Calpain-1 catalytic subunit

CAPN1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ZCM, 2ARY
Identifiers
Aliases	CAPN1 , CANP, CANP1, CANPL1, muCANP, muCL, SPG76, calpain 1
External IDs	OMIM: 114220 MGI: 88263 HomoloGene: 3800 GeneCards: CAPN1
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q13.1 Start 65,180,566 bp [1] End 65,212,006 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19 A|19 4.34 cM Start 6,038,573 bp [2] End 6,065,927 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of abdomen minor salivary gland right uterine tube right lobe of thyroid gland left lobe of thyroid gland gallbladder gastric mucosa canal of the cervix body of pancreas vagina Top expressed in lip esophagus corneal stroma ankle triceps brachii muscle knee joint extensor digitorum longus muscle thymus skeletal muscle tissue ileum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cysteine-type peptidase activity metal ion binding peptidase activity protein binding hydrolase activity endopeptidase activity calcium ion binding calcium-dependent cysteine-type endopeptidase activity Cellular component membrane focal adhesion intracellular anatomical structure mitochondrion lysosome extracellular exosome cytosol extracellular region cytoplasm plasma membrane ficolin-1-rich granule lumen Biological process extracellular matrix disassembly receptor catabolic process positive regulation of cell population proliferation regulation of macroautophagy mammary gland involution neutrophil degranulation regulation of catalytic activity cornification self proteolysis proteolysis regulation of NMDA receptor activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 823 12333 Ensembl ENSG00000014216 ENSMUSG00000024942 UniProt P07384 O35350 RefSeq (mRNA) NM_001198868 NM_001198869 NM_005186 NM_001110504 NM_007600 RefSeq (protein) NP_001185797 NP_001185798 NP_005177 NP_001103974 NP_031626 Location (UCSC) Chr 11: 65.18 – 65.21 Mb Chr 19: 6.04 – 6.07 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Calpain-1 catalytic subunit(CANP 1) is a protein that in humans is encoded by the CAPN1 gene. ^{[5] [6] [7]}

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. ^[7]

Interactions

CAPN1 has been shown to interact with PSEN2. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000014216 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024942 - 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.
5. 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.
6. 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.
7. "Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit".
8. 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.

Further reading

• 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 .