[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS LONG AND SHORT).
DOI=10.1006/cyto.1998.0466; PubMed=10433800 [NCBI, ExPASy, EBI, Israel, Japan]
Cerretti D.P.,
Poindexter K.,
Castner B.J.,
Means G.,
Copeland N.G.,
Gilbert D.J.,
Jenkins N.A.,
Black R.A.,
Nelson N.;
"Characterization of the cDNA and gene for mouse tumour necrosis factor alpha converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25.";
Cytokine 11:541-551(1999).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
DOI=10.1016/S0014-5793(98)01031-X; PubMed=9755855 [NCBI, ExPASy, EBI, Israel, Japan]
Amour A.,
Slocombe P.M.,
Webster A.,
Butler M.,
Knight C.G.,
Smith B.J.,
Stephens P.E.,
Shelley C.,
Hutton M.,
Knauper V.,
Docherty A.J.,
Murphy G.;
"TNF-alpha converting enzyme (TACE) is inhibited by TIMP-3.";
FEBS Lett. 435:39-44(1998).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
DOI=10.1016/S0378-1119(99)00155-9; PubMed=10375622 [NCBI, ExPASy, EBI, Israel, Japan]
Mizui Y.,
Yamazaki K.,
Sagane K.,
Tanaka I.;
"cDNA cloning of mouse tumor necrosis factor-alpha converting enzyme (TACE) and partial analysis of its promoter.";
Gene 233:67-74(1999).
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[4]
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FUNCTION IN PROCESSING OF GROWTH HORMONE RECEPTOR.
DOI=10.1210/en.141.12.4342; PubMed=11108241 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y.,
Jiang J.,
Black R.A.,
Baumann G.,
Frank S.J.;
"Tumor necrosis factor-alpha converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation.";
Endocrinology 141:4342-4348(2000).
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[5]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Cerretti D.P.;
"Isolation of murine TNF-alpha converting enzyme.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
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[6]
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CHARACTERIZATION.
DOI=10.1074/jbc.275.19.14608; PubMed=10799547 [NCBI, ExPASy, EBI, Israel, Japan]
Reddy P.,
Slack J.L.,
Davis R.,
Cerretti D.P.,
Kozlosky C.J.,
Blanton R.A.,
Shows D.,
Peschon J.J.,
Black R.A.;
"Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme.";
J. Biol. Chem. 275:14608-14614(2000).
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[7]
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CHARACTERIZATION.
DOI=10.1016/S1097-2765(00)80417-7; PubMed=10882063 [NCBI, ExPASy, EBI, Israel, Japan]
Brou C.,
Logeat F.,
Gupta N.,
Bessia C.,
LeBail O.,
Doedens J.R.,
Cumano A.,
Roux P.,
Black R.A.,
Israel A.;
"A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE.";
Mol. Cell 5:207-216(2000).
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- FUNCTION: Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form. Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein. Also involved in the activation of Notch pathway (By similarity).
- CATALYTIC ACTIVITY: Narrow endopeptidase specificity. Cleaves Pro-Leu-Ala-Gln-Ala-|-Val-Arg-Ser-Ser-Ser in the membrane-bound, 26-kDa form of tumor necrosis factor alpha (TNF-alpha). Similarly cleaves other membrane-anchored, cell-surface proteins to 'shed' the extracellular domains.
- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
- ENZYME REGULATION: Inhibited by metalloproteinase inhibitor 3 (TIMP-3), but not by TIMP-1, TIMP-2 and TIMP-4.
- SUBUNIT: Interacts with MAD2L1 and MUC1 (By similarity).
- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass type I membrane protein.
- SUBCELLULAR LOCATION: Isoform Short: Secreted.
- ALTERNATIVE PRODUCTS:
2 named isoforms [FASTA] produced by alternative splicing.
- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at highest levels in heart, liver, skeletal muscle, kidney and testes. Expressed at lower levels in brain, spleen and lung.
- DOMAIN: Must be membrane anchored to cleave the different substrates. The cytoplasmic domain is not required for the this activity. Only the catalytic domain is essential to shed TNF and p75 TNFR.
- 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).
- PTM: Phosphorylated. Stimulation by growth factor or phorbol 12-myristate 13-acetate induces phosphorylation of Ser-822 but decreases phosphorylation of Ser-794 (By similarity).
- SIMILARITY: Contains 1 disintegrin domain.
- SIMILARITY: Contains 1 peptidase M12B domain [view classification].
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