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P26619

- PGFRA_XENLA

UniProt

P26619 - PGFRA_XENLA

Protein

Platelet-derived growth factor receptor alpha

Gene

pdgfra

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      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. Required for normal development of the gastrointestinal tract. 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 By similarity.By similarity

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei629 – 6291ATPPROSITE-ProRule annotation
    Active sitei818 – 8181Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi601 – 6099ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. platelet-derived growth factor alpha-receptor activity Source: InterPro

    GO - Biological processi

    1. chemotaxis Source: UniProtKB-KW
    2. multicellular organismal development Source: UniProtKB-KW

    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. 6726.

    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
    Gene namesi
    Name:pdgfra
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-6072934. 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. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 10871063Platelet-derived growth factor receptor alphaPRO_0000016763Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 101PROSITE-ProRule annotation
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi151 ↔ 192PROSITE-ProRule annotation
    Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi238 ↔ 293PROSITE-ProRule annotation
    Glycosylationi282 – 2821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi438 ↔ 503PROSITE-ProRule annotation
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
    Modified residuei574 – 5741Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei576 – 5761Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei722 – 7221Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei733 – 7331Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei744 – 7441Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei756 – 7561Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei764 – 7641Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei849 – 8491Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei988 – 9881Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1017 – 10171Phosphotyrosine; by autocatalysisBy similarity

    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 By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP26619.
    SMRiP26619. Positions 553-695, 785-951.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 530506ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini552 – 1087536CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei531 – 55121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 11488Ig-like C2-type 1Add
    BLAST
    Domaini118 – 21194Ig-like C2-type 2Add
    BLAST
    Domaini217 – 30993Ig-like C2-type 3Add
    BLAST
    Domaini315 – 40995Ig-like C2-type 4Add
    BLAST
    Domaini417 – 519103Ig-like C2-type 5Add
    BLAST
    Domaini595 – 970376Protein 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

    HOVERGENiHBG004335.

    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.
    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. 2 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500950. Alpha-PDGF_receptor. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTiSM00409. IG. 2 hits.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P26619-1 [UniParc]FASTAAdd to Basket

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    MMPAMRASLI LGCLLIIGPW AILAENPLPT IFPDKDELVQ ALHSSFTLKC     50
    TGESEVSWQN PNSNPEKQNV VIRSEENNSG LFVSILEVSD ASAFDTGLYT 100
    CYHNHTQTEE SEIEGTDIYI YVPDPNVPFA PPGLFDHIIV VEEDESALVP 150
    CRTTDPSSEV TLKNIESSRT VFAFYDSKQG FAGNFPPGSY ICETTSNKMV 200
    YQTEPYILQT WKATHNISVE MEAPKTMFRA GETIAIDCIV LDNEVVDLKW 250
    TYPGKQRGVG IRNVEESKVP YQRLVYTLTL ANATTEDSGE YECAVIHATL 300
    DNRVVKKTNI TVHEKGFIDL EPMFGSEEFA NLHEVKSFIV NLHAYPTPGL 350
    FWLKDNRTLS ENLTEITTSI VTTKETRFQS KLKLIRAKEE DSGLYTLVAQ 400
    NDRETKSYSF ILQIKVPALI LELVDKHHGA SGEQTVGCLA KGMPVPDVEW 450
    LVCKDIKRCN NDTLWSILAT NGSEISMETH QDDEQIESQV TFKKIEETMA 500
    IRCIAKNELG VVARELKLVA PTLRSELTVA AAVLVLLVIV IISLIVLVII 550
    WKQKPRYEIR WRVIESISPD GHEYIYVDPM QLPYDSRWEF PRDGLVLGRI 600
    LGSGAFGKVV EGAAYGLSRS QPVMKVAVKM LKPTARSSEK QALMSELKIM 650
    THLGAHLNIV NLLGACTKSG PIYIITEYCF YGDLVNYLHK NRDNFQSRHP 700
    EKPKKDLDIF GLNPADESTR SYVILSFENN GDYMDMKQAD TMQYVPMLEM 750
    KEPSKYSDIQ RSLYDRPASY KKKPLSEVKN ILSDDGFEGL TVLDLLSFTY 800
    QVARGMEFLA SKNCVHRDLA ARNVLLAHGK IVKICDFGLA RDIMHDSNYV 850
    SKGSTFLPVK WMAPESIFDN LYTTLSDVWS FGILLWEIFS LGGTPYPGMI 900
    VDSTFYNKIK SGYRMAKPDH ATHEVYDIMV KCWNSEPEKR PSFRHLSDIV 950
    ESLLPMEYKR CYETVLHDFL KSDHPAVTRM RSDSDNSYIG VTYKNEHKMK 1000
    DRESGFDEQR LSADSGYIIP LPDIDPVSED ESGKRNRHSS QTSEESAIET 1050
    GSSSSTFIKR DDETIEDIDM MDDIGIDSSD LVEDSFL 1087
    Length:1,087
    Mass (Da):122,699
    Last modified:August 1, 1992 - v1
    Checksum:iA621E6B0A5BADCA6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80798 mRNA. Translation: AAA49929.1.
    PIRiI51552.
    UniGeneiXl.20029.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80798 mRNA. Translation: AAA49929.1 .
    PIRi I51552.
    UniGenei Xl.20029.

    3D structure databases

    ProteinModelPortali P26619.
    SMRi P26619. Positions 553-695, 785-951.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Xenbasei XB-GENE-6072934. pdgfra.

    Phylogenomic databases

    HOVERGENi HBG004335.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 6726.

    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.
    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. 2 hits.
    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.
    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. "The Xenopus platelet-derived growth factor alpha receptor: cDNA cloning and demonstration that mesoderm induction establishes the lineage-specific pattern of ligand and receptor gene expression."
      Jones S.D., Ho L., Smith J.C., Yordan C., Stiles C.D., Mercola M.
      Dev. Genet. 14:185-193(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPGFRA_XENLA
    AccessioniPrimary (citable) accession number: P26619
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3