ADAM15

ADAM metallopeptidase domain 15 (metargidin), also known as ADAM15, is a human gene.

PBB_Summary
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summary_text = 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.cite web | title = Entrez Gene: ADAM15 ADAM metallopeptidase domain 15 (metargidin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8751| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Primakoff P, Myles DG |title=The ADAM gene family: surface proteins with adhesion and protease activity. |journal=Trends Genet. |volume=16 |issue= 2 |pages= 83–7 |year= 2000 |pmid= 10652535 |doi=
*cite journal | author=Takagi J |title= [First atomic view of alpha V beta 3 integrin extracellular domain] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 2 |pages= 153–9 |year= 2002 |pmid= 11840679 |doi=
*cite journal | author=Krätzschmar J, Lum L, Blobel CP |title=Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. |journal=J. Biol. Chem. |volume=271 |issue= 9 |pages= 4593–6 |year= 1996 |pmid= 8617717 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=McKie N, Edwards T, Dallas DJ, "et al." |title=Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. |journal=Biochem. Biophys. Res. Commun. |volume=230 |issue= 2 |pages= 335–9 |year= 1997 |pmid= 9016778 |doi= 10.1006/bbrc.1996.5957
*cite journal | author=Herren B, Raines EW, Ross R |title=Expression of a disintegrin-like protein in cultured human vascular cells and "in vivo". |journal=FASEB J. |volume=11 |issue= 2 |pages= 173–80 |year= 1997 |pmid= 9039960 |doi=
*cite journal | author=Zhang XP, Kamata T, Yokoyama K, "et al." |title=Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3. |journal=J. Biol. Chem. |volume=273 |issue= 13 |pages= 7345–50 |year= 1998 |pmid= 9516430 |doi=
*cite journal | author=Nath D, Slocombe PM, Stephens PE, "et al." |title=Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1 integrins on different haemopoietic cells. |journal=J. Cell. Sci. |volume=112 ( Pt 4) |issue= |pages= 579–87 |year= 1999 |pmid= 9914169 |doi=
*cite journal | author=Howard L, Nelson KK, Maciewicz RA, Blobel CP |title=Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. |journal=J. Biol. Chem. |volume=274 |issue= 44 |pages= 31693–9 |year= 1999 |pmid= 10531379 |doi=
*cite journal | author=Kärkkäinen I, Karhu R, Huovila AP |title=Assignment of the ADAM15 gene to human chromosome band 1q21.3 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=88 |issue= 3-4 |pages= 206–7 |year= 2000 |pmid= 10828588 |doi=
*cite journal | author=Seldin MF, Hirohata S, Apte SS |title=Chromosomal mapping of Adam9, Adam15 and Adam21. |journal=Matrix Biol. |volume=19 |issue= 2 |pages= 185–7 |year= 2000 |pmid= 10842103 |doi=
*cite journal | author=Poghosyan Z, Robbins SM, Houslay MD, "et al." |title=Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4999–5007 |year= 2002 |pmid= 11741929 |doi= 10.1074/jbc. M107430200
*cite journal | author=Arndt M, Lendeckel U, Röcken C, "et al." |title=Altered expression of ADAMs (A Disintegrin And Metalloproteinase) in fibrillating human atria. |journal=Circulation |volume=105 |issue= 6 |pages= 720–5 |year= 2002 |pmid= 11839628 |doi=
*cite journal | author=Eto K, Huet C, Tarui T, "et al." |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 20 |pages= 17804–10 |year= 2002 |pmid= 11882657 |doi= 10.1074/jbc. M200086200
*cite journal | author=Martin J, Eynstone LV, Davies M, "et al." |title=The role of ADAM 15 in glomerular mesangial cell migration. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 33683–9 |year= 2002 |pmid= 12091380 |doi= 10.1074/jbc. M200988200
*cite journal | author=Ham C, Levkau B, Raines EW, Herren B |title=ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin. |journal=Exp. Cell Res. |volume=279 |issue= 2 |pages= 239–47 |year= 2002 |pmid= 12243749 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Abram CL, Seals DF, Pass I, "et al." |title=The adaptor protein fish associates with members of the ADAMs family and localizes to podosomes of Src-transformed cells. |journal=J. Biol. Chem. |volume=278 |issue= 19 |pages= 16844–51 |year= 2003 |pmid= 12615925 |doi= 10.1074/jbc. M300267200

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