Pdgfra
entrez
18595
canonical
uniprot
P26618
canonical
ensembl
ENSMUSG00000029231
resolver
ensp
ENSMUSP00000000476
resolver
ensp
ENSMUSP00000127173
resolver
ensp
ENSMUSP00000143891
resolver
ensp
ENSMUSP00000143906
resolver
ensp
ENSMUSP00000298803
resolver
ensp
ENSMUSP00000298805
resolver
ensp
ENSMUSP00000298806
resolver
genesymbol
Pdgfra
resolver
uniprot
Q3TQ37
resolver
uniprot
Q62046
resolver
uniprot
Q7TSJ3
resolver
uniprot
Q8C4N3
resolver
uniprot_entry
PGFRA_MOUSE
resolver
uniprot_sec
Q3TQ37
resolver
uniprot_sec
Q62046
resolver
uniprot_sec
Q7TSJ3
resolver
uniprot_sec
Q8C4N3
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
MGTSHQVFLVLSCLLTGPGLISCQLLLPSILPNENEKIVQLNSSFSLRCVGESEVSWQHPMSEEDDPNVEIRSEENNSGLFVTVLEVVNASAAHTGWYTCYYNHTQTDESEIEGRHIYIYVPDPDMAFVPLGMTDSLVIVEEDDSAIIPCRTTDPETQVTLHNNGRLVPASYDSRQGFNGTFSVGPYICEATVKGRTFKTSEFNVYALKATSELNLEMDARQTVYKAGETIVVTCAVFNNEVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGEYECAARQATKEVKEMKRVTISVHEKGFVEIEPTFGQLEAVNLHEVREFVVEVQAYPTPRISWLKDNLTLIENLTEITTDVQKSQETRYQSKLKLIRAKEEDSGHYTIIVQNEDDVKSYTFELSTLVPASILDLVDDHHGSGGGQTVRCTAEGTPLPEIDWMICKHIKKCNNDTSWTVLASNVSNIITELPRRGRSTVEGRVSFAKVEETIAVRCLAKNNLSVVARELKLVAPTLRSELTVAAAVLVLLVIVIVSLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSQHPEKPKKDLDIFGLNPADESTRSYVILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKNLLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMMVDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKKSYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYIIPLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDSSDLVEDSFL
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. {ECO:0000269|PubMed:10903171, ECO:0000269|PubMed:19030102, ECO:0000269|PubMed:20110689, ECO:0000269|PubMed:30986375, ECO:0000269|PubMed:9226440}.
uniprot
proteins
mass_dalton
122683
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated, leading to its internalization and degradation. {ECO:0000269|PubMed:29237719}.; 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|UniProtKB:P16234}.
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
10837138
uniprot
proteins
pubmed
10903171
uniprot
proteins
pubmed
1321404
uniprot
proteins
pubmed
14514732
uniprot
proteins
pubmed
15207813
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19030102
uniprot
proteins
pubmed
20110689
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2174116
uniprot
proteins
pubmed
29237719
uniprot
proteins
pubmed
30986375
uniprot
proteins
pubmed
9226440
uniprot
proteins
sequence_length
1089
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:0000269|PubMed:29237719}. Golgi apparatus {ECO:0000269|PubMed:29237719}.
uniprot
proteins
transmembrane_region
TRANSMEM 529..549; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins