Pdgfra
entrez
25267
canonical
uniprot
P20786
canonical
ensembl
ENSRNOG00000002244
resolver
ensp
ENSRNOP00000003077
resolver
enst
ENSRNOT00000003077
resolver
genesymbol
Pdgfra
resolver
uniprot
G3V6A0
resolver
uniprot_entry
G3V6A0_RAT
resolver
uniprot_entry
PGFRA_RAT
resolver
activity_regulation
ACTIVITY 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}.
uniprot
proteins
amino_acid_sequence
MGTSQAFLVLSCLLTGPSLIVCQLLLPSILPNENEKIVPLSSSFSLRCFGESEVSWQHPMSEEEDPNVEIRTEENNSSLFVTVLEVVNASAAHTGWYTCYYNHTQTEESEIEGRHIYIYVPDPDMAFVPLGMTDSLVIVEEDDSAIIPCLTTDPDTEVTLHNNGRLVPASYDSRQGFNGTFSVGPYICEATVRGRTFKTSEFNVYALKATSELNLEMDTRQTVYKAGETIVVTCAVFNNEVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGDYECAARQATKEVKEMKTVTISVHEKGFVQIRPTFGHLETVNLHQVREFVVEVQAYPTPRISWLKDNLTLIENLTEITTDVQRSQETRYQSKLKLIRAKEEDSGHYTIIVQNDDDMKSYTFELSTLVPASILELVDDHHGSGGGQTVRCTAEGTPLPNIEWMICKDIKKCNNDTSWTVLASNVSNIITEFHQRGRSTVEGRVSFAKVEETIAVRCLAKNDLGIGNRELKLVAPSLRSELTVAAAVLVLLVIVIVSLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSRHPEKPKKDLDIFGLNPADESTRSYVILSFENNGDYVDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEAKNLLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGVLLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKEWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
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 (By similarity). {ECO:0000250|UniProtKB:P16234, ECO:0000250|UniProtKB:P26618}.
uniprot
proteins
mass_dalton
122642
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated, leading to its internalization and degradation. {ECO:0000250|UniProtKB:P26618}.; 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-730 and Tyr-741 is important for interaction with PIK3R1. Phosphorylation at Tyr-719 and Tyr-753 is important for interaction with PTPN11. Phosphorylation at Tyr-761 is important for interaction with CRK. Phosphorylation at Tyr-571 and Tyr-573 is important for interaction with SRC and SRC family members. Phosphorylation at Tyr-987 and Tyr-1017 is important for interaction with PLCG1 (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
CSF-1/PDGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
2157969
uniprot
proteins
pubmed
8318539
uniprot
proteins
sequence_length
1088
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P16234}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P16234}. Cell projection, cilium {ECO:0000250|UniProtKB:P26618}. Golgi apparatus {ECO:0000250|UniProtKB:P26618}.
uniprot
proteins
transmembrane_region
TRANSMEM 528..548; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins