Caspase 7

CASP7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1F1J, 1GQF, 1I4O, 1I51, 1K86, 1K88, 1KMC, 1SHJ, 1SHL, 2QL5, 2QL7, 2QL9, 2QLB, 2QLF, 2QLJ, 3EDR, 3H1P, 3IBC, 3IBF, 3R5K, 4FDL, 4FEA, 4HQ0, 4HQR, 4JB8, 4JJ8, 4JR1, 4JR2, 4LSZ, 4ZVR, 4ZVQ, 4ZVO, 4ZVU, 4ZVT, 4ZVS, 4ZVP, 5IC6
Identifiers
Aliases	CASP7, CASP-7, CMH-1, ICE-LAP3, LICE2, MCH3, Caspase 7
External IDs	MGI: 109383 HomoloGene: 11168 GeneCards: CASP7
Genetically Related Diseases
Vitiligo[1]
Gene ontology Molecular function • cysteine-type endopeptidase activity involved in execution phase of apoptosis • peptidase activity • cysteine-type peptidase activity • cysteine-type endopeptidase activity • protein binding • hydrolase activity Cellular component • cytoplasm • cytosol • nucleus • nucleoplasm Biological process • execution phase of apoptosis • cellular component disassembly involved in execution phase of apoptosis • activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c • apoptotic process • proteolysis Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	840	12369
Ensembl	ENSG00000165806	ENSMUSG00000025076
UniProt	P55210	P97864
RefSeq (mRNA)	NM_001227 NM_001267056 NM_001267057 NM_001267058 NM_033338 NM_033339 NM_033340 NM_001320911	NM_007611
RefSeq (protein)	NP_001218.1 NP_001253985.1 NP_001253986.1 NP_001253987.1 NP_203124.1 NP_203125.1 NP_203126.1 NP_001307840.1	NP_031637.1
Location (UCSC)	Chr 10: 113.68 – 113.73 Mb	Chr 19: 56.4 – 56.44 Mb
PubMed search	[2]	[3]
Wikidata

View/Edit Human

View/Edit Mouse

Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7 gene. CASP7 orthologs ^[4] have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.

Function

Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms.^[5]

Interactions

Caspase 7 has been shown to interact with:

• Caspase 8,^[6][7]
• Survivin^[8][9] and
• XIAP.^{[10][11][12][13]}

See also

• The Proteolysis Map
• Caspase

References

1. "Diseases that are genetically associated with CASP7 view/edit references on wikidata".
2. "Human PubMed Reference:".
3. "Mouse PubMed Reference:".
4. "OrthoMaM phylogenetic marker: CASP7 coding sequence".
5. "Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase".
6. Guo Y, Srinivasula SM, Druilhe A, Fernandes-Alnemri T, Alnemri ES (Apr 2002). "Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria". J. Biol. Chem. 277 (16): 13430–7. doi:10.1074/jbc.M108029200. PMID 11832478.
7. Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri ES (Dec 1996). "Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases". Proc. Natl. Acad. Sci. U.S.A. 93 (25): 14486–91. doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078.
8. Tamm I, Wang Y, Sausville E, Scudiero DA, Vigna N, Oltersdorf T, Reed JC (Dec 1998). "IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs". Cancer Res. 58 (23): 5315–20. PMID 9850056.
9. Shin S, Sung BJ, Cho YS, Kim HJ, Ha NC, Hwang JI, Chung CW, Jung YK, Oh BH (Jan 2001). "An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7". Biochemistry. 40 (4): 1117–23. doi:10.1021/bi001603q. PMID 11170436.
10. Riedl SJ, Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik SW, Liddington RC, Salvesen GS (Mar 2001). "Structural basis for the inhibition of caspase-3 by XIAP". Cell. 104 (5): 791–800. doi:10.1016/S0092-8674(01)00274-4. PMID 11257232.
11. Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC (Dec 1997). "The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases". EMBO J. 16 (23): 6914–25. doi:10.1093/emboj/16.23.6914. PMC 1170295. PMID 9384571.
12. Deveraux QL, Takahashi R, Salvesen GS, Reed JC (Jul 1997). "X-linked IAP is a direct inhibitor of cell-death proteases". Nature. 388 (6639): 300–4. doi:10.1038/40901. PMID 9230442.
13. Suzuki Y, Nakabayashi Y, Nakata K, Reed JC, Takahashi R (Jul 2001). "X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes". J. Biol. Chem. 276 (29): 27058–63. doi:10.1074/jbc.M102415200. PMID 11359776.

Further reading

• Cohen GM (1997). "Caspases: the executioners of apoptosis". Biochem. J. 326 (Pt 1): 1–16. doi:10.1042/bj3260001. PMC 1218630. PMID 9337844.

External links

• The MEROPS online database for peptidases and their inhibitors: C14.004