GP5 (gene)

GP5
Identifiers
Aliases	GP5, CD42d, GPV, glycoprotein V platelet
External IDs	OMIM: 173511 MGI: 1096363 HomoloGene: 74523 GeneCards: GP5
Gene location (Human)
Chr.	Chromosome 3 (human)[1]
End	194,399,266 bp[1]
Gene location (Mouse)
Chr.	Chromosome 16 (mouse)[2]
End	30,129,597 bp[2]
RNA expression pattern
	Top expressed in
	monocyte; ; cancellous bone; ; right uterine tube; ; bronchial epithelial cell; ; lymph node; ; blood; ; appendix; ; bone marrow; ; gallbladder; ; thymus;
	Top expressed in
	blood; ; morula; ; spleen; ; yolk sac; ; abdominal wall; ; bone marrow; ; lip; ; body of femur; ; lung; ; cerebellar cortex;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding;
Cellular component	integral component of membrane; plasma membrane; integral component of plasma membrane; extracellular exosome; membrane; extracellular space;
Biological process	platelet activation; blood coagulation, intrinsic pathway; hemostasis; cell adhesion; blood coagulation; axonogenesis;
	Sources:Amigo / QuickGO
Orthologs
	2814
	14729
	ENSG00000178732
	ENSMUSG00000047953
	P40197
	O08742; Q9QZU3
	NM_004488
	NM_008148
	NP_004479
	NP_032174
	Wikidata
View/Edit Human	View/Edit Mouse

Glycoprotein V (platelet) (GP5) also known as CD42d (Cluster of Differentiation 42d), is a human gene.[5]

Human platelet glycoprotein V (GP5) is a part of the Ib-V-IX system of surface glycoproteins that constitute the receptor for von Willebrand factor (VWF; MIM 193400) and mediate the adhesion of platelets to injured vascular surfaces in the arterial circulation, a critical initiating event in hemostasis. The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain (GP1BA; MIM 606672) and a beta chain (GP1BB; MIM 138720), that are linked by disulfide bonds. The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX (GP9; MIM 173515) and GP5. Mutations in GP1BA, GP1BB, and GP9 have been shown to cause Bernard-Soulier syndrome (MIM 231200), a bleeding disorder.[supplied by OMIM][5]

References

GRCh38: Ensembl release 89: ENSG00000178732 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000047953 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: GP5 glycoprotein V (platelet)".

Modderman PW, Admiraal LG, Sonnenberg A, von dem Borne AE (1992). "Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane". J. Biol. Chem. 267 (1): 364–9. doi:10.1016/S0021-9258(18)48503-1. PMID 1730602.
Shimomura T, Fujimura K, Maehama S, et al. (1990). "Rapid purification and characterization of human platelet glycoprotein V: the amino acid sequence contains leucine-rich repetitive modules as in glycoprotein Ib". Blood. 75 (12): 2349–56. doi:10.1182/blood.V75.12.2349.2349. PMID 2350580.
Roth GJ, Church TA, McMullen BA, Williams SA (1990). "Human platelet glycoprotein V: a surface leucine-rich glycoprotein related to adhesion". Biochem. Biophys. Res. Commun. 170 (1): 153–61. doi:10.1016/0006-291X(90)91253-O. PMID 2372284.
Hickey MJ, Hagen FS, Yagi M, Roth GJ (1993). "Human platelet glycoprotein V: characterization of the polypeptide and the related Ib-V-IX receptor system of adhesive, leucine-rich glycoproteins". Proc. Natl. Acad. Sci. U.S.A. 90 (18): 8327–31. Bibcode:1993PNAS...90.8327H. doi:10.1073/pnas.90.18.8327. PMC 47349. PMID 7690959.
Meyer SC, Fox JE (1995). "Interaction of platelet glycoprotein V with glycoprotein Ib-IX regulates expression of the glycoproteins and binding of von Willebrand factor to glycoprotein Ib-IX in transfected cells". J. Biol. Chem. 270 (24): 14693–9. doi:10.1074/jbc.270.24.14693. PMID 7782333.
Takafuta T, Fujimura K, Kawano H, et al. (1995). "Expression of platelet membrane glycoprotein V in human megakaryocytes and megakaryocytic cell lines: a study using a novel monoclonal antibody against GPV". Thromb. Haemost. 72 (5): 762–9. PMID 7900083.
Lanza F, Morales M, de La Salle C, et al. (1993). "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". J. Biol. Chem. 268 (28): 20801–7. doi:10.1016/S0021-9258(19)36855-3. PMID 8407908.
Yagi M, Edelhoff S, Disteche CM, Roth GJ (1996). "Human platelet glycoproteins V and IX: mapping of two leucine-rich glycoprotein genes to chromosome 3 and analysis of structures". Biochemistry. 34 (49): 16132–7. doi:10.1021/bi00049a028. PMID 8519770.
Berger G, Massé JM, Cramer EM (1996). "Alpha-granule membrane mirrors the platelet plasma membrane and contains the glycoproteins Ib, IX, and V." Blood. 87 (4): 1385–95. doi:10.1182/blood.V87.4.1385.bloodjournal8741385. PMID 8608228.
Ravanat C, Morales M, Azorsa DO, et al. (1997). "Gene cloning of rat and mouse platelet glycoprotein V: identification of megakaryocyte-specific promoters and demonstration of functional thrombin cleavage". Blood. 89 (9): 3253–62. doi:10.1182/blood.V89.9.3253. PMID 9129030.
Bradford HN, Dela Cadena RA, Kunapuli SP, et al. (1997). "Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex". Blood. 90 (4): 1508–15. doi:10.1182/blood.V90.4.1508. PMID 9269768.
Wu G, Essex DW, Meloni FJ, et al. (1997). "Human endothelial cells in culture and in vivo express on their surface all four components of the glycoprotein Ib/IX/V complex". Blood. 90 (7): 2660–9. doi:10.1182/blood.V90.7.2660. PMID 9326233.
Andrews RK, Harris SJ, McNally T, Berndt MC (1998). "Binding of purified 14-3-3 zeta signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex". Biochemistry. 37 (2): 638–47. doi:10.1021/bi970893g. PMID 9425086.
Longhurst CM, White MM, Wilkinson DA, Jennings LK (1999). "A CD9, alphaIIbbeta3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by alphaIIbbeta3 conformational states". Eur. J. Biochem. 263 (1): 104–11. doi:10.1046/j.1432-1327.1999.00467.x. PMID 10429193.
Dicker IB, Pedicord DL, Seiffert DA, et al. (2002). "Both the high affinity thrombin receptor (GPIb-IX-V) and GPIIb/IIIa are implicated in expression of thrombin-induced platelet procoagulant activity". Thromb. Haemost. 86 (4): 1065–9. PMID 11686325.
Rabie T, Strehl A, Ludwig A, Nieswandt B (2005). "Evidence for a role of ADAM17 (TACE) in the regulation of platelet glycoprotein V." J. Biol. Chem. 280 (15): 14462–8. doi:10.1074/jbc.M500041200. PMID 15691827.
Aktas B, Pozgajova M, Bergmeier W, et al. (2006). "Aspirin induces platelet receptor shedding via ADAM17 (TACE)". J. Biol. Chem. 280 (48): 39716–22. doi:10.1074/jbc.M507762200. PMID 16179345.
Lewandrowski U, Moebius J, Walter U, Sickmann A (2006). "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach" (PDF). Mol. Cell. Proteomics. 5 (2): 226–33. doi:10.1074/mcp.M500324-MCP200. PMID 16263699. S2CID 7856143.

External links

GP5+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000178732 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000047953 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: GP5 glycoprotein V (platelet)".

Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

GP5 (gene)

See also

References

Further reading

External links