CAPN1

From Wikipedia, the free encyclopedia

Calpain 1, (mu/I) large subunit

PDB rendering based on 1zcm.

Available structures: 1zcm, 2ary

Identifiers

Symbol(s)

CAPN1; CANP; CANPL1; muCANP; muCL

External IDs

OMIM: 114220 MGI: 88263 HomoloGene: 3800

Gene ontology
Molecular Function:	• calpain activity • calcium ion binding
Cellular Component:	• intracellular
Biological Process:	• proteolysis • positive regulation of cell proliferation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005186 (mRNA)
NP_005177 (protein)

NM_007600 (mRNA)
NP_031626 (protein)

Location

Chr 11: 64.71 - 64.74 Mb

Chr 19: 5.99 - 6.02 Mb

Pubmed search

[1]

[2]

Calpain 1, (mu/I) large subunit, also known as CAPN1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit.

[edit] Further reading

Suzuki K, Sorimachi H, Yoshizawa T, et al. (1996). "Calpain: novel family members, activation, and physiologic function.". Biol. Chem. Hoppe-Seyler 376 (9): 523–9. PMID 8561910.
Huang Y, Wang KK (2001). "The calpain family and human disease.". Trends in molecular medicine 7 (8): 355–62. PMID 11516996.
Goll DE, Thompson VF, Li H, et al. (2003). "The calpain system.". Physiol. Rev. 83 (3): 731–801. doi:10.1152/physrev.00029.2002. PMID 12843408.
Banik NL, DeVries GH, Neuberger T, et al. (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.
Ohno S, Minoshima S, Kudoh J, et al. (1990). "Four genes for the calpain family locate on four distinct human chromosomes.". Cytogenet. Cell Genet. 53 (4): 225–9. PMID 2209092.
Sorimachi H, Ohmi S, Emori Y, et al. (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. PMID 2844821.
Aoki K, Imajoh S, Ohno S, et al. (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. PMID 3017764.
Ishiguro H, Higashiyama S, Namikawa C, et al. (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. PMID 3038169.
Morishita R, Nakayama H, Isobe T, et al. (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. 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. PMID 7499244.
Du X, Saido TC, Tsubuki S, et al. (1995). "Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit.". J. Biol. Chem. 270 (44): 26146–51. PMID 7592818.
Bradford HN, Jameson BA, Adam AA, et al. (1994). "Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain.". J. Biol. Chem. 268 (35): 26546–51. PMID 8253784.
Oda A, Ozaki K, Druker BJ, et al. (1996). "p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin.". Blood 88 (4): 1330–8. 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. PMID 8702541.
Courseaux A, Grosgeorge J, Gaudray P, et al. (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. PMID 8938448.
Corasaniti MT, Navarra M, Catani MV, et al. (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, et al. (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. PMID 9110986.