[1]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
DOI=10.1074/jbc.271.3.1621; PubMed=8576161 [NCBI, ExPASy, EBI, Israel, Japan]
Duan H.,
Chinnaiyan A.M.,
Hudson P.L.,
Wing J.P.,
He W.-W.,
Dixit V.M.;
"ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis.";
J. Biol. Chem. 271:1621-1625(1996).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Spleen;
DOI=10.1074/jbc.271.4.1825; PubMed=8567622 [NCBI, ExPASy, EBI, Israel, Japan]
Lippke J.A.,
Gu Y.,
Sarnecki C.,
Caron P.R.,
Su M.S.-S.;
"Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32.";
J. Biol. Chem. 271:1825-1828(1996).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=T-cell;
PubMed=8521391 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandes-Alnemri T.,
Takahashi A.,
Armstrong R.C.,
Krebs J.,
Fritz L.C.,
Tomaselli K.J.,
Wang L.,
Yu Z.,
Croce C.M.,
Salveson G.,
Earnshaw W.C.,
Litwack G.,
Alnemri E.S.;
"Mch3, a novel human apoptotic cysteine protease highly related to CPP32.";
Cancer Res. 55:6045-6052(1995).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA').
TISSUE=Fetal lung, and Fetal spleen;
DOI=10.1006/geno.1996.4548; PubMed=9070923 [NCBI, ExPASy, EBI, Israel, Japan]
Juan T.S.-C.,
McNiece I.K.,
Argento J.M.,
Jenkins N.A.,
Gilbert D.J.,
Copeland N.G.,
Fletcher F.A.;
"Identification and mapping of Casp7, a cysteine protease resembling CPP32 beta, interleukin-1 beta converting enzyme, and CED-3.";
Genomics 40:86-93(1997).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[6]
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PROTEOLYTIC PROCESSING.
DOI=10.1073/pnas.93.15.7464; PubMed=8755496 [NCBI, ExPASy, EBI, Israel, Japan]
Fernandes-Alnemri T.,
Armstrong R.C.,
Krebs J.F.,
Srinivasula S.M.,
Wang L.,
Bullrich F.,
Fritz L.C.,
Trapani J.A.,
Tomaselli K.J.,
Litwack G.,
Alnemri E.S.;
"In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains.";
Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996).
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[7]
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X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, AND SUBUNIT.
DOI=10.1016/S0092-8674(01)00544-X; PubMed=11701129 [NCBI, ExPASy, EBI, Israel, Japan]
Chai J.,
Wu Q.,
Shiozaki E.,
Srinivasula S.M.,
Alnemri E.S.,
Shi Y.;
"Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding.";
Cell 107:399-407(2001).
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- FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.
- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
- ENZYME REGULATION: Inhibited by isatin sulfonamides.
- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit.
- INTERACTION:
Q13490:BIRC2; NbExp=2; IntAct=EBI-523958, EBI-514538;
- SUBCELLULAR LOCATION: Cytoplasm.
- ALTERNATIVE PRODUCTS:
3 named isoforms [FASTA] produced by alternative splicing.
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| Name | Beta |
| Isoform ID | P55210-2 |
| Note: Not proteolytically active. |
| Features which should be applied to build the isoform sequence: VSP_000807. |
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| Name | Alpha' |
| Synonyms | Beta |
| Isoform ID | P55210-3 |
| Note: What we call isoform Alpha' is known in Ref.4 as Beta. |
| Features which should be applied to build the isoform sequence: VSP_000806. |
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- TISSUE SPECIFICITY: Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain.
- PTM: Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur.
- SIMILARITY: Belongs to the peptidase C14 family [view classification].
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