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P40197

- GPV_HUMAN

UniProt

P40197 - GPV_HUMAN

Protein

Platelet glycoprotein V

Gene

GP5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis.

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. blood coagulation, intrinsic pathway Source: Reactome
    3. cell adhesion Source: ProtInc
    4. cell-matrix adhesion Source: Ensembl
    5. negative regulation of platelet activation Source: Ensembl
    6. platelet activation Source: Reactome

    Keywords - Biological processi

    Blood coagulation, Cell adhesion, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_1230. Platelet Adhesion to exposed collagen.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_278. Platelet Aggregation (Plug Formation).
    REACT_326. Intrinsic Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet glycoprotein V
    Short name:
    GPV
    Alternative name(s):
    Glycoprotein 5
    CD_antigen: CD42d
    Gene namesi
    Name:GP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:4443. GP5.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28823.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 560544Platelet glycoprotein VPRO_0000021361Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi51 – 511N-linked (GlcNAc...)
    Glycosylationi181 – 1811N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi243 – 2431N-linked (GlcNAc...) (complex)1 Publication
    Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi298 – 2981N-linked (GlcNAc...)
    Glycosylationi312 – 3121N-linked (GlcNAc...)
    Glycosylationi385 – 3851N-linked (GlcNAc...)
    Glycosylationi499 – 4991N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP40197.
    PeptideAtlasiP40197.
    PRIDEiP40197.

    PTM databases

    PhosphoSiteiP40197.

    Miscellaneous databases

    PMAP-CutDBP40197.

    Expressioni

    Tissue specificityi

    Platelets and megakaryocytes.

    Gene expression databases

    ArrayExpressiP40197.
    BgeeiP40197.
    CleanExiHS_GP5.
    GenevestigatoriP40197.

    Interactioni

    Protein-protein interaction databases

    BioGridi109076. 1 interaction.
    MINTiMINT-1530430.
    STRINGi9606.ENSP00000319286.

    Structurei

    3D structure databases

    ProteinModelPortaliP40197.
    SMRiP40197. Positions 20-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 523507ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini545 – 56016CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei524 – 54421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 5034LRRNTAdd
    BLAST
    Repeati75 – 9622LRR 1Add
    BLAST
    Repeati99 – 12022LRR 2Add
    BLAST
    Repeati123 – 14422LRR 3Add
    BLAST
    Repeati147 – 16822LRR 4Add
    BLAST
    Repeati171 – 19323LRR 5Add
    BLAST
    Repeati195 – 21622LRR 6Add
    BLAST
    Repeati219 – 24022LRR 7Add
    BLAST
    Repeati243 – 26422LRR 8Add
    BLAST
    Repeati267 – 28822LRR 9Add
    BLAST
    Repeati291 – 31222LRR 10Add
    BLAST
    Repeati340 – 36122LRR 11Add
    BLAST
    Repeati364 – 38522LRR 12Add
    BLAST
    Repeati388 – 40922LRR 13Add
    BLAST
    Domaini421 – 47454LRRCTAdd
    BLAST

    Sequence similaritiesi

    Contains 13 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000112798.
    HOVERGENiHBG005906.
    InParanoidiP40197.
    KOiK06260.
    OMAiCPPACKC.
    OrthoDBiEOG712TVW.
    PhylomeDBiP40197.
    TreeFamiTF351124.

    Family and domain databases

    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF00560. LRR_1. 1 hit.
    PF13504. LRR_7. 1 hit.
    PF13855. LRR_8. 3 hits.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 9 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 12 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P40197-1 [UniParc]FASTAAdd to Basket

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    MLRGTLLCAV LGLLRAQPFP CPPACKCVFR DAAQCSGGDV ARISALGLPT    50
    NLTHILLFGM GRGVLQSQSF SGMTVLQRLM ISDSHISAVA PGTFSDLIKL 100
    KTLRLSRNKI THLPGALLDK MVLLEQLFLD HNALRGIDQN MFQKLVNLQE 150
    LALNQNQLDF LPASLFTNLE NLKLLDLSGN NLTHLPKGLL GAQAKLERLL 200
    LHSNRLVSLD SGLLNSLGAL TELQFHRNHI RSIAPGAFDR LPNLSSLTLS 250
    RNHLAFLPSA LFLHSHNLTL LTLFENPLAE LPGVLFGEMG GLQELWLNRT 300
    QLRTLPAAAF RNLSRLRYLG VTLSPRLSAL PQGAFQGLGE LQVLALHSNG 350
    LTALPDGLLR GLGKLRQVSL RRNRLRALPR ALFRNLSSLE SVQLDHNQLE 400
    TLPGDVFGAL PRLTEVLLGH NSWRCDCGLG PFLGWLRQHL GLVGGEEPPR 450
    CAGPGAHAGL PLWALPGGDA ECPGPRGPPP RPAADSSSEA PVHPALAPNS 500
    SEPWVWAQPV TTGKGQDHSP FWGFYFLLLA VQAMITVIIV FAMIKIGQLF 550
    RKLIRERALG 560
    Length:560
    Mass (Da):60,959
    Last modified:February 1, 1995 - v1
    Checksum:iB1CDB04AF8AF7115
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti130 – 1301D → W AA sequence (PubMed:2350580)Curated
    Sequence conflicti136 – 1383GID → PGG AA sequence (PubMed:2350580)Curated
    Sequence conflicti267 – 2671N → H AA sequence (PubMed:2350580)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11238 mRNA. Translation: AAA03069.1.
    Z23091 Genomic DNA. Translation: CAA80637.1.
    GU138099 Genomic DNA. Translation: ACZ44929.1.
    CH471052 Genomic DNA. Translation: EAW78053.1.
    CCDSiCCDS3307.1.
    PIRiA48030. A60164.
    RefSeqiNP_004479.1. NM_004488.2.
    UniGeneiHs.73734.

    Genome annotation databases

    EnsembliENST00000401815; ENSP00000383931; ENSG00000178732.
    GeneIDi2814.
    KEGGihsa:2814.
    UCSCiuc003ftv.1. human.

    Polymorphism databases

    DMDMi729616.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11238 mRNA. Translation: AAA03069.1 .
    Z23091 Genomic DNA. Translation: CAA80637.1 .
    GU138099 Genomic DNA. Translation: ACZ44929.1 .
    CH471052 Genomic DNA. Translation: EAW78053.1 .
    CCDSi CCDS3307.1.
    PIRi A48030. A60164.
    RefSeqi NP_004479.1. NM_004488.2.
    UniGenei Hs.73734.

    3D structure databases

    ProteinModelPortali P40197.
    SMRi P40197. Positions 20-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109076. 1 interaction.
    MINTi MINT-1530430.
    STRINGi 9606.ENSP00000319286.

    PTM databases

    PhosphoSitei P40197.

    Polymorphism databases

    DMDMi 729616.

    Proteomic databases

    PaxDbi P40197.
    PeptideAtlasi P40197.
    PRIDEi P40197.

    Protocols and materials databases

    DNASUi 2814.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000401815 ; ENSP00000383931 ; ENSG00000178732 .
    GeneIDi 2814.
    KEGGi hsa:2814.
    UCSCi uc003ftv.1. human.

    Organism-specific databases

    CTDi 2814.
    GeneCardsi GC03M194115.
    HGNCi HGNC:4443. GP5.
    MIMi 173511. gene.
    neXtProti NX_P40197.
    PharmGKBi PA28823.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000112798.
    HOVERGENi HBG005906.
    InParanoidi P40197.
    KOi K06260.
    OMAi CPPACKC.
    OrthoDBi EOG712TVW.
    PhylomeDBi P40197.
    TreeFami TF351124.

    Enzyme and pathway databases

    Reactomei REACT_1230. Platelet Adhesion to exposed collagen.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_278. Platelet Aggregation (Plug Formation).
    REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    GeneWikii GP5.
    GenomeRNAii 2814.
    NextBioi 11093.
    PMAP-CutDB P40197.
    PROi P40197.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40197.
    Bgeei P40197.
    CleanExi HS_GP5.
    Genevestigatori P40197.

    Family and domain databases

    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF00560. LRR_1. 1 hit.
    PF13504. LRR_7. 1 hit.
    PF13855. LRR_8. 3 hits.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 9 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 12 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human platelet glycoprotein V: characterization of the polypeptide and the related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins."
      Hickey M.J., Hagen F.S., Yagi M., Roth G.J.
      Proc. Natl. Acad. Sci. U.S.A. 90:8327-8331(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    2. "Cloning and characterization of the gene encoding the human platelet glycoprotein V. A member of the leucine-rich glycoprotein family cleaved during thrombin-induced platelet activation."
      Lanza F., Morales M., de la Salle C., Cazenave J.-P., Clemetson K.J., Shimomura T., Phillips D.R.
      J. Biol. Chem. 268:20801-20807(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Platelet.
    3. "Single novel mutation in transmembrane region of glycoprotein IX affects platelet surface expressions of glycoprotein GP-Ib-IX complex and causes Bernard Soulier syndrome."
      Xu L., Liu L., Zhang D., Sun G., Wang P., Sun N., Hu Q., Li X., Cao F., Peng B., Yu S.
      Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Rapid purification and characterization of human platelet glycoprotein V: the amino acid sequence contains leucine-rich repetitive modules as in glycoprotein Ib."
      Shimomura T., Fujimura K., Maehama S., Takemoto M., Oda K., Fujimoto T., Oyama R., Suzuki M., Icihara-Tanaka K., Titani K., Kuramoto A.
      Blood 75:2349-2356(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Platelet.
    6. "Human platelet glycoprotein V: a surface leucine-rich glycoprotein related to adhesion."
      Roth G.J., Church T.A., McMullen B.A., Williams S.A.
      Biochem. Biophys. Res. Commun. 170:153-161(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Platelet.
    7. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181.
      Tissue: Platelet.
    8. Cited for: GLYCOSYLATION AT ASN-181 AND ASN-243.

    Entry informationi

    Entry nameiGPV_HUMAN
    AccessioniPrimary (citable) accession number: P40197
    Secondary accession number(s): D1MER9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 133 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3