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P40197 (GPV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet glycoprotein V

Short name=GPV
Alternative name(s):
Glycoprotein 5
CD_antigen=CD42d
Gene names
Name:GP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Platelets and megakaryocytes.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Contains 13 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 560544Platelet glycoprotein V
PRO_0000021361

Regions

Topological domain17 – 523507Extracellular Potential
Transmembrane524 – 54421Helical; Potential
Topological domain545 – 56016Cytoplasmic Potential
Domain17 – 5034LRRNT
Repeat75 – 9622LRR 1
Repeat99 – 12022LRR 2
Repeat123 – 14422LRR 3
Repeat147 – 16822LRR 4
Repeat171 – 19323LRR 5
Repeat195 – 21622LRR 6
Repeat219 – 24022LRR 7
Repeat243 – 26422LRR 8
Repeat267 – 28822LRR 9
Repeat291 – 31222LRR 10
Repeat340 – 36122LRR 11
Repeat364 – 38522LRR 12
Repeat388 – 40922LRR 13
Domain421 – 47454LRRCT

Amino acid modifications

Glycosylation511N-linked (GlcNAc...)
Glycosylation1811N-linked (GlcNAc...) (complex) Ref.7 Ref.8
Glycosylation2431N-linked (GlcNAc...) (complex) Ref.8
Glycosylation2671N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...)
Glycosylation3121N-linked (GlcNAc...)
Glycosylation3851N-linked (GlcNAc...)
Glycosylation4991N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1301D → W AA sequence Ref.5
Sequence conflict136 – 1383GID → PGG AA sequence Ref.5
Sequence conflict2671N → H AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P40197 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: B1CDB04AF8AF7115

FASTA56060,959
        10         20         30         40         50         60 
MLRGTLLCAV LGLLRAQPFP CPPACKCVFR DAAQCSGGDV ARISALGLPT NLTHILLFGM 

        70         80         90        100        110        120 
GRGVLQSQSF SGMTVLQRLM ISDSHISAVA PGTFSDLIKL KTLRLSRNKI THLPGALLDK 

       130        140        150        160        170        180 
MVLLEQLFLD HNALRGIDQN MFQKLVNLQE LALNQNQLDF LPASLFTNLE NLKLLDLSGN 

       190        200        210        220        230        240 
NLTHLPKGLL GAQAKLERLL LHSNRLVSLD SGLLNSLGAL TELQFHRNHI RSIAPGAFDR 

       250        260        270        280        290        300 
LPNLSSLTLS RNHLAFLPSA LFLHSHNLTL LTLFENPLAE LPGVLFGEMG GLQELWLNRT 

       310        320        330        340        350        360 
QLRTLPAAAF RNLSRLRYLG VTLSPRLSAL PQGAFQGLGE LQVLALHSNG LTALPDGLLR 

       370        380        390        400        410        420 
GLGKLRQVSL RRNRLRALPR ALFRNLSSLE SVQLDHNQLE TLPGDVFGAL PRLTEVLLGH 

       430        440        450        460        470        480 
NSWRCDCGLG PFLGWLRQHL GLVGGEEPPR CAGPGAHAGL PLWALPGGDA ECPGPRGPPP 

       490        500        510        520        530        540 
RPAADSSSEA PVHPALAPNS SEPWVWAQPV TTGKGQDHSP FWGFYFLLLA VQAMITVIIV 

       550        560 
FAMIKIGQLF RKLIRERALG 

« Hide

References

« Hide 'large scale' references
[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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-181 AND ASN-243.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L11238 mRNA. Translation: AAA03069.1.
Z23091 Genomic DNA. Translation: CAA80637.1.
GU138099 Genomic DNA. Translation: ACZ44929.1.
CH471052 Genomic DNA. Translation: EAW78053.1.
CCDSCCDS3307.1.
PIRA60164. A48030.
RefSeqNP_004479.1. NM_004488.2.
UniGeneHs.73734.

3D structure databases

ProteinModelPortalP40197.
SMRP40197. Positions 20-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109076. 1 interaction.
MINTMINT-1530430.
STRING9606.ENSP00000319286.

PTM databases

PhosphoSiteP40197.

Polymorphism databases

DMDM729616.

Proteomic databases

PaxDbP40197.
PeptideAtlasP40197.
PRIDEP40197.

Protocols and materials databases

DNASU2814.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323007; ENSP00000319286; ENSG00000178732.
ENST00000401815; ENSP00000383931; ENSG00000178732.
GeneID2814.
KEGGhsa:2814.
UCSCuc003ftv.1. human.

Organism-specific databases

CTD2814.
GeneCardsGC03M194115.
HGNCHGNC:4443. GP5.
MIM173511. gene.
neXtProtNX_P40197.
PharmGKBPA28823.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000112798.
HOVERGENHBG005906.
InParanoidP40197.
KOK06260.
OMACPPACKC.
OrthoDBEOG712TVW.
PhylomeDBP40197.
TreeFamTF351124.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP40197.
BgeeP40197.
CleanExHS_GP5.
GenevestigatorP40197.

Family and domain databases

InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 3 hits.
[Graphical view]
SMARTSM00369. LRR_TYP. 9 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 12 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGP5.
GenomeRNAi2814.
NextBio11093.
PMAP-CutDBP40197.
PROP40197.
SOURCESearch...

Entry information

Entry nameGPV_HUMAN
AccessionPrimary (citable) accession number: P40197
Secondary accession number(s): D1MER9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries