Calpain-1 catalytic subunit

An Error has occurred retrieving Wikidata item for infobox Calpain-1 catalytic subunit (CANP 1) is a protein that in humans is encoded by the CAPN1 gene.^[1]^[2]^[3]

Function

The calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1.^[3]

Interactions

CAPN1 has been shown to interact with PSEN2.^[4]

References

^ Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K (Oct 1986). "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence". FEBS Lett. 205 (2): 313–7. doi:10.1016/0014-5793(86)80919-X. PMID 3017764. S2CID 36697759.
^ Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (Nov 1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenet Cell Genet. 53 (4): 225–9. doi:10.1159/000132937. PMID 2209092.
^ ^a ^b "Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit".
^ Shinozaki K, Maruyama K, Kume H, Tomita T, Saido TC, Iwatsubo T, Obata K (1998). "The presenilin 2 loop domain interacts with the mu-calpain C-terminal region". Int. J. Mol. Med. 1 (5): 797–9. doi:10.3892/ijmm.1.5.797. PMID 9852298.

Suzuki K, Sorimachi H, Yoshizawa T, Kinbara K, Ishiura S (1996). "Calpain: novel family members, activation, and physiologic function". Biol. Chem. Hoppe-Seyler. 376 (9): 523–9. doi:10.1515/bchm3.1995.376.9.523. PMID 8561910.
Huang Y, Wang KK (2001). "The calpain family and human disease". Trends in Molecular Medicine. 7 (8): 355–62. doi:10.1016/S1471-4914(01)02049-4. PMID 11516996.
Goll DE, Thompson VF, Li H, Wei W, Cong J (2003). "The calpain system". Physiol. Rev. 83 (3): 731–801. doi:10.1152/physrev.00029.2002. PMID 12843408.
Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL (1991). "Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP". J. Neurosci. Res. 29 (3): 346–54. doi:10.1002/jnr.490290310. PMID 1656060. S2CID 40120102.
Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K (1990). "A novel member of the calcium-dependent cysteine protease family". Biol. Chem. Hoppe-Seyler. 371 Suppl: 171–6. PMID 2400579.
Harris AS, Croall DE, Morrow JS (1988). "The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site". J. Biol. Chem. 263 (30): 15754–61. doi:10.1016/S0021-9258(19)37652-5. PMID 2844821.
Ishiguro H, Higashiyama S, Namikawa C, Kunimatsu M, Takano E, Tanaka K, Ohkubo I, Murachi T, Sasaki M (1987). "Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations". Biochemistry. 26 (10): 2863–70. doi:10.1021/bi00384a030. PMID 3038169.
Morishita R, Nakayama H, Isobe T, Matsuda T, Hashimoto Y, Okano T, Fukada Y, Mizuno K, Ohno S, Kozawa O (1996). "Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C". J. Biol. Chem. 270 (49): 29469–75. doi:10.1074/jbc.270.49.29469. PMID 7493986.
Kavita U, Mizel SB (1996). "Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease". J. Biol. Chem. 270 (46): 27758–65. doi:10.1074/jbc.270.46.27758. PMID 7499244.
Du X, Saido TC, Tsubuki S, Indig FE, Williams MJ, Ginsberg MH (1995). "Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit". J. Biol. Chem. 270 (44): 26146–51. doi:10.1074/jbc.270.44.26146. PMID 7592818.
Bradford HN, Jameson BA, Adam AA, Wassell RP, Colman RW (1994). "Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain". J. Biol. Chem. 268 (35): 26546–51. doi:10.1016/S0021-9258(19)74347-6. PMID 8253784.
Oda A, Ozaki K, Druker BJ, Miyakawa Y, Miyazaki H, Handa M, Morita H, Ohashi H, Ikeda Y (1996). "p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin". Blood. 88 (4): 1330–8. doi:10.1182/blood.V88.4.1330.bloodjournal8841330. PMID 8695851.
Zhang W, Lane RD, Mellgren RL (1996). "The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells". J. Biol. Chem. 271 (31): 18825–30. doi:10.1074/jbc.271.31.18825. PMID 8702541.
Courseaux A, Grosgeorge J, Gaudray P, Pannett AA, Forbes SA, Williamson C, Bassett D, Thakker RV, Teh BT, Farnebo F, Shepherd J, Skogseid B, Larsson C, Giraud S, Zhang CX, Salandre J, Calender A (1997). "Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1)". Genomics. 37 (3): 354–65. doi:10.1006/geno.1996.0570. PMID 8938448.
Corasaniti MT, Navarra M, Catani MV, Melino G, Nisticò G, Finazzi-Agrò A (1997). "NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain". Biochem. Biophys. Res. Commun. 229 (1): 299–304. doi:10.1006/bbrc.1996.1796. PMID 8954122.
Stabach PR, Cianci CD, Glantz SB, Zhang Z, Morrow JS (1997). "Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility". Biochemistry. 36 (1): 57–65. doi:10.1021/bi962034i. PMID 8993318.
Norris FA, Atkins RC, Majerus PW (1997). "Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets". J. Biol. Chem. 272 (17): 10987–9. doi:10.1074/jbc.272.17.10987. PMID 9110986.

External links

The MEROPS online database for peptidases and their inhibitors: C02.001
Human CAPN1 genome location and CAPN1 gene details page in the UCSC Genome Browser.

This article on a gene on human chromosome 11 is a stub. You can help Justapedia by expanding it.

[pmid3017764-1] Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K (Oct 1986). "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence". FEBS Lett. 205 (2): 313–7. doi:10.1016/0014-5793(86)80919-X. PMID 3017764. S2CID 36697759.

[pmid2209092-2] Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K (Nov 1990). "Four genes for the calpain family locate on four distinct human chromosomes". Cytogenet Cell Genet. 53 (4): 225–9. doi:10.1159/000132937. PMID 2209092.

[entrez-3] "Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit".

[pmid9852298-4] Shinozaki K, Maruyama K, Kume H, Tomita T, Saido TC, Iwatsubo T, Obata K (1998). "The presenilin 2 loop domain interacts with the mu-calpain C-terminal region". Int. J. Mol. Med. 1 (5): 797–9. doi:10.3892/ijmm.1.5.797. PMID 9852298.

[1]

[2]

[3]

[4]

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

Calpain-1 catalytic subunit

Contents

Function

Interactions

References

Further reading

External links

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