence,
tissue-specific expression and correlation with metastatic
phenotype.";
Oncogene 7:1567-1575(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
TISSUE=Cerebellum, Colon, Embryonic head, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9226440;
Soriano P.;
"The PDGF alpha receptor is required for neural crest cell development
and for normal patterning of the somites.";
Development 124:2691-2700(1997).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10903171;
Karlsson L., Lindahl P., Heath J.K., Betsholtz C.;
"Abnormal gastrointestinal development in PDGF-A and PDGFR-(alpha)
deficient mice implicates a novel mesenchymal structure with putative
instructive properties in villus morphogenesis.";
Development 127:3457-3466(2000).
[7]
INTERACTION WITH SHB.
PubMed=10837138; DOI=10.1006/excr.2000.4896;
Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M.;
"Platelet-derived growth factor-mediated signaling through the Shb
adaptor protein: effects on cytoskeletal organization.";
Exp. Cell Res. 257:245-254(2000).
[8]
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).
[9]
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).
[10]
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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Lung;
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).
[12]
FUNCTION.
PubMed=20110689; DOI=10.1159/000276562;
Schneider L., Cammer M., Lehman J., Nielsen S.K., Guerra C.F.,
Veland I.R., Stock C., Hoffmann E.K., Yoder B.K., Schwab A., Satir P.,
Christensen S.T.;
"Directional cell migration and chemotaxis in wound healing response
to PDGF-AA are coordinated by the primary cilium in fibroblasts.";
Cell. Physiol. Biochem. 25:279-292(2010).
-!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface
receptor for PDGFA, PDGFB and PDGFC and plays an essential role in
the regulation of embryonic development, cell proliferation,
survival and chemotaxis. Depending on the context, promotes or
inhibits cell proliferation and cell migration. Plays an important
role in the differentiation of bone marrow-derived mesenchymal
stem cells. Required for normal skeleton development and cephalic
closure during embryonic development. Required for normal
development of the mucosa lining the gastrointestinal tract, and
for recruitment of mesenchymal cells and normal development of
intestinal villi. Plays a role in cell migration and chemotaxis in
wound healing. Plays a role in platelet activation, secretion of
agonists from platelet granules, and in thrombin-induced platelet
aggregation. Binding of its cognate ligands - homodimeric PDGFA,
homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
homodimeric PDGFC -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 PIK3R1, PLCG1, and PTPN11. 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. Phosphorylates PIK3R1, the regulatory subunit of
phosphatidylinositol 3-kinase, and thereby mediates activation of
the AKT1 signaling pathway. Mediates activation of HRAS and of the
MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of
STAT family members STAT1, STAT3 and STAT5A and/or STAT5B.
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:0000269|PubMed:10903171, ECO:0000269|PubMed:19030102,
ECO:0000269|PubMed:20110689, ECO:0000269|PubMed:9226440}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. Binding of PDGFA and/or PDGFB leads to
dimerization and activation by autophosphorylation on tyrosine
residues. Inhibited by imatinib, nilotinib and sorafenib (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and
with heterodimers formed by PDGFA and PDGFB. Monomer in the
absence of bound ligand. Interaction with dimeric PDGFA, PDGFB
and/or PDGFC leads to receptor dimerization, where both PDGFRA
homodimers and heterodimers with PDGFRB are observed. Interacts
(tyrosine phosphorylated) with SHB (via SH2 domain). Interacts
(tyrosine phosphorylated) with SHF (via SH2 domain). Interacts
(tyrosine phosphorylated) with SRC (via SH2 domain). Interacts
(tyrosine phosphorylated) with PIK3R1. Interacts (tyrosine
phosphorylated) with PLCG1 (via SH2 domain). Interacts (tyrosine
phosphorylated) with CRK, GRB2 and GRB7 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Note=The activated receptor is rapidly internalized and
degraded. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P26618-1; Sequence=Displayed;
Name=2;
IsoId=P26618-2; Sequence=VSP_031877, VSP_031878;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Focally expressed in cortical interstitial
cells and highly expressed in the interstitium of the papillary
region. Also expressed by adventitial cells in arterial vessels.
Up-regulated in areas of renal fibrosis. In mice with unilateral
ureteral obstruction, expression in cortical interstitial cells
becomes prominent at day 4 which increases progressively until day
14. {ECO:0000269|PubMed:14514732}.
-!- PTM: Ubiquitinated, leading to its degradation. {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
Autophosphorylation occurs in trans, i.e. one subunit of the
dimeric receptor phosphorylates tyrosine residues on the other
subunit. Phosphorylation at Tyr-731 and Tyr-742 is important for
interaction with PIK3R1. Phosphorylation at Tyr-720 and Tyr-754 is
important for interaction with PTPN11. Phosphorylation at Tyr-762
is important for interaction with CRK. Phosphorylation at Tyr-572
and Tyr-574 is important for interaction with SRC and SRC family
members. Phosphorylation at Tyr-988 and Tyr-1018 is important for
interaction with PLCG1 (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonically lethal. Most embryos survive
up to 13 dpc, but display important defects in skeleton
development, including spina bifida, fusions of cervical vertebrae
and ribs, and incomplete fusion of the skull parietal bone.
Embryos display also abnormal mucosa lining the gastrointestinal
tract, including fewer and misshapen villi and loss of pericryptal
mesenchyme. At about 16 dpc, embryos display extensive
hemorrhaging. {ECO:0000269|PubMed:10903171,
ECO:0000269|PubMed:15207813, ECO:0000269|PubMed:9226440}.
-!- 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; M57683; AAA39733.1; -; mRNA.
EMBL; M84607; AAA39904.1; -; mRNA.
EMBL; AK081664; BAC38283.1; -; mRNA.
EMBL; AK136490; BAE23004.1; -; mRNA.
EMBL; AK147267; BAE27808.1; -; mRNA.
EMBL; AK163952; BAE37548.1; -; mRNA.
EMBL; BC053036; AAH53036.1; -; mRNA.
CCDS; CCDS19351.1; -. [P26618-1]
PIR; I57511; S33727.
RefSeq; NP_001076785.1; NM_001083316.2. [P26618-1]
RefSeq; NP_001334647.1; NM_001347718.1. [P26618-2]
RefSeq; NP_001334648.1; NM_001347719.1. [P26618-2]
RefSeq; NP_035188.2; NM_011058.3. [P26618-1]
RefSeq; XP_006504324.1; XM_006504261.3. [P26618-1]
RefSeq; XP_006504325.1; XM_006504262.3. [P26618-1]
RefSeq; XP_006504326.1; XM_006504263.3. [P26618-1]
UniGene; Mm.221403; -.
ProteinModelPortal; P26618; -.
SMR; P26618; -.
BioGrid; 202088; 2.
IntAct; P26618; 3.
MINT; P26618; -.
STRING; 10090.ENSMUSP00000000476; -.
BindingDB; P26618; -.
ChEMBL; CHEMBL2096980; -.
GuidetoPHARMACOLOGY; 1803; -.
iPTMnet; P26618; -.
PhosphoSitePlus; P26618; -.
SwissPalm; P26618; -.
MaxQB; P26618; -.
PaxDb; P26618; -.
PeptideAtlas; P26618; -.
PRIDE; P26618; -.
Ensembl; ENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231. [P26618-1]
Ensembl; ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231. [P26618-1]
Ensembl; ENSMUST00000201711; ENSMUSP00000143891; ENSMUSG00000029231. [P26618-2]
Ensembl; ENSMUST00000202681; ENSMUSP00000143906; ENSMUSG00000029231. [P26618-2]
GeneID; 18595; -.
KEGG; mmu:18595; -.
UCSC; uc008xub.1; mouse. [P26618-2]
UCSC; uc008xuc.1; mouse. [P26618-1]
CTD; 5156; -.
MGI; MGI:97530; Pdgfra.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112009; -.
HOVERGEN; HBG004335; -.
InParanoid; P26618; -.
KO; K04363; -.
OMA; CKDIKKC; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P26618; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-186797; Signaling by PDGF.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
ChiTaRS; Pdgfra; mouse.
PRO; PR:P26618; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029231; -.
ExpressionAtlas; P26618; baseline and differential.
Genevisible; P26618; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
GO; GO:0005902; C:microvillus; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:UniProtKB.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
GO; GO:0032403; F:protein complex binding; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; ISO:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISO:MGI.
GO; GO:0038085; F:vascular endothelial growth factor binding; ISO:MGI.
GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0030325; P:adrenal gland development; IGI:MGI.
GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0055003; P:cardiac myofibril assembly; IGI:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:UniProtKB.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:UniProtKB.
GO; GO:0008210; P:estrogen metabolic process; IGI:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0060325; P:face morphogenesis; IMP:MGI.
GO; GO:0008585; P:female gonad development; IGI:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0001553; P:luteinization; IMP:MGI.
GO; GO:0030539; P:male genitalia development; IMP:MGI.
GO; GO:0072277; P:metanephric glomerular capillary formation; IGI:UniProtKB.
GO; GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0060021; P:palate development; IMP:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0035790; P:platelet-derived growth factor receptor-alpha signaling pathway; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0050920; P:regulation of chemotaxis; ISO:MGI.
GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; ISS:UniProtKB.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IGI:UniProtKB.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0042060; P:wound healing; IMP:UniProtKB.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR027290; PDGFRA.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF07679; I-set; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500950; Alpha-PDGF_receptor; 1.
SMART; SM00409; IG; 4.
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;
Alternative splicing; ATP-binding; Cell membrane; Chemotaxis;
Complete proteome; Developmental protein; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1089 Platelet-derived growth factor receptor
alpha.
/FTId=PRO_0000016761.
TOPO_DOM 25 528 Extracellular. {ECO:0000255}.
TRANSMEM 529 549 Helical. {ECO:0000255}.
TOPO_DOM 550 1089 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 113 Ig-like C2-type 1.
DOMAIN 117 201 Ig-like C2-type 2.
DOMAIN 202 306 Ig-like C2-type 3.
DOMAIN 319 410 Ig-like C2-type 4.
DOMAIN 414 517 Ig-like C2-type 5.
DOMAIN 593 954 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 599 607 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 818 818 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 627 627 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 572 572 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 574 574 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 720 720 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234,
ECO:0000305}.
MOD_RES 731 731 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 742 742 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 754 754 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 762 762 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 768 768 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 849 849 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 988 988 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 1018 1018 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 359 359 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 506 506 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 100 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 150 189 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 235 290 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 435 501 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 775 790 DSEVKNLLSDDDSEGL -> GKSAHAHSGKYDLSVV (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_031877.
VAR_SEQ 791 1089 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_031878.
CONFLICT 65 65 D -> E (in Ref. 1; AAA39733 and 2;
AAA39904). {ECO:0000305}.
CONFLICT 192 192 T -> A (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 202 202 E -> A (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 252 252 E -> G (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 271 271 L -> V (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 322 322 G -> S (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 326 326 A -> P (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 439 440 GT -> EG (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 472 472 I -> V (in Ref. 3; BAE37548).
{ECO:0000305}.
CONFLICT 529 529 A -> E (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 737 737 A -> D (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 849 849 Y -> D (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 936 936 E -> D (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 950 950 V -> L (in Ref. 1; AAA39733).
{ECO:0000305}.
CONFLICT 1005 1005 G -> S (in Ref. 2; AAA39904).
{ECO:0000305}.
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


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