Calpain-3

Details

Name
Calpain-3
Kind
protein
Synonyms
  • 3.4.22.54
  • Calcium-activated neutral proteinase 3
  • Calpain L3
  • Calpain p94
  • CANP 3
  • CANP3
  • CANPL3
  • Muscle-specific calcium-activated neutral protease 3
  • nCL-1
  • NCL1
  • New calpain 1
Gene Name
CAPN3
UniProtKB Entry
P20807Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0006741|Calpain-3
MPTVISASVAPRTAAEPRSPGPVPHPAQSKATEAGGGNPSGIYSAIISRNFPIIGVKEKT
FEQLHKKCLEKKVLYVDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIDGANRTD
ICQGELGDCWFLAAIACLTLNQHLLFRVIPHDQSFIENYAGIFHFQFWRYGEWVDVVIDD
CLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVAEFFE
IRDAPSDMYKIMKKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLQ
DSDLDPRGSDERPTRTIIPVQYETRMACGLVRGHAYSVTGLDEVPFKGEKVKLVRLRNPW
GQVEWNGSWSDRWKDWSFVDKDEKARLQHQVTEDGEFWMSYEDFIYHFTKLEICNLTADA
LQSDKLQTWTVSVNEGRWVRGCSAGGCRNFPDTFWTNPQYRLKLLEEDDDPDDSEVICSF
LVALMQKNRRKDRKLGASLFTIGFAIYEVPKEMHGNKQHLQKDFFLYNASKARSKTYINM
REVSQRFRLPPSEYVIVPSTYEPHQEGEFILRVFSEKRNLSEEVENTISVDRPVKKKKTK
PIIFVSDRANSNKELGVDQESEEGKGKTSPDKQKQSPQPQPGSSDQESEEQQQFRNIFKQ
IAGDDMEICADELKKVLNTVVNKHKDLKTHGFTLESCRSMIALMDTDGSGKLNLQEFHHL
WNKIKAWQKIFKHYDTDQSGTINSYEMRNAVNDAGFHLNNQLYDIITMRYADKHMNIDFD
SFICCFVRLEGMFRAFHAFDKDGDGIIKLNVLEWLQLTMYA
Number of residues
821
Molecular Weight
94252.95
Theoretical pI
6.09
GO Classification
Functions
calcium ion binding / calcium-dependent cysteine-type endopeptidase activity / catalytic activity / cysteine-type peptidase activity / ligase regulator activity / peptidase activity / sodium ion binding / structural constituent of muscle / titin binding
Processes
apoptotic process / cellular response to calcium ion / cellular response to salt stress / G1 to G0 transition involved in cell differentiation / muscle cell cellular homeostasis / muscle organ development / muscle structure development / myofibril assembly / negative regulation of apoptotic process / negative regulation of protein sumoylation / positive regulation of NF-kappaB transcription factor activity / positive regulation of proteolysis / positive regulation of release of sequestered calcium ion into cytosol / positive regulation of satellite cell activation involved in skeletal muscle regeneration / protein localization to membrane / proteolysis / regulation of catalytic activity / regulation of myoblast differentiation / response to calcium ion / response to muscle activity / sarcomere organization / self proteolysis
Components
cytoplasm / cytosol / myofibril / nucleus / plasma membrane / T-tubule / Z disc
General Function
Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-409'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53 (PubMed:23357851, PubMed:27657329)
Specific Function
calcium ion binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0012423|Calpain-3 (CAPN3)
ATGCCGACCGTCATTAGCGCATCTGTGGCTCCAAGGACAGCGGCTGAGCCCCGGTCCCCA
GGGCCAGTTCCTCACCCGGCCCAGAGCAAGGCCACTGAGGCTGGGGGTGGAAACCCAAGT
GGCATCTATTCAGCCATCATCAGCCGCAATTTTCCTATTATCGGAGTGAAAGAGAAGACA
TTCGAGCAACTTCACAAGAAATGTCTAGAAAAGAAAGTTCTTTATGTGGACCCTGAGTTC
CCACCGGATGAGACCTCTCTCTTTTATAGCCAGAAGTTCCCCATCCAGTTCGTCTGGAAG
AGACCTCCGGAAATTTGCGAGAATCCCCGATTTATCATTGATGGAGCCAACAGAACTGAC
ATCTGTCAAGGAGAGCTAGGGGACTGCTGGTTTCTCGCAGCCATTGCCTGCCTGACCCTG
AACCAGCACCTTCTTTTCCGAGTCATACCCCATGATCAAAGTTTCATCGAAAACTACGCA
GGGATCTTCCACTTCCAGTTCTGGCGCTATGGAGAGTGGGTGGACGTGGTTATAGATGAC
TGCCTGCCAACGTACAACAATCAACTGGTTTTCACCAAGTCCAACCACCGCAATGAGTTC
TGGAGTGCTCTGCTGGAGAAGGCTTATGCTAAGCTCCATGGTTCCTACGAAGCTCTGAAA
GGTGGGAACACCACAGAGGCCATGGAGGACTTCACAGGAGGGGTGGCAGAGTTTTTTGAG
ATCAGGGATGCTCCTAGTGACATGTACAAGATCATGAAGAAAGCCATCGAGAGAGGCTCC
CTCATGGGCTGCTCCATTGATGATGGCACGAACATGACCTATGGAACCTCTCCTTCTGGT
CTGAACATGGGGGAGTTGATTGCACGGATGGTAAGGAATATGGATAACTCACTGCTCCAG
GACTCAGACCTCGACCCCAGAGGCTCAGATGAAAGACCGACCCGGACAATCATTCCGGTT
CAGTATGAGACAAGAATGGCCTGCGGGCTGGTCAGAGGTCACGCCTACTCTGTCACGGGG
CTGGATGAGGTCCCGTTCAAAGGTGAGAAAGTGAAGCTGGTGCGGCTGCGGAATCCGTGG
GGCCAGGTGGAGTGGAACGGTTCTTGGAGTGATAGATGGAAGGACTGGAGCTTTGTGGAC
AAAGATGAGAAGGCCCGTCTGCAGCACCAGGTCACTGAGGATGGAGAGTTCTGGATGTCC
TATGAGGATTTCATCTACCATTTCACAAAGTTGGAGATCTGCAACCTCACGGCCGATGCT
CTGCAGTCTGACAAGCTTCAGACCTGGACAGTGTCTGTGAACGAGGGCCGCTGGGTACGG
GGTTGCTCTGCCGGAGGCTGCCGCAACTTCCCAGATACTTTCTGGACCAACCCTCAGTAC
CGTCTGAAGCTCCTGGAGGAGGACGATGACCCTGATGACTCGGAGGTGATTTGCAGCTTC
CTGGTGGCCCTGATGCAGAAGAACCGGCGGAAGGACCGGAAGCTAGGGGCCAGTCTCTTC
ACCATTGGCTTCGCCATCTACGAGGTTCCCAAAGAGATGCACGGGAACAAGCAGCACCTG
CAGAAGGACTTCTTCCTGTACAACGCCTCCAAGGCCAGGAGCAAAACCTACATCAACATG
CGGGAGGTGTCCCAGCGCTTCCGCCTGCCTCCCAGCGAGTACGTCATCGTGCCCTCCACC
TACGAGCCCCACCAGGAGGGGGAATTCATCCTCCGGGTCTTCTCTGAAAAGAGGAACCTC
TCTGAGGAAGTTGAAAATACCATCTCCGTGGATCGGCCAGTGAAAAAGAAAAAAACCAAG
CCCATCATCTTCGTTTCGGACAGAGCAAACAGCAACAAGGAGCTGGGTGTGGACCAGGAG
TCAGAGGAGGGCAAAGGCAAAACAAGCCCTGATAAGCAAAAGCAGTCCCCACAGCCACAG
CCTGGCAGCTCTGATCAGGAAAGTGAGGAACAGCAACAATTCCGGAACATTTTCAAGCAG
ATAGCAGGAGATGACATGGAGATCTGTGCAGATGAGCTCAAGAAGGTCCTTAACACAGTC
GTGAACAAACACAAGGACCTGAAGACACACGGGTTCACACTGGAGTCCTGCCGTAGCATG
ATTGCGCTCATGGATACAGATGGCTCTGGAAAGCTCAACCTGCAGGAGTTCCACCACCTC
TGGAACAAGATTAAGGCCTGGCAGAAAATTTTCAAACACTATGACACAGACCAGTCCGGC
ACCATCAACAGCTACGAGATGCGAAATGCAGTCAACGACGCAGGATTCCACCTCAACAAC
CAGCTCTATGACATCATTACCATGCGGTACGCAGACAAACACATGAACATCGACTTTGAC
AGTTTCATCTGCTGCTTCGTTAGGCTGGAGGGCATGTTCAGAGCTTTTCATGCATTTGAC
AAGGATGGAGATGGTATCATCAAGCTCAACGTTCTGGAGTGGCTGCAGCTCACCATGTAT
GCCTGA
Chromosome Location
15
Locus
15q15.1
External Identifiers
ResourceLink
UniProtKB IDP20807
UniProtKB Entry NameCAN3_HUMAN
GenBank Gene IDBC003169
GeneCard IDCAPN3
GenAtlas IDCAPN3
HGNC IDHGNC:1480
PDB ID(s)4OKH, 6BDT, 6BGP, 6BJD, 6BKJ
KEGG IDhsa:825
NCBI Gene ID825
General References
  1. Richard I, Broux O, Allamand V, Fougerousse F, Chiannilkulchai N, Bourg N, Brenguier L, Devaud C, Pasturaud P, Roudaut C, et al.: Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 1995 Apr 7;81(1):27-40. [Article]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Sorimachi H, Imajoh-Ohmi S, Emori Y, Kawasaki H, Ohno S, Minami Y, Suzuki K: Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle. J Biol Chem. 1989 Nov 25;264(33):20106-11. [Article]
  5. Miller MK, Bang ML, Witt CC, Labeit D, Trombitas C, Watanabe K, Granzier H, McElhinny AS, Gregorio CC, Labeit S: The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules. J Mol Biol. 2003 Nov 7;333(5):951-64. [Article]
  6. Richard I, Roudaut C, Saenz A, Pogue R, Grimbergen JE, Anderson LV, Beley C, Cobo AM, de Diego C, Eymard B, Gallano P, Ginjaar HB, Lasa A, Pollitt C, Topaloglu H, Urtizberea JA, de Visser M, van der Kooi A, Bushby K, Bakker E, Lopez de Munain A, Fardeau M, Beckmann JS: Calpainopathy-a survey of mutations and polymorphisms. Am J Hum Genet. 1999 Jun;64(6):1524-40. [Article]
  7. Sarparanta J, Blandin G, Charton K, Vihola A, Marchand S, Milic A, Hackman P, Ehler E, Richard I, Udd B: Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies. J Biol Chem. 2010 Sep 24;285(39):30304-15. doi: 10.1074/jbc.M110.108720. Epub 2010 Jul 15. [Article]
  8. Fardeau M, Hillaire D, Mignard C, Feingold N, Feingold J, Mignard D, de Ubeda B, Collin H, Tome FM, Richard I, Beckmann J: Juvenile limb-girdle muscular dystrophy. Clinical, histopathological and genetic data from a small community living in the Reunion Island. Brain. 1996 Feb;119 ( Pt 1):295-308. [Article]
  9. Richard I, Brenguier L, Dincer P, Roudaut C, Bady B, Burgunder JM, Chemaly R, Garcia CA, Halaby G, Jackson CE, Kurnit DM, Lefranc G, Legum C, Loiselet J, Merlini L, Nivelon-Chevallier A, Ollagnon-Roman E, Restagno G, Topaloglu H, Beckmann JS: Multiple independent molecular etiology for limb-girdle muscular dystrophy type 2A patients from various geographical origins. Am J Hum Genet. 1997 May;60(5):1128-38. [Article]
  10. Dincer P, Leturcq F, Richard I, Piccolo F, Yalnizoglu D, de Toma C, Akcoren Z, Broux O, Deburgrave N, Brenguier L, Roudaut C, Urtizberea JA, Jung D, Tan E, Jeanpierre M, Campbell KP, Kaplan JC, Beckmann JS, Topaloglu H: A biochemical, genetic, and clinical survey of autosomal recessive limb girdle muscular dystrophies in Turkey. Ann Neurol. 1997 Aug;42(2):222-9. [Article]
  11. Urtasun M, Saenz A, Roudaut C, Poza JJ, Urtizberea JA, Cobo AM, Richard I, Garcia Bragado F, Leturcq F, Kaplan JC, Marti Masso JF, Beckmann JS, Lopez de Munain A: Limb-girdle muscular dystrophy in Guipuzcoa (Basque Country, Spain). Brain. 1998 Sep;121 ( Pt 9):1735-47. [Article]
  12. Haffner K, Speer A, Hubner C, Voit T, Oexle K: A small in-frame deletion within the protease domain of muscle-specific calpain, p94 causes early-onset limb-girdle muscular dystrophy 2A. Hum Mutat. 1998;Suppl 1:S298-300. [Article]
  13. Penisson-Besnier I, Richard I, Dubas F, Beckmann JS, Fardeau M: Pseudometabolic expression and phenotypic variability of calpain deficiency in two siblings. Muscle Nerve. 1998 Aug;21(8):1078-80. [Article]
  14. Kawai H, Akaike M, Kunishige M, Inui T, Adachi K, Kimura C, Kawajiri M, Nishida Y, Endo I, Kashiwagi S, Nishino H, Fujiwara T, Okuno S, Roudaut C, Richard I, Beckmann JS, Miyoshi K, Matsumoto T: Clinical, pathological, and genetic features of limb-girdle muscular dystrophy type 2A with new calpain 3 gene mutations in seven patients from three Japanese families. Muscle Nerve. 1998 Nov;21(11):1493-501. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
L-aminocarnityl-succinyl-leucyl-argininal-diethylacetalinvestigationalunknowntargetDetails