[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 216-237.
DOI=10.1074/jbc.272.39.24588; PubMed=9305925 [NCBI, ExPASy, EBI, Israel, Japan]
Rosendahl M.S.,
Ko S.C.,
Long D.L.,
Brewer M.T.,
Rosenzweig B.,
Hedl E.,
Anderson L.,
Pyle S.M.,
Moreland J.,
Meyers M.A.,
Kohno T.,
Lyons D.,
Lichenstein H.S.;
"Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases.";
J. Biol. Chem. 272:24588-24593(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] OF 109-748.
PubMed=8694785 [NCBI, ExPASy, EBI, Israel, Japan]
Howard L.,
Mitchell S.,
Lu X.,
Griffiths S.,
Glynn P.;
"Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types.";
Biochem. J. 317:45-50(1996).
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[3]
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TISSUE SPECIFICITY.
DOI=10.1006/bbrc.1996.5957; PubMed=9016778 [NCBI, ExPASy, EBI, Israel, Japan]
McKie N.,
Edwards T.,
Dallas D.J.,
Houghton A.,
Stringer B.,
Graham R.,
Russell G.,
Croucher P.I.;
"Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes.";
Biochem. Biophys. Res. Commun. 230:335-339(1997).
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[4]
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FUNCTION.
DOI=10.1096/fj.02-0430fje; PubMed=12475894 [NCBI, ExPASy, EBI, Israel, Japan]
Gutwein P.,
Mechtersheimer S.,
Riedle S.,
Stoeck A.,
Gast D.,
Joumaa S.,
Zentgraf H.,
Fogel M.,
Altevogt P.;
"ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles.";
FASEB J. 17:292-294(2003).
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[5]
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FUNCTION.
DOI=10.1074/jbc.M105677200; PubMed=11477090 [NCBI, ExPASy, EBI, Israel, Japan]
Vincent B.,
Paitel E.,
Saftig P.,
Frobert Y.,
Hartmann D.,
De Strooper B.,
Grassi J.,
Lopez-Perez E.,
Checler F.;
"The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein.";
J. Biol. Chem. 276:37743-37746(2001).
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[6]
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TISSUE SPECIFICITY.
PubMed=11511685 [NCBI, ExPASy, EBI, Israel, Japan]
Chubinskaya S.,
Mikhail R.,
Deutsch A.,
Tindal M.H.;
"ADAM-10 protein is present in human articular cartilage primarily in the membrane-bound form and is upregulated in osteoarthritis and in response to IL-1alpha in bovine nasal cartilage.";
J. Histochem. Cytochem. 49:1165-1176(2001).
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[7]
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FUNCTION.
DOI=10.1038/nm0102-41; PubMed=11786905 [NCBI, ExPASy, EBI, Israel, Japan]
Lemjabbar H.,
Basbaum C.;
"Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells.";
Nat. Med. 8:41-46(2002).
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[8]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan]
Lewandrowski U.,
Moebius J.,
Walter U.,
Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
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[9]
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GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R.,
Jiang X.,
Sun D.,
Han G.,
Wang F.,
Ye M.,
Wang L.,
Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
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- FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. Controls also the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity).
- CATALYTIC ACTIVITY: Endopeptidase of broad specificity.
- COFACTOR: Binds 1 zinc ion (By similarity).
- SUBUNIT: Interacts with ephrin-A2 (By similarity).
- INTERACTION:
P10275:AR; NbExp=1; IntAct=EBI-1536151, EBI-608057;
- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. Note=Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived likely from the Golgi.
- TISSUE SPECIFICITY: Expressed in spleen, lymph node, thymus, peripheral blood leukocyte, bone marrow, cartilage, chondrocytes and fetal liver.
- INDUCTION: In osteoarthritis affected-cartilage.
- DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
- PTM: The precursor is cleaved by a furin endopeptidase (By similarity).
- SIMILARITY: Contains 1 disintegrin domain.
- SIMILARITY: Contains 1 peptidase M12B domain [view classification].
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