Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01211
Entry Name
UniProt Accession
Theoretical PI
5.03
Molecular Weight
122683.35
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Platelet-derived growth factor receptor alpha
Protein Synonyms/Alias
PDGF-R-alpha; PDGFR-alpha; 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; CD140a;
Gene Name
Pdgfra
Gene Synonyms/Alias
Created Date
01-AUG-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
23
Canonical
TGPGLISCQLLLPSI
[1]
S-Palmitoylation
501
Canonical
EETIAVRCLAKNNLS
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Topological domain: 25 528 Extracellular.
Transmembrane: 529 549 Helical.
Topological domain: 550 1089 Cytoplasmic.
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.
Nucleotide-binding: 599 607 ATP.
Active site: 818 818 Proton acceptor.
Binding site: 627 627 ATP.
Modified residue: 555 555 Phosphotyrosine.
Modified residue: 572 572 Phosphotyrosine; by autocatalysis.
Modified residue: 574 574 Phosphotyrosine; by autocatalysis.
Modified residue: 582 582 Phosphotyrosine.
Modified residue: 720 720 Phosphotyrosine; by autocatalysis.
Modified residue: 731 731 Phosphotyrosine; by autocatalysis.
Modified residue: 742 742 Phosphotyrosine; by autocatalysis.
Modified residue: 754 754 Phosphotyrosine; by autocatalysis.
Modified residue: 762 762 Phosphotyrosine; by autocatalysis.
Modified residue: 768 768 Phosphotyrosine; by autocatalysis.
Modified residue: 849 849 Phosphotyrosine; by autocatalysis.
Modified residue: 944 944 Phosphotyrosine.
Modified residue: 958 958 Phosphotyrosine.
Modified residue: 962 962 Phosphotyrosine.
Modified residue: 988 988 Phosphotyrosine; by autocatalysis.
Modified residue: 993 993 Phosphotyrosine.
Modified residue: 1018 1018 Phosphotyrosine; by autocatalysis.
Protein Length
1089 AA.
Protein Sequence
(Canonical)
MGTSHQVFLV LSCLLTGPGL ISCQLLLPSI LPNENEKIVQ LNSSFSLRCV GESEVSWQHP  60
MSEEDDPNVE IRSEENNSGL FVTVLEVVNA SAAHTGWYTC YYNHTQTDES EIEGRHIYIY  120
VPDPDMAFVP LGMTDSLVIV EEDDSAIIPC RTTDPETQVT LHNNGRLVPA SYDSRQGFNG  180
TFSVGPYICE ATVKGRTFKT SEFNVYALKA TSELNLEMDA RQTVYKAGET IVVTCAVFNN  240
EVVDLQWTYP GEVRNKGITM LEEIKLPSIK LVYTLTVPKA TVKDSGEYEC AARQATKEVK  300
EMKRVTISVH EKGFVEIEPT FGQLEAVNLH EVREFVVEVQ AYPTPRISWL KDNLTLIENL  360
TEITTDVQKS QETRYQSKLK LIRAKEEDSG HYTIIVQNED DVKSYTFELS TLVPASILDL  420
VDDHHGSGGG QTVRCTAEGT PLPEIDWMIC KHIKKCNNDT SWTVLASNVS NIITELPRRG  480
RSTVEGRVSF AKVEETIAVR CLAKNNLSVV ARELKLVAPT LRSELTVAAA VLVLLVIVIV  540
SLIVLVVIWK QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG  600
SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH LGPHLNIVNL  660
LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFMSQHPEK PKKDLDIFGL NPADESTRSY  720
VILSFENNGD YMDMKQADTT QYVPMLERKE VSKYSDIQRS LYDRPASYKK KSMLDSEVKN  780
LLSDDDSEGL TLLDLLSFTY QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA  840
RDIMHDSNYV SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM  900
VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV QCWNSEPEKR PSFYHLSEIV ENLLPGQYKK  960
SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL KDWEGGLDEQ RLSADSGYII  1020
PLPDIDPVPE EEDLGKRNRH SSQTSEESAI ETGSSSSTFI KREDETIEDI DMMDDIGIDS  1080
SDLVEDSFL                                                          1089
FASTA
(Canonical)
>LipidDB-10090-01211|P26618
MGTSHQVFLVLSCLLTGPGLISCQLLLPSILPNENEKIVQLNSSFSLRCVGESEVSWQHP
MSEEDDPNVEIRSEENNSGLFVTVLEVVNASAAHTGWYTCYYNHTQTDESEIEGRHIYIY
VPDPDMAFVPLGMTDSLVIVEEDDSAIIPCRTTDPETQVTLHNNGRLVPASYDSRQGFNG
TFSVGPYICEATVKGRTFKTSEFNVYALKATSELNLEMDARQTVYKAGETIVVTCAVFNN
EVVDLQWTYPGEVRNKGITMLEEIKLPSIKLVYTLTVPKATVKDSGEYECAARQATKEVK
EMKRVTISVHEKGFVEIEPTFGQLEAVNLHEVREFVVEVQAYPTPRISWLKDNLTLIENL
TEITTDVQKSQETRYQSKLKLIRAKEEDSGHYTIIVQNEDDVKSYTFELSTLVPASILDL
VDDHHGSGGGQTVRCTAEGTPLPEIDWMICKHIKKCNNDTSWTVLASNVSNIITELPRRG
RSTVEGRVSFAKVEETIAVRCLAKNNLSVVARELKLVAPTLRSELTVAAAVLVLLVIVIV
SLIVLVVIWKQKPRYEIRWRVIESISPDGHEYIYVDPMQLPYDSRWEFPRDGLVLGRILG
SGAFGKVVEGTAYGLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGPHLNIVNL
LGACTKSGPIYIITEYCFYGDLVNYLHKNRDSFMSQHPEKPKKDLDIFGLNPADESTRSY
VILSFENNGDYMDMKQADTTQYVPMLERKEVSKYSDIQRSLYDRPASYKKKSMLDSEVKN
LLSDDDSEGLTLLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLA
RDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMM
VDSTFYNKIKSGYRMAKPDHATSEVYEIMVQCWNSEPEKRPSFYHLSEIVENLLPGQYKK
SYEKIHLDFLKSDHPAVARMRVDSDNAYIGVTYKNEEDKLKDWEGGLDEQRLSADSGYII
PLPDIDPVPEEEDLGKRNRHSSQTSEESAIETGSSSSTFIKREDETIEDIDMMDDIGIDS
SDLVEDSFL
Gene Ontology
GO:0009986; C:cell surface; IDA:BHF-UCL
GO:0005737; C:cytoplasm; ISS:UniProtKB
GO:0009897; C:external side of plasma membrane; IDA:MGI
GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB
GO:0005902; C:microvillus; IDA:MGI
GO:0005634; C:nucleus; ISS:UniProtKB
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0005018; F:platelet-derived growth factor alpha-receptor activity; IDA:UniProtKB
GO:0048407; F:platelet-derived growth factor binding; IDA:UniProtKB
GO:0042803; F:protein homodimerization activity; ISS:UniProtKB
GO:0005021; F:vascular endothelial growth factor-activated receptor activity; ISS:UniProtKB
GO:0030325; P:adrenal gland development; IGI:MGI
GO:0009653; P:anatomical structure morphogenesis; IMP:MGI
GO:0055003; P:cardiac myofibril assembly; IGI:UniProtKB
GO:0060326; P:cell chemotaxis; IMP:UniProtKB
GO:0016477; P:cell migration; IMP:UniProtKB
GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI
GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:UniProtKB
GO:0048557; P:embryonic digestive tract morphogenesis; IMP:UniProtKB
GO:0008210; P:estrogen metabolic process; IGI:MGI
GO:0030198; P:extracellular matrix organization; IMP:MGI
GO:0060325; P:face morphogenesis; IMP:MGI
GO:0008585; P:female gonad development; IGI:MGI
GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI
GO:0001701; P:in utero embryonic development; IMP:MGI
GO:0033327; P:Leydig cell differentiation; IMP:MGI
GO:0030324; P:lung development; IMP:MGI
GO:0001553; P:luteinization; IMP:MGI
GO:0030539; P:male genitalia development; IMP:MGI
GO:0072277; P:metanephric glomerular capillary formation; IGI:UniProtKB
GO:0010544; P:negative regulation of platelet activation; ISS:UniProtKB
GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI
GO:0009887; P:organ morphogenesis; IMP:MGI
GO:0060021; P:palate development; IMP:MGI
GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB
GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB
GO:0070527; P:platelet aggregation; ISS:UniProtKB
GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI
GO:0035790; P:platelet-derived growth factor receptor-alpha signaling pathway; IDA:UniProtKB
GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB
GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB
GO:0038091; P:positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway; ISS:BHF-UCL
GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:UniProtKB
GO:0045740; P:positive regulation of DNA replication; ISS:UniProtKB
GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB
GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB
GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB
GO:0010863; P:positive regulation of phospholipase C activity; IEA:Ensembl
GO:0046777; P:protein autophosphorylation; IDA:UniProtKB
GO:0050920; P:regulation of chemotaxis; IEA:Ensembl
GO:2000739; P:regulation of mesenchymal stem cell differentiation; ISS:UniProtKB
GO:0061298; P:retina vasculature development in camera-type eye; IGI:UniProtKB
GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI
GO:0048705; P:skeletal system morphogenesis; IMP:MGI
GO:0042060; P:wound healing; IMP:UniProtKB
Interpro
InterPro; IPR007110; Ig-like_dom
InterPro; IPR013783; Ig-like_fold
InterPro; IPR013098; Ig_I-set
InterPro; IPR003599; Ig_sub
InterPro; IPR003598; Ig_sub2
InterPro; IPR011009; Kinase-like_dom
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; IPR016243; Tyr_kinase_CSF1/PDGF_rcpt
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS
Pfam
Pfam; PF07679; I-set;
Pfam; PF07714; Pkinase_Tyr;
SMART
SMART; SM00409; IG;
SMART; SM00408; IGc2;
SMART; SM00219; TyrKc;
PROSITE
PROSITE; PS50835; IG_LIKE;
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS00240; RECEPTOR_TYR_KIN_III;
PRINTS