Каспаза 7

CASP7
Доступные структуры
PDB	Поиск ортолога: PDBE RCSB
showСписок кодов идентификаторов PDB
	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
Идентификаторы
Псевдонимы	CASP7 , CASP-7, CMH-1, ICE-LAP3, Lice2, MCH3, каспаза 7
Внешние идентификаторы	OMIM: 601761; MGI: 109383; HomoloGene: 11168; GeneCards: CASP7; OMA:CASP7 - orthologs
showGene location (Human)
Chr.	Chromosome 10 (human)
End	113,730,907 bp
showGene location (Mouse)
Chr.	Chromosome 19 (mouse)
End	56,430,776 bp
showRNA expression pattern
	Top expressed in
	rectum; ; palpebral conjunctiva; ; epithelium of nasopharynx; ; jejunal mucosa; ; mucosa of transverse colon; ; duodenum; ; parotid gland; ; nasal epithelium; ; mucosa of sigmoid colon; ; mucosa of paranasal sinus;
	Top expressed in
	intestinal villus; ; Ileal epithelium; ; jejunum; ; lens; ; left colon; ; duodenum; ; submandibular gland; ; pineal gland; ; conjunctival fornix; ; choroidal fissure;
	More reference expression data
	More reference expression data
showGene ontology
Molecular function	cysteine-type peptidase activity; cysteine-type endopeptidase activity; protein binding; hydrolase activity; peptidase activity; cysteine-type endopeptidase activity involved in execution phase of apoptosis; cysteine-type endopeptidase activity involved in apoptotic process;
Cellular component	cytoplasm; cytosol; nucleus; nucleoplasm;
Biological process	proteolysis; cellular response to staurosporine; execution phase of apoptosis; apoptotic process;
	Sources:Amigo / QuickGO
hideOrthologs
	840
	12369
	ENSG00000165806
	ENSMUSG00000025076
	P55210
	P97864
showNM_001227; NM_001267056; NM_001267057; NM_001267058; NM_033338;
	NM_033339; NM_033340; NM_001320911
	NM_007611
showNP_001218; NP_001253985; NP_001253986; NP_001253987; NP_001307840;
	NP_203124; NP_203125; NP_203126
	NP_031637
	Wikidata
View/Edit Human	View/Edit Mouse

Каспаза-7, связанная с апоптозом цистеин-пептидазу , также известную как CASP7 , является белком человека, кодируемым CASP7 геном . CASP7 Ортологи ^{[ 5 ]} были идентифицированы почти у всех млекопитающих , для которых доступны полные данные генома. Уникальные ортологи также присутствуют у птиц , ящериц , лиссамбийцев и телеостов .

Функция

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.^[6]

Interactions

Caspase 7 has been shown to interact with:

References

^ Jump up to: ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000165806 – Ensembl, May 2017
^ Jump up to: ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025076 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "OrthoMaM phylogenetic marker: CASP7 coding sequence". Archived from the original on 2016-03-04. Retrieved 2009-12-20.
^ "Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase".
^ 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.
^ 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. Bibcode:1996PNAS...9314486S. doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078.
^ 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.
^ 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.
^ 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. S2CID 17915093.
^ 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.
^ 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. Bibcode:1997Natur.388..300D. doi:10.1038/40901. PMID 9230442. S2CID 4395885.
^ 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.

External links

The MEROPS online database for peptidases and their inhibitors: C14.004^{[permanent dead link]}
Overview of all the structural information available in the PDB for UniProt: P55210 (Human Caspase-7) at the PDBe-KB.

This article on a gene on human chromosome 10 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] Jump up to: ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000165806 – Ensembl, May 2017

[refGRCm38Ensembl-2] Jump up to: ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000025076 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[OrthoMaM-5] "OrthoMaM phylogenetic marker: CASP7 coding sequence". Archived from the original on 2016-03-04. Retrieved 2009-12-20.

[6] "Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase".

[pmid11832478-7] 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.

[pmid8962078-8] 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. Bibcode:1996PNAS...9314486S. doi:10.1073/pnas.93.25.14486. PMC 26159. PMID 8962078.

[pmid9850056-9] 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.

[pmid11170436-10] 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.

[pmid11257232-11] 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. S2CID 17915093.

[pmid9384571-12] 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.

[pmid9230442-13] 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. Bibcode:1997Natur.388..300D. doi:10.1038/40901. PMID 9230442. S2CID 4395885.

[pmid11359776-14] 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.

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v t e Proteases: cysteine proteases (EC 3.4.22)
Caspase	Caspase 1 Caspase 2 Caspase 3 Caspase 4 Caspase 5 Caspase 6 Caspase 7 Caspase 8 Caspase 9 Caspase 10 Caspase 12 Caspase 13 Caspase 14
Fruit-derived	Papain Ficain Bromelain Actinidain
Calpain	CAPN1 CAPN2 CAPN3 CAPN5 CAPN6 CAPN7 CAPN8 CAPN9 CAPN10 CAPN11 CAPN12 CAPN13 CAPN14 CAPNS1 CAPNS2
Cathepsin	B C F H K L1/L2 O S W Z
Other	Clostripain Cancer procoagulant Separase Autophagin Cruzipain 3C-like protease Gingipain R Gingipain K

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Каспаза 7

Функция

Interactions

See also

References

Further reading

External links