ADAM15 Information & ADAM15 Links at HealthHaven.com

ADAM metallopeptidase domain 15 (metargidin)
Identifiers
Symbols	ADAM15; MDC15
External IDs	OMIM: 605548 MGI: 1333882 HomoloGene: 2829 GeneCards: ADAM15 Gene
Gene ontology
Molecular function	• metalloendopeptidase activity; • protein binding; • zinc ion binding; • SH3 domain binding; • metal ion binding;
Cellular component	• membrane; • integral to membrane;
Biological process	• proteolysis; • cell adhesion; • cell-matrix adhesion;
RNA expression pattern
	More reference expression data
Orthologs

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Disintegrin and metalloproteinase domain-containing protein 15 is an enzyme that in humans is encoded by the ADAM15 gene.^[1]

The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as an EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed.^[2]

[edit] Interactions

ADAM15 has been shown to interact with Grb2,^[3] HCK,^[3] SNX9,^[4] Lck^[3] and SH3GL2.^[4]

[edit] References

^ Zhang XP, Kamata T, Yokoyama K, Puzon-McLaughlin W, Takada Y (Apr 1998). "Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3". J Biol Chem 273 (13): 7345–50. PMID 9516430.
^ "Entrez Gene: ADAM15 ADAM metallopeptidase domain 15 (metargidin)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8751.
^ ^a ^b ^c Poghosyan, Zaruhi; Robbins Stephen M, Houslay Miles D, Webster Ailsa, Murphy Gillian, Edwards Dylan R (Feb. 2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases". J. Biol. Chem. (United States) 277 (7): 4999–5007. doi:10.1074/jbc.M107430200. ISSN 0021-9258. PMID 11741929.
^ ^a ^b Howard, L; Nelson K K, Maciewicz R A, Blobel C P (Oct. 1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". J. Biol. Chem. (UNITED STATES) 274 (44): 31693–9. ISSN 0021-9258. PMID 10531379.

[edit] Further reading

Primakoff P, Myles DG (2000). "The ADAM gene family: surface proteins with adhesion and protease activity.". Trends Genet. 16 (2): 83–7. PMID 10652535.
Takagi J (2002). "[First atomic view of alpha V beta 3 integrin extracellular domain]". Tanpakushitsu Kakusan Koso 47 (2): 153–9. PMID 11840679.
Krätzschmar J, Lum L, Blobel CP (1996). "Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence.". J. Biol. Chem. 271 (9): 4593–6. PMID 8617717.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
McKie N, Edwards T, Dallas DJ, et al. (1997). "Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes.". Biochem. Biophys. Res. Commun. 230 (2): 335–9. doi:10.1006/bbrc.1996.5957. PMID 9016778.
Herren B, Raines EW, Ross R (1997). "Expression of a disintegrin-like protein in cultured human vascular cells and in vivo.". Faseb J. 11 (2): 173–80. PMID 9039960.
Nath D, Slocombe PM, Stephens PE, et al. (1999). "Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells.". J. Cell. Sci. 112 ( Pt 4): 579–87. PMID 9914169.
Howard L, Nelson KK, Maciewicz RA, Blobel CP (1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1.". J. Biol. Chem. 274 (44): 31693–9. PMID 10531379.
Kärkkäinen I, Karhu R, Huovila AP (2000). "Assignment of the ADAM15 gene to human chromosome band 1q21.3 by in situ hybridization.". Cytogenet. Cell Genet. 88 (3-4): 206–7. PMID 10828588.
Seldin MF, Hirohata S, Apte SS (2000). "Chromosomal mapping of Adam9, Adam15 and Adam21.". Matrix Biol. 19 (2): 185–7. PMID 10842103.
Poghosyan Z, Robbins SM, Houslay MD, et al. (2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases.". J. Biol. Chem. 277 (7): 4999–5007. doi:10.1074/jbc.. PMID 11741929.
Arndt M, Lendeckel U, Röcken C, et al. (2002). "Altered expression of ADAMs (A Disintegrin And Metalloproteinase) in fibrillating human atria.". Circulation 105 (6): 720–5. PMID 11839628.
Eto K, Huet C, Tarui T, et al. (2002). "Functional classification of ADAMs based on a conserved motif for binding to integrin alpha 9beta 1: implications for sperm-egg binding and other cell interactions.". J. Biol. Chem. 277 (20): 17804–10. doi:10.1074/jbc.. PMID 11882657.
Martin J, Eynstone LV, Davies M, et al. (2002). "The role of ADAM 15 in glomerular mesangial cell migration.". J. Biol. Chem. 277 (37): 33683–9. doi:10.1074/jbc.. PMID 12091380.
Ham C, Levkau B, Raines EW, Herren B (2002). "ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin.". Exp. Cell Res. 279 (2): 239–47. PMID 12243749.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Abram CL, Seals DF, Pass I, et al. (2003). "The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells.". J. Biol. Chem. 278 (19): 16844–51. doi:10.1074/jbc.. PMID 12615925.

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[pmid9516430-0] Zhang XP, Kamata T, Yokoyama K, Puzon-McLaughlin W, Takada Y (Apr 1998). "Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3". J Biol Chem 273 (13): 7345–50. PMID 9516430.

[entrez-1] "Entrez Gene: ADAM15 ADAM metallopeptidase domain 15 (metargidin)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8751.

[pmid11741929-2] Poghosyan, Zaruhi; Robbins Stephen M, Houslay Miles D, Webster Ailsa, Murphy Gillian, Edwards Dylan R (Feb. 2002). "Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases". J. Biol. Chem. (United States) 277 (7): 4999–5007. doi:10.1074/jbc.M107430200. ISSN 0021-9258. PMID 11741929.

[pmid10531379-3] Howard, L; Nelson K K, Maciewicz R A, Blobel C P (Oct. 1999). "Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1". J. Biol. Chem. (UNITED STATES) 274 (44): 31693–9. ISSN 0021-9258. PMID 10531379.

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