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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_RAT               Reviewed;        1088 AA.
P20786;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 2.
20-JUN-2018, entry version 172.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
PubMed=2157969; DOI=10.1128/MCB.10.5.2237;
Lee K.H., Bowen-Pope D.F., Reed R.R.;
"Isolation and characterization of the alpha platelet-derived growth
factor receptor from rat olfactory epithelium.";
Mol. Cell. Biol. 10:2237-2246(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 33-524.
PubMed=8318539; DOI=10.1016/0167-4781(93)90127-Y;
Herren B., Weyer K.A., Rouge M., Loetscher P., Pech M.;
"Conservation in sequence and affinity of human and rodent PDGF
ligands and receptors.";
Biochim. Biophys. Acta 1173:294-302(1993).
[3]
PROTEIN SEQUENCE OF 833-840, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
-!- 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}.
-!- 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}.
-!- 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-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}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA40743.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M63837; AAA40743.1; ALT_INIT; mRNA.
EMBL; Z14118; CAA78488.1; -; mRNA.
PIR; A34710; PFRTGA.
RefSeq; NP_036934.1; NM_012802.1.
UniGene; Rn.55127; -.
ProteinModelPortal; P20786; -.
SMR; P20786; -.
IntAct; P20786; 1.
MINT; P20786; -.
STRING; 10116.ENSRNOP00000003077; -.
ChEMBL; CHEMBL2111344; -.
iPTMnet; P20786; -.
PhosphoSitePlus; P20786; -.
PaxDb; P20786; -.
PRIDE; P20786; -.
GeneID; 25267; -.
KEGG; rno:25267; -.
UCSC; RGD:3284; rat.
CTD; 5156; -.
RGD; 3284; Pdgfra.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000112009; -.
HOVERGEN; HBG004335; -.
InParanoid; P20786; -.
KO; K04363; -.
PhylomeDB; P20786; -.
BRENDA; 2.7.10.1; 5301.
PRO; PR:P20786; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:RGD.
GO; GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISS:UniProtKB.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISS:UniProtKB.
GO; GO:0048839; P:inner ear development; IEP:RGD.
GO; GO:0060437; P:lung growth; IMP:RGD.
GO; GO:0001553; P:luteinization; ISS:UniProtKB.
GO; GO:0008584; P:male gonad development; IEP:RGD.
GO; GO:0072277; P:metanephric glomerular capillary formation; ISS:UniProtKB.
GO; GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS: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; ISS:UniProtKB.
GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; 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:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:2000739; P:regulation of mesenchymal stem cell differentiation; ISS:UniProtKB.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:1904404; P:response to formaldehyde; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:UniProtKB.
GO; GO:0042060; P:wound healing; IEP:RGD.
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; SM00220; S_TKc; 1.
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;
ATP-binding; Cell membrane; Chemotaxis; Complete proteome;
Developmental protein; Direct protein sequencing; 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 23
CHAIN 24 1088 Platelet-derived growth factor receptor
alpha.
/FTId=PRO_0000016762.
TOPO_DOM 24 527 Extracellular. {ECO:0000255}.
TRANSMEM 528 548 Helical. {ECO:0000255}.
TOPO_DOM 549 1088 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 112 Ig-like C2-type 1.
DOMAIN 116 200 Ig-like C2-type 2.
DOMAIN 201 305 Ig-like C2-type 3.
DOMAIN 318 409 Ig-like C2-type 4.
DOMAIN 413 516 Ig-like C2-type 5.
DOMAIN 592 953 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 598 606 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 817 817 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 626 626 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 571 571 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 573 573 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 719 719 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 730 730 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 741 741 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 753 753 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 761 761 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 767 767 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 848 848 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 987 987 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
MOD_RES 1017 1017 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P16234}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 467 467 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 99 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 149 188 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 234 289 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 434 500 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 150 150 L -> R (in Ref. 2; CAA78488).
{ECO:0000305}.
CONFLICT 519 519 S -> T (in Ref. 2; CAA78488).
{ECO:0000305}.
SEQUENCE 1088 AA; 122642 MW; 590C8BB0418801E7 CRC64;
MGTSQAFLVL SCLLTGPSLI VCQLLLPSIL PNENEKIVPL SSSFSLRCFG ESEVSWQHPM
SEEEDPNVEI RTEENNSSLF VTVLEVVNAS AAHTGWYTCY YNHTQTEESE IEGRHIYIYV
PDPDMAFVPL GMTDSLVIVE EDDSAIIPCL TTDPDTEVTL HNNGRLVPAS YDSRQGFNGT
FSVGPYICEA TVRGRTFKTS EFNVYALKAT SELNLEMDTR QTVYKAGETI VVTCAVFNNE
VVDLQWTYPG EVRNKGITML EEIKLPSIKL VYTLTVPKAT VKDSGDYECA ARQATKEVKE
MKTVTISVHE KGFVQIRPTF GHLETVNLHQ VREFVVEVQA YPTPRISWLK DNLTLIENLT
EITTDVQRSQ ETRYQSKLKL IRAKEEDSGH YTIIVQNDDD MKSYTFELST LVPASILELV
DDHHGSGGGQ TVRCTAEGTP LPNIEWMICK DIKKCNNDTS WTVLASNVSN IITEFHQRGR
STVEGRVSFA KVEETIAVRC LAKNDLGIGN RELKLVAPSL RSELTVAAAV LVLLVIVIVS
LIVLVVIWKQ KPRYEIRWRV IESISPDGHE YIYVDPMQLP YDSRWEFPRD GLVLGRILGS
GAFGKVVEGT AYGLSRSQPV MKVAVKMLKP TARSSEKQAL MSELKIMTHL GPHLNIVNLL
GACTKSGPIY IITEYCFYGD LVNYLHKNRD SFMSRHPEKP KKDLDIFGLN PADESTRSYV
ILSFENNGDY VDMKQADTTQ YVPMLERKEV SKYSDIQRSL YDRPASYKKK SMLDSEAKNL
LSDDDSEGLT LLDLLSFTYQ VARGMEFLAS KNCVHRDLAA RNVLLAQGKI VKICDFGLAR
DIMHDSNYVS KGSTFLPVKW MAPESIFDNL YTTLSDVWSY GVLLWEIFSL GGTPYPGMMV
DSTFYNKIKS GYRMAKPDHA TSEVYEIMVQ CWNSEPEKRP SFYHLSEIVE NLLPGQYKKS
YEKIHLDFLK SDHPAVARMR VDSDNAYIGV TYKNEEDKLK EWEGGLDEQR LSADSGYIIP
LPDIDPVPEE EDLGKRNRHS SQTSEESAIE TGSSSSTFIK REDETIEDID MMDDIGIDSS
DLVEDSFL


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