CAPN5: Difference between revisions
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{{ | '''Calpain-5''' is a [[protein]] that in humans is encoded by the ''CAPN5'' [[gene]].<ref name="pmid9503024">{{cite journal | vauthors = Matena K, Boehm T, Dear N | title = Genomic organization of mouse Capn5 and Capn6 genes confirms that they are a distinct calpain subfamily | journal = Genomics | volume = 48 | issue = 1 | pages = 117–20 |date=Apr 1998 | pmid = 9503024 | pmc = | doi =10.1006/geno.1997.5133 }}</ref><ref name="pmid9367857">{{cite journal | vauthors = Mugita N, Kimura Y, Ogawa M, Saya H, Nakao M | title = Identification of a novel, tissue-specific calpain htra-3; a human homologue of the Caenorhabditis elegans sex determination gene | journal = Biochem Biophys Res Commun | volume = 239 | issue = 3 | pages = 845–50 |date=Dec 1997 | pmid = 9367857 | pmc = | doi = 10.1006/bbrc.1997.7571 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CAPN5 calpain 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=726| accessdate = }}</ref> | ||
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| summary_text = Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the large subunits. Unlike some of the calpains, CAPN5 and CAPN6 lack a calmodulin-like domain IV. Because of the significant similarity to Caenorhabditis elegans sex determination gene tra-3, CAPN5 is also called as HTRA3.<ref name="entrez" | | summary_text = Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the large subunits. Unlike some of the calpains, CAPN5 and CAPN6 lack a calmodulin-like domain IV. Because of the significant similarity to Caenorhabditis elegans sex determination gene tra-3, CAPN5 is also called as HTRA3.<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Vanderklish PW, Bahr BA |title=The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states |journal=International journal of experimental pathology |volume=81 |issue= 5 |pages= 323–39 |year= 2001 |pmid= 11168679 |doi=10.1111/j.1365-2613.2000.00169.x |pmc=2517738}} | ||
*{{cite journal | | *{{cite journal | vauthors=Sato K, Kawashima S |title=Calpain function in the modulation of signal transduction molecules |journal=Biol. Chem. |volume=382 |issue= 5 |pages= 743–51 |year= 2002 |pmid= 11517927 |doi=10.1515/BC.2001.090 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Dear N, Matena K, Vingron M, Boehm T |title=A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution |journal=Genomics |volume=45 |issue= 1 |pages= 175–84 |year= 1997 |pmid= 9339374 |doi= 10.1006/geno.1997.4870 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}} | |||
*{{cite journal | vauthors=Waghray A, Wang DS, McKinsey D |title=Molecular cloning and characterization of rat and human calpain-5 |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 1 |pages= 46–51 |year= 2004 |pmid= 15464980 |doi= 10.1016/j.bbrc.2004.09.012 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=González A, Sáez ME, Aragón MJ |title=Specific haplotypes of the CALPAIN-5 gene are associated with polycystic ovary syndrome |journal=Hum. Reprod. |volume=21 |issue= 4 |pages= 943–51 |year= 2006 |pmid= 16396936 |doi= 10.1093/humrep/dei443 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Sáez ME, Martínez-Larrad MT, Ramírez-Lorca R |title=Calpain-5 gene variants are associated with diastolic blood pressure and cholesterol levels |journal=BMC Med. Genet. |volume=8|pages= 1 |year= 2007 |pmid= 17227582 |doi= 10.1186/1471-2350-8-1 | pmc=1783645 |display-authors=etal}} | ||
*{{cite journal | | |||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{ | ==External links== | ||
{{ | * The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=C02.011 C02.011] | ||
* {{UCSC gene info|CAPN5}} | |||
* {{UCSC gene info|HTRA3}} | |||
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{{Cysteine proteases}} | |||
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Latest revision as of 09:11, 30 August 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
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/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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Calpain-5 is a protein that in humans is encoded by the CAPN5 gene.[1][2][3]
Calpains are calcium-dependent cysteine proteases involved in signal transduction in a variety of cellular processes. A functional calpain protein consists of an invariant small subunit and 1 of a family of large subunits. CAPN5 is one of the large subunits. Unlike some of the calpains, CAPN5 and CAPN6 lack a calmodulin-like domain IV. Because of the significant similarity to Caenorhabditis elegans sex determination gene tra-3, CAPN5 is also called as HTRA3.[3]
References
- ↑ Matena K, Boehm T, Dear N (Apr 1998). "Genomic organization of mouse Capn5 and Capn6 genes confirms that they are a distinct calpain subfamily". Genomics. 48 (1): 117–20. doi:10.1006/geno.1997.5133. PMID 9503024.
- ↑ Mugita N, Kimura Y, Ogawa M, Saya H, Nakao M (Dec 1997). "Identification of a novel, tissue-specific calpain htra-3; a human homologue of the Caenorhabditis elegans sex determination gene". Biochem Biophys Res Commun. 239 (3): 845–50. doi:10.1006/bbrc.1997.7571. PMID 9367857.
- ↑ 3.0 3.1 "Entrez Gene: CAPN5 calpain 5".
Further reading
- Vanderklish PW, Bahr BA (2001). "The pathogenic activation of calpain: a marker and mediator of cellular toxicity and disease states". International journal of experimental pathology. 81 (5): 323–39. doi:10.1111/j.1365-2613.2000.00169.x. PMC 2517738. PMID 11168679.
- Sato K, Kawashima S (2002). "Calpain function in the modulation of signal transduction molecules". Biol. Chem. 382 (5): 743–51. doi:10.1515/BC.2001.090. PMID 11517927.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Dear N, Matena K, Vingron M, Boehm T (1997). "A new subfamily of vertebrate calpains lacking a calmodulin-like domain: implications for calpain regulation and evolution". Genomics. 45 (1): 175–84. doi:10.1006/geno.1997.4870. PMID 9339374.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Waghray A, Wang DS, McKinsey D, et al. (2004). "Molecular cloning and characterization of rat and human calpain-5". Biochem. Biophys. Res. Commun. 324 (1): 46–51. doi:10.1016/j.bbrc.2004.09.012. PMID 15464980.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- González A, Sáez ME, Aragón MJ, et al. (2006). "Specific haplotypes of the CALPAIN-5 gene are associated with polycystic ovary syndrome". Hum. Reprod. 21 (4): 943–51. doi:10.1093/humrep/dei443. PMID 16396936.
- Sáez ME, Martínez-Larrad MT, Ramírez-Lorca R, et al. (2007). "Calpain-5 gene variants are associated with diastolic blood pressure and cholesterol levels". BMC Med. Genet. 8: 1. doi:10.1186/1471-2350-8-1. PMC 1783645. PMID 17227582.
External links
- The MEROPS online database for peptidases and their inhibitors: C02.011
- Human CAPN5 genome location and CAPN5 gene details page in the UCSC Genome Browser.
- Human HTRA3 genome location and HTRA3 gene details page in the UCSC Genome Browser.
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