Caspase 7: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Caspase-7, apoptosis-related cysteine peptidase''', also known as '''CASP7''', is a human protein encoded by the ''CASP7'' [[gene]].
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''CASP7'' [[orthologs]] <ref name="OrthoMaM">{{cite web | title = OrthoMaM phylogenetic marker: CASP7 coding sequence | url = http://www.orthomam.univ-montp2.fr/orthomam/data/cds/detailMarkers/ENSG00000165806_CASP7.xml }}</ref> have been identified in nearly all [[mammals]] for which complete genome data are available. Unique orthologs are also present in [[birds]], [[lizards]], [[lissamphibian]]s, and [[teleosts]].
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_CASP7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f1j.
| Name = Caspase 7, apoptosis-related cysteine peptidase
| HGNCid = 1508
| Symbol = CASP7
| AltSymbols =; CMH-1; ICE-LAP3; MCH3
| OMIM = 601761
| ECnumber = 
| Homologene = 11168
| MGIid = 109383
| GeneAtlas_image1 = PBB_GE_CASP7_207181_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}} {{GNF_GO|id=GO:0030693 |text = caspase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005789 |text = endoplasmic reticulum membrane}} {{GNF_GO|id=GO:0031966 |text = mitochondrial membrane}}
| Process = {{GNF_GO|id=GO:0001836 |text = release of cytochrome c from mitochondria}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008632 |text = apoptotic program}} {{GNF_GO|id=GO:0009411 |text = response to UV}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 840
    | Hs_Ensembl = ENSG00000165806
    | Hs_RefseqProtein = NP_001218
    | Hs_RefseqmRNA = NM_001227
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 115428953
    | Hs_GenLoc_end = 115480652
    | Hs_Uniprot = P55210
    | Mm_EntrezGene = 12369
    | Mm_Ensembl = ENSMUSG00000025076
    | Mm_RefseqmRNA = NM_007611
    | Mm_RefseqProtein = NP_031637
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 56457666
    | Mm_GenLoc_end = 56494345
    | Mm_Uniprot = Q4FJQ4
  }}
}}


Caspase-7 is a member of the [[caspase]] ('''c'''ysteine '''asp'''artate prote'''ase''') 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 [[proenzyme]]s 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 [[CASP3|caspase 3]], [[CASP10|caspase 10]], and [[CASP9|caspase 9]]. It is activated upon cell death stimuli and induces apoptosis. [[Alternative splicing]] results in four transcript variants, encoding three distinct [[isoform]]s.<ref>{{cite web | title = Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=840| accessdate = }}</ref>


==Overview==
== Interactions ==
'''Caspase 7, apoptosis-related cysteine peptidase''', also known as '''CASP7''', is a human protein and [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
Caspase 7 has been shown to [[Protein-protein interaction|interact]] with:
{{PBB_Summary
* [[Caspase 8]],<ref name = pmid11832478>{{cite journal | vauthors = Guo Y, Srinivasula SM, Druilhe A, Fernandes-Alnemri T, Alnemri ES | title = Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria | journal = J. Biol. Chem. | volume = 277 | issue = 16 | pages = 13430–7 | date = Apr 2002 | pmid = 11832478 | doi = 10.1074/jbc.M108029200 }}</ref><ref name = pmid8962078>{{cite journal | vauthors = Srinivasula SM, Ahmad M, Fernandes-Alnemri T, Litwack G, Alnemri ES | title = 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 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 93 | issue = 25 | pages = 14486–91 | date = Dec 1996 | pmid = 8962078 | pmc = 26159 | doi =  10.1073/pnas.93.25.14486}}</ref>
| section_title =  
* [[Survivin]]<ref name = pmid9850056>{{cite journal | vauthors = Tamm I, Wang Y, Sausville E, Scudiero DA, Vigna N, Oltersdorf T, Reed JC | title = IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs | journal = Cancer Res. | volume = 58 | issue = 23 | pages = 5315–20 | date = Dec 1998 | pmid = 9850056 | doi =  }}</ref><ref name = pmid11170436>{{cite journal | vauthors = Shin S, Sung BJ, Cho YS, Kim HJ, Ha NC, Hwang JI, Chung CW, Jung YK, Oh BH | title = An anti-apoptotic protein human survivin is a direct inhibitor of caspase-3 and -7 | journal = Biochemistry | volume = 40 | issue = 4 | pages = 1117–23 | date = Jan 2001 | pmid = 11170436 | doi =  10.1021/bi001603q}}</ref>  and
| summary_text = This gene encodes a protein which is a member of the cysteine-aspartic acid [[protease]] ([[caspase]]) family. Sequential activation of caspases plays a central role in the execution-phase of cell [[apoptosis]]. Caspases exist as inactive [[proenzyme]]s which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The precursor of this caspase is cleaved by [[CASP3|caspase 3]] and [[CASP10|caspase 10]]. It is activated upon cell death stimuli and induces apoptosis. [[Alternative splicing]] results in four transcript variants, encoding three distinct [[isoform]]s.<ref>{{cite web | title = Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=840| accessdate = }}</ref>
* [[XIAP]].<ref name = pmid11257232>{{cite journal | vauthors = Riedl SJ, Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik SW, Liddington RC, Salvesen GS | title = Structural basis for the inhibition of caspase-3 by XIAP | journal = Cell | volume = 104 | issue = 5 | pages = 791–800 | date = Mar 2001 | pmid = 11257232 | doi = 10.1016/S0092-8674(01)00274-4}}</ref><ref name = pmid9384571>{{cite journal | vauthors = Roy N, Deveraux QL, Takahashi R, Salvesen GS, Reed JC | title = The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases | journal = EMBO J. | volume = 16 | issue = 23 | pages = 6914–25 | date = Dec 1997 | pmid = 9384571 | pmc = 1170295 | doi = 10.1093/emboj/16.23.6914 }}</ref><ref name = pmid9230442>{{cite journal | vauthors = Deveraux QL, Takahashi R, Salvesen GS, Reed JC | title = X-linked IAP is a direct inhibitor of cell-death proteases | journal = Nature | volume = 388 | issue = 6639 | pages = 300–4 | date = Jul 1997 | pmid = 9230442 | doi = 10.1038/40901 }}</ref><ref name = pmid11359776>{{cite journal | vauthors = Suzuki Y, Nakabayashi Y, Nakata K, Reed JC, Takahashi R | title = X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes | journal = J. Biol. Chem. | volume = 276 | issue = 29 | pages = 27058–63 | date = Jul 2001 | pmid = 11359776 | doi = 10.1074/jbc.M102415200 }}</ref>
}}


==References==
== See also ==
* [[The Proteolysis Map]]
* [[Caspase]]
 
== References ==
{{reflist}}
{{reflist}}
==Further reading==
 
{{refbegin | 2}}
== Further reading ==
{{PBB_Further_reading
{{refbegin}}
| citations =
* {{cite journal | vauthors = Cohen GM | title = Caspases: the executioners of apoptosis | journal = Biochem. J. | volume = 326 | issue = Pt 1 | pages = 1–16 | year = 1997 | pmid = 9337844 | pmc = 1218630 | doi =  10.1042/bj3260001}}
*{{cite journal | author=Cohen GM |title=Caspases: the executioners of apoptosis. |journal=Biochem. J. |volume=326 ( Pt 1) |issue= |pages= 1–16 |year= 1997 |pmid= 9337844 |doi=  }}
}}
{{refend}}
{{refend}}


{{WH}}
== External links ==
{{WS}}
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=C14.004 C14.004]
 
{{PDB Gallery|geneid=840}}
{{Cysteine proteases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
[[Category:EC 3.4.22]]
[[Category:Caspases]]
 
 
{{gene-10-stub}}

Latest revision as of 11:38, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7 gene. CASP7 orthologs [1] 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.[2]

Interactions

Caspase 7 has been shown to interact with:

See also

References

  1. ↑ "OrthoMaM phylogenetic marker: CASP7 coding sequence".
  2. ↑ "Entrez Gene: CASP7 caspase 7, apoptosis-related cysteine peptidase".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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

External links

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


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