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P26618

- PGFRA_MOUSE

UniProt

P26618 - PGFRA_MOUSE

Protein

Platelet-derived growth factor receptor alpha

Gene

Pdgfra

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    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 Ca2+ 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.4 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Enzyme regulationi

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei627 – 6271ATPPROSITE-ProRule annotation
    Active sitei818 – 8181Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi599 – 6079ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. platelet-derived growth factor alpha-receptor activity Source: UniProtKB
    3. platelet-derived growth factor binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. vascular endothelial growth factor-activated receptor activity Source: UniProtKB

    GO - Biological processi

    1. adrenal gland development Source: MGI
    2. anatomical structure morphogenesis Source: MGI
    3. cardiac myofibril assembly Source: UniProtKB
    4. cell chemotaxis Source: UniProtKB
    5. cell migration Source: UniProtKB
    6. cellular response to amino acid stimulus Source: MGI
    7. embryonic cranial skeleton morphogenesis Source: UniProtKB
    8. embryonic digestive tract morphogenesis Source: UniProtKB
    9. estrogen metabolic process Source: MGI
    10. extracellular matrix organization Source: MGI
    11. face morphogenesis Source: MGI
    12. female gonad development Source: MGI
    13. hematopoietic progenitor cell differentiation Source: MGI
    14. in utero embryonic development Source: MGI
    15. Leydig cell differentiation Source: MGI
    16. lung development Source: MGI
    17. luteinization Source: MGI
    18. male genitalia development Source: MGI
    19. metanephric glomerular capillary formation Source: UniProtKB
    20. negative regulation of platelet activation Source: UniProtKB
    21. odontogenesis of dentin-containing tooth Source: MGI
    22. organ morphogenesis Source: MGI
    23. palate development Source: MGI
    24. peptidyl-tyrosine phosphorylation Source: UniProtKB
    25. phosphatidylinositol-mediated signaling Source: UniProtKB
    26. platelet aggregation Source: UniProtKB
    27. platelet-derived growth factor receptor-alpha signaling pathway Source: UniProtKB
    28. platelet-derived growth factor receptor signaling pathway Source: MGI
    29. positive regulation of cell migration Source: UniProtKB
    30. positive regulation of cell proliferation Source: UniProtKB
    31. positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway Source: BHF-UCL
    32. positive regulation of cytosolic calcium ion concentration Source: UniProtKB
    33. positive regulation of DNA replication Source: UniProtKB
    34. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    35. positive regulation of fibroblast proliferation Source: UniProtKB
    36. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    37. positive regulation of phospholipase C activity Source: Ensembl
    38. protein autophosphorylation Source: UniProtKB
    39. regulation of chemotaxis Source: Ensembl
    40. regulation of mesenchymal stem cell differentiation Source: UniProtKB
    41. retina vasculature development in camera-type eye Source: UniProtKB
    42. signal transduction involved in regulation of gene expression Source: MGI
    43. skeletal system morphogenesis Source: MGI
    44. wound healing Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Chemotaxis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.
    ReactomeiREACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet-derived growth factor receptor alpha (EC:2.7.10.1)
    Short name:
    PDGF-R-alpha
    Short name:
    PDGFR-alpha
    Alternative name(s):
    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
    Gene namesi
    Name:Pdgfra
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:97530. Pdgfra.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein
    Note: The activated receptor is rapidly internalized and degraded.By similarity

    GO - Cellular componenti

    1. cell surface Source: BHF-UCL
    2. cytoplasm Source: UniProtKB
    3. external side of plasma membrane Source: MGI
    4. integral component of plasma membrane Source: UniProtKB
    5. microvillus Source: MGI
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Embryonically lethal. Most embryos survive up to 13 dpc, but display important defects in skeleton development, including spina bifida, fusions of cervical vertebrae and ribs, and incomplete fusion of the skull parietal bone. Embryos display also abnormal mucosa lining the gastrointestinal tract, including fewer and misshapen villi and loss of pericryptal mesenchyme. At about 16 dpc, embryos display extensive hemorrhaging.3 Publications

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 10891065Platelet-derived growth factor receptor alphaPRO_0000016761Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi49 ↔ 100PROSITE-ProRule annotation
    Glycosylationi76 – 761N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi150 ↔ 189PROSITE-ProRule annotation
    Glycosylationi179 – 1791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi235 ↔ 290PROSITE-ProRule annotation
    Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi435 ↔ 501PROSITE-ProRule annotation
    Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi506 – 5061N-linked (GlcNAc...)Sequence Analysis
    Modified residuei555 – 5551PhosphotyrosineBy similarity
    Modified residuei572 – 5721Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei574 – 5741Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei582 – 5821PhosphotyrosineBy similarity
    Modified residuei720 – 7201Phosphotyrosine; by autocatalysisCurated
    Modified residuei731 – 7311Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei742 – 7421Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei754 – 7541Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei762 – 7621Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei768 – 7681Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei849 – 8491Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei944 – 9441PhosphotyrosineBy similarity
    Modified residuei958 – 9581PhosphotyrosineBy similarity
    Modified residuei962 – 9621PhosphotyrosineBy similarity
    Modified residuei988 – 9881Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei993 – 9931PhosphotyrosineBy similarity
    Modified residuei1018 – 10181Phosphotyrosine; by autocatalysis

    Post-translational modificationi

    Ubiquitinated, leading to its degradation.By similarity
    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.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP26618.
    PRIDEiP26618.

    PTM databases

    PhosphoSiteiP26618.

    Expressioni

    Tissue specificityi

    Focally expressed in cortical interstitial cells and highly expressed in the interstitium of the papillary region. Also expressed by adventitial cells in arterial vessels. Up-regulated in areas of renal fibrosis. In mice with unilateral ureteral obstruction, expression in cortical interstitial cells becomes prominent at day 4 which increases progressively until day 14.1 Publication

    Gene expression databases

    ArrayExpressiP26618.
    BgeeiP26618.
    GenevestigatoriP26618.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi202088. 1 interaction.
    IntActiP26618. 3 interactions.
    MINTiMINT-4107325.

    Structurei

    3D structure databases

    ProteinModelPortaliP26618.
    SMRiP26618. Positions 28-507, 553-997.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 528504ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini550 – 1089540CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei529 – 54921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 11389Ig-like C2-type 1Add
    BLAST
    Domaini117 – 20185Ig-like C2-type 2Add
    BLAST
    Domaini202 – 306105Ig-like C2-type 3Add
    BLAST
    Domaini319 – 41092Ig-like C2-type 4Add
    BLAST
    Domaini414 – 517104Ig-like C2-type 5Add
    BLAST
    Domaini593 – 954362Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108490.
    HOGENOMiHOG000112009.
    HOVERGENiHBG004335.
    InParanoidiP26618.
    KOiK04363.
    OMAiDYECAAR.
    OrthoDBiEOG71G9T1.
    PhylomeDBiP26618.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR027290. PDGFRA.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    [Graphical view]
    PANTHERiPTHR24416:SF52. PTHR24416:SF52. 1 hit.
    PfamiPF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500950. Alpha-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTiSM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50835. IG_LIKE. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P26618-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGTSHQVFLV LSCLLTGPGL ISCQLLLPSI LPNENEKIVQ LNSSFSLRCV     50
    GESEVSWQHP MSEEDDPNVE IRSEENNSGL FVTVLEVVNA SAAHTGWYTC 100
    YYNHTQTDES EIEGRHIYIY VPDPDMAFVP LGMTDSLVIV EEDDSAIIPC 150
    RTTDPETQVT LHNNGRLVPA SYDSRQGFNG TFSVGPYICE ATVKGRTFKT 200
    SEFNVYALKA TSELNLEMDA RQTVYKAGET IVVTCAVFNN EVVDLQWTYP 250
    GEVRNKGITM LEEIKLPSIK LVYTLTVPKA TVKDSGEYEC AARQATKEVK 300
    EMKRVTISVH EKGFVEIEPT FGQLEAVNLH EVREFVVEVQ AYPTPRISWL 350
    KDNLTLIENL TEITTDVQKS QETRYQSKLK LIRAKEEDSG HYTIIVQNED 400
    DVKSYTFELS TLVPASILDL VDDHHGSGGG QTVRCTAEGT PLPEIDWMIC 450
    KHIKKCNNDT SWTVLASNVS NIITELPRRG RSTVEGRVSF AKVEETIAVR 500
    CLAKNNLSVV ARELKLVAPT LRSELTVAAA VLVLLVIVIV SLIVLVVIWK 550
    QKPRYEIRWR VIESISPDGH EYIYVDPMQL PYDSRWEFPR DGLVLGRILG 600
    SGAFGKVVEG TAYGLSRSQP VMKVAVKMLK PTARSSEKQA LMSELKIMTH 650
    LGPHLNIVNL LGACTKSGPI YIITEYCFYG DLVNYLHKNR DSFMSQHPEK 700
    PKKDLDIFGL NPADESTRSY VILSFENNGD YMDMKQADTT QYVPMLERKE 750
    VSKYSDIQRS LYDRPASYKK KSMLDSEVKN LLSDDDSEGL TLLDLLSFTY 800
    QVARGMEFLA SKNCVHRDLA ARNVLLAQGK IVKICDFGLA RDIMHDSNYV 850
    SKGSTFLPVK WMAPESIFDN LYTTLSDVWS YGILLWEIFS LGGTPYPGMM 900
    VDSTFYNKIK SGYRMAKPDH ATSEVYEIMV QCWNSEPEKR PSFYHLSEIV 950
    ENLLPGQYKK SYEKIHLDFL KSDHPAVARM RVDSDNAYIG VTYKNEEDKL 1000
    KDWEGGLDEQ RLSADSGYII PLPDIDPVPE EEDLGKRNRH SSQTSEESAI 1050
    ETGSSSSTFI KREDETIEDI DMMDDIGIDS SDLVEDSFL 1089
    Length:1,089
    Mass (Da):122,683
    Last modified:February 26, 2008 - v3
    Checksum:i07AAFD2BAA12533A
    GO
    Isoform 2 (identifier: P26618-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         775-790: DSEVKNLLSDDDSEGL → GKSAHAHSGKYDLSVV
         791-1089: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:790
    Mass (Da):88,629
    Checksum:iFE13756876B68B95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651D → E in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti65 – 651D → E in AAA39904. (PubMed:1321404)Curated
    Sequence conflicti192 – 1921T → A in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti202 – 2021E → A in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti252 – 2521E → G in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti271 – 2711L → V in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti322 – 3221G → S in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti326 – 3261A → P in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti439 – 4402GT → EG in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti472 – 4721I → V in BAE37548. (PubMed:16141072)Curated
    Sequence conflicti529 – 5291A → E in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti737 – 7371A → D in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti849 – 8491Y → D in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti936 – 9361E → D in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti950 – 9501V → L in AAA39733. (PubMed:2174116)Curated
    Sequence conflicti1005 – 10051G → S in AAA39904. (PubMed:1321404)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei775 – 79016DSEVK…DSEGL → GKSAHAHSGKYDLSVV in isoform 2. 1 PublicationVSP_031877Add
    BLAST
    Alternative sequencei791 – 1089299Missing in isoform 2. 1 PublicationVSP_031878Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57683 mRNA. Translation: AAA39733.1.
    M84607 mRNA. Translation: AAA39904.1.
    AK081664 mRNA. Translation: BAC38283.1.
    AK136490 mRNA. Translation: BAE23004.1.
    AK147267 mRNA. Translation: BAE27808.1.
    AK163952 mRNA. Translation: BAE37548.1.
    BC053036 mRNA. Translation: AAH53036.1.
    CCDSiCCDS19351.1. [P26618-1]
    PIRiI57511. S33727.
    RefSeqiNP_001076785.1. NM_001083316.1. [P26618-1]
    NP_035188.2. NM_011058.2. [P26618-1]
    XP_006504324.1. XM_006504261.1. [P26618-1]
    XP_006504325.1. XM_006504262.1. [P26618-1]
    XP_006504326.1. XM_006504263.1. [P26618-1]
    UniGeneiMm.221403.

    Genome annotation databases

    EnsembliENSMUST00000000476; ENSMUSP00000000476; ENSMUSG00000029231. [P26618-1]
    ENSMUST00000168162; ENSMUSP00000127173; ENSMUSG00000029231. [P26618-1]
    GeneIDi18595.
    KEGGimmu:18595.
    UCSCiuc008xub.1. mouse. [P26618-2]
    uc008xuc.1. mouse. [P26618-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57683 mRNA. Translation: AAA39733.1 .
    M84607 mRNA. Translation: AAA39904.1 .
    AK081664 mRNA. Translation: BAC38283.1 .
    AK136490 mRNA. Translation: BAE23004.1 .
    AK147267 mRNA. Translation: BAE27808.1 .
    AK163952 mRNA. Translation: BAE37548.1 .
    BC053036 mRNA. Translation: AAH53036.1 .
    CCDSi CCDS19351.1. [P26618-1 ]
    PIRi I57511. S33727.
    RefSeqi NP_001076785.1. NM_001083316.1. [P26618-1 ]
    NP_035188.2. NM_011058.2. [P26618-1 ]
    XP_006504324.1. XM_006504261.1. [P26618-1 ]
    XP_006504325.1. XM_006504262.1. [P26618-1 ]
    XP_006504326.1. XM_006504263.1. [P26618-1 ]
    UniGenei Mm.221403.

    3D structure databases

    ProteinModelPortali P26618.
    SMRi P26618. Positions 28-507, 553-997.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202088. 1 interaction.
    IntActi P26618. 3 interactions.
    MINTi MINT-4107325.

    Chemistry

    BindingDBi P26618.
    ChEMBLi CHEMBL2096980.

    PTM databases

    PhosphoSitei P26618.

    Proteomic databases

    PaxDbi P26618.
    PRIDEi P26618.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000476 ; ENSMUSP00000000476 ; ENSMUSG00000029231 . [P26618-1 ]
    ENSMUST00000168162 ; ENSMUSP00000127173 ; ENSMUSG00000029231 . [P26618-1 ]
    GeneIDi 18595.
    KEGGi mmu:18595.
    UCSCi uc008xub.1. mouse. [P26618-2 ]
    uc008xuc.1. mouse. [P26618-1 ]

    Organism-specific databases

    CTDi 5156.
    MGIi MGI:97530. Pdgfra.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108490.
    HOGENOMi HOG000112009.
    HOVERGENi HBG004335.
    InParanoidi P26618.
    KOi K04363.
    OMAi DYECAAR.
    OrthoDBi EOG71G9T1.
    PhylomeDBi P26618.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.
    Reactomei REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi PDGFRA. mouse.
    NextBioi 294480.
    PROi P26618.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26618.
    Bgeei P26618.
    Genevestigatori P26618.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR027290. PDGFRA.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    [Graphical view ]
    PANTHERi PTHR24416:SF52. PTHR24416:SF52. 1 hit.
    Pfami PF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500950. Alpha-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTi SM00409. IG. 2 hits.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50835. IG_LIKE. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Retinoic acid promotes transcription of the platelet-derived growth factor alpha-receptor gene."
      Stiles C.D., Wang C.
      Mol. Cell. Biol. 10:6781-6784(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Mouse platelet-derived growth factor alpha receptor: sequence, tissue-specific expression and correlation with metastatic phenotype."
      Do M.S., Fitzer-Attas C., Gubbay J., Greenfeld L., Feldman M., Eisenbach L.
      Oncogene 7:1567-1575(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Cerebellum, Colon, Embryonic head and Placenta.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.
    5. "The PDGF alpha receptor is required for neural crest cell development and for normal patterning of the somites."
      Soriano P.
      Development 124:2691-2700(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    6. "Abnormal gastrointestinal development in PDGF-A and PDGFR-(alpha) deficient mice implicates a novel mesenchymal structure with putative instructive properties in villus morphogenesis."
      Karlsson L., Lindahl P., Heath J.K., Betsholtz C.
      Development 127:3457-3466(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    7. "Platelet-derived growth factor-mediated signaling through the Shb adaptor protein: effects on cytoskeletal organization."
      Hooshmand-Rad R., Lu L., Heldin C.-H., Claesson-Welsh L., Welsh M.
      Exp. Cell Res. 257:245-254(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    8. "Obstructive uropathy in mice and humans: potential role for PDGF-D in the progression of tubulointerstitial injury."
      Taneda S., Hudkins K.L., Topouzis S., Gilbertson D.G., Ophascharoensuk V., Truong L., Johnson R.J., Alpers C.E.
      J. Am. Soc. Nephrol. 14:2544-2555(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. "Insight into the physiological functions of PDGF through genetic studies in mice."
      Betsholtz C.
      Cytokine Growth Factor Rev. 15:215-228(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION, DISRUPTION PHENOTYPE.
    10. "Comprehensive dissection of PDGF-PDGFR signaling pathways in PDGFR genetically defined cells."
      Wu E., Palmer N., Tian Z., Moseman A.P., Galdzicki M., Wang X., Berger B., Zhang H., Kohane I.S.
      PLoS ONE 3:E3794-E3794(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Directional cell migration and chemotaxis in wound healing response to PDGF-AA are coordinated by the primary cilium in fibroblasts."
      Schneider L., Cammer M., Lehman J., Nielsen S.K., Guerra C.F., Veland I.R., Stock C., Hoffmann E.K., Yoder B.K., Schwab A., Satir P., Christensen S.T.
      Cell. Physiol. Biochem. 25:279-292(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiPGFRA_MOUSE
    AccessioniPrimary (citable) accession number: P26618
    Secondary accession number(s): Q3TQ37
    , Q62046, Q7TSJ3, Q8C4N3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 151 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3