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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)

 F6VUV9_CALJA            Unreviewed;      1089 AA.
F6VUV9;
27-JUL-2011, integrated into UniProtKB/TrEMBL.
27-JUL-2011, sequence version 1.
28-MAR-2018, entry version 62.
RecName: Full=Platelet-derived growth factor receptor alpha {ECO:0000256|PIRNR:PIRNR500950};
Short=PDGF-R-alpha {ECO:0000256|PIRNR:PIRNR500950};
Short=PDGFR-alpha {ECO:0000256|PIRNR:PIRNR500950};
EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR500950};
AltName: Full=Alpha platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500950};
AltName: Full=Alpha-type platelet-derived growth factor receptor {ECO:0000256|PIRNR:PIRNR500950};
Name=PDGFRA {ECO:0000313|EMBL:JAB23079.1,
ECO:0000313|Ensembl:ENSCJAP00000034181};
Callithrix jacchus (White-tufted-ear marmoset).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix.
NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000034181, ECO:0000313|Proteomes:UP000008225};
[1] {ECO:0000313|Ensembl:ENSCJAP00000034181, ECO:0000313|Proteomes:UP000008225}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSCJAP00000034181}
IDENTIFICATION.
Ensembl;
Submitted (JUN-2011) to UniProtKB.
[3] {ECO:0000313|EMBL:JAB23079.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Cerebellum {ECO:0000313|EMBL:JAB47573.1},
Cerebral cortex {ECO:0000313|EMBL:JAB33904.1}, and
Hippocampus {ECO:0000313|EMBL:JAB23079.1};
PubMed=25243066; DOI=10.1186/2047-217X-3-14;
Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
Moriyama E.N., French J.A., Norgren R.B.Jr.;
"De novo assembly of the common marmoset transcriptome from NextGen
mRNA sequences.";
Gigascience 3:14-14(2014).
-!- 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.
{ECO:0000256|PIRNR:PIRNR500950}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00701269}.
-!- 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. {ECO:0000256|PIRNR:PIRNR500950}.
-!- SUBUNIT: Interacts with homodimeric PDGFA, PDGFB and PDGFC, and
with heterodimers formed by PDGFA and PDGFB. Monomer in the
absence of bound ligand. {ECO:0000256|PIRNR:PIRNR500950}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000256|PIRNR:PIRNR500950}; Single-pass type I membrane
protein {ECO:0000256|PIRNR:PIRNR500950}. Membrane
{ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane
protein {ECO:0000256|RuleBase:RU000311}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000256|PIRNR:PIRNR500950, ECO:0000256|RuleBase:RU000311}.
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EMBL; ACFV01029888; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ACFV01029889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; ACFV01029890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; GAMS01000057; JAB23079.1; -; mRNA.
EMBL; GAMR01000028; JAB33904.1; -; mRNA.
EMBL; GAMP01005182; JAB47573.1; -; mRNA.
RefSeq; NP_001257517.1; NM_001270588.1.
RefSeq; XP_008991533.1; XM_008993285.2.
RefSeq; XP_008991534.1; XM_008993286.2.
RefSeq; XP_017825530.1; XM_017970041.1.
STRING; 9483.ENSCJAP00000034181; -.
Ensembl; ENSCJAT00000036109; ENSCJAP00000034181; ENSCJAG00000018415.
GeneID; 100412331; -.
KEGG; cjc:100412331; -.
CTD; 5156; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
KO; K04363; -.
OMA; CKDIKKC; -.
OrthoDB; EOG091G01TL; -.
TreeFam; TF325768; -.
Proteomes; UP000008225; Chromosome 3.
GO; GO:0030054; C:cell junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IEA:Ensembl.
GO; GO:0048407; F:platelet-derived growth factor binding; IEA:Ensembl.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0038085; F:vascular endothelial growth factor binding; IEA:Ensembl.
GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IEA:Ensembl.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0055003; P:cardiac myofibril assembly; IEA:Ensembl.
GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0008210; P:estrogen metabolic process; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0001553; P:luteinization; IEA:Ensembl.
GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
GO; GO:0072277; P:metanephric glomerular capillary formation; IEA:Ensembl.
GO; GO:0010544; P:negative regulation of platelet activation; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:Ensembl.
GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0050920; P:regulation of chemotaxis; IEA:Ensembl.
GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IEA:Ensembl.
GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IEA:Ensembl.
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; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00220; S_TKc; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 5.
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.
2: Evidence at transcript level;
ATP-binding {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00708816};
Cell membrane {ECO:0000256|PIRNR:PIRNR500950};
Chemotaxis {ECO:0000256|PIRNR:PIRNR500950};
Complete proteome {ECO:0000313|Proteomes:UP000008225};
Developmental protein {ECO:0000256|PIRNR:PIRNR500950};
Disulfide bond {ECO:0000256|SAAS:SAAS00916669};
Immunoglobulin domain {ECO:0000256|RuleBase:RU000311,
ECO:0000256|SAAS:SAAS00941986};
Kinase {ECO:0000256|PIRNR:PIRNR500950, ECO:0000256|SAAS:SAAS00582553};
Membrane {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00602683, ECO:0000256|SAM:Phobius};
Nucleotide-binding {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00708816};
Receptor {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|RuleBase:RU000311, ECO:0000256|SAAS:SAAS00600436,
ECO:0000313|EMBL:JAB23079.1};
Reference proteome {ECO:0000313|Proteomes:UP000008225};
Repeat {ECO:0000256|SAAS:SAAS00457685};
Signal {ECO:0000256|SAM:SignalP};
Transferase {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00582553};
Transmembrane {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00602683,
ECO:0000256|SAM:Phobius};
Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR500950,
ECO:0000256|SAAS:SAAS00582553}.
SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
CHAIN 24 1089 Platelet-derived growth factor receptor
alpha. {ECO:0000256|SAM:SignalP}.
/FTId=PRO_5014090281.
TRANSMEM 525 549 Helical. {ECO:0000256|SAM:Phobius}.
DOMAIN 28 113 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 202 306 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 319 406 Ig-like. {ECO:0000259|PROSITE:PS50835}.
DOMAIN 593 954 Protein kinase.
{ECO:0000259|PROSITE:PS50011}.
SEQUENCE 1089 AA; 122688 MW; F64CF80E68709601 CRC64;
MGTSHPVFLV LGCLLTGLSL ILCQLSLPSV LPNENEKVVQ LNSSFSLRCF GESEVSWQYP
MSEEENPNVE IRNEENNSGL FVTVLEVSSA SAAHTGLYTC YYNHTQTEEN ELEGRHIYIY
VPDPDVAFVP LGMTDYLVIV EDDDSAIIPC RTTDPETPVT LHNSEGVVPA SYDSRQGFNG
TFTVGPYICE ATVEGKKFQT IPFNVYALKA TSKLDLEMEA LKTVYKSGET IVVTCAVFNN
EVVDLQWTYP GEVKGKGITM LEEIKVPSIK LVYTLTVPEA TVKDSGDYEC AARQATREVK
EMKKVTISVH EKGFIEIKPN FSQLEAVNLH EVKNFVVEVQ AYPTPRISWL KNNLTLIENL
TEITTDVEKI QETRYRSQLK LIRAKEEDSG HYTIVVQNED DVKSYTFELL TQVPSSILDL
VDDHHGSTGG QTVRCMAEGT PLPDIEWMIC KDIKKCNNET SWTILANNVS NIITEVHPRG
RSTVEGRVTF AKVEETIAVR CLAKNLLGAE NRELKLVAPT LRSELTVAAA VLVLLVIVII
SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRVLG
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFLSHHPEK AKKELDIFGL NPADESTRSY
VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN
LLSDDNSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV KCWNSEPEKR PSFYHLSEIV ENLLPGQYKK
SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII
PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS
SDLVEDSFL


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