Calpain-1 catalytic subunit

Details

Name

Calpain-1 catalytic subunit

Synonyms

• 3.4.22.52
• Calcium-activated neutral proteinase 1
• Calpain mu-type
• Calpain-1 large subunit
• CANP 1
• CANPL1
• Cell proliferation-inducing gene 30 protein
• Micromolar-calpain
• muCANP

Gene Name

CAPN1

Organism

Humans

Amino acid sequence

>lcl|BSEQ0017070|Calpain-1 catalytic subunit
MSEEIITPVYCTGVSAQVQKQRARELGLGRHENAIKYLGQDYEQLRVRCLQSGTLFRDEA
FPPVPQSLGYKDLGPNSSKTYGIKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAA
IASLTLNDTLLHRVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHS
AEGNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPSDLYQIILK
ALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQVNYRGQVVSLIRMRNPWGE
VEWTGAWSDSSSEWNNVDPYERDQLRVKMEDGEFWMSFRDFMREFTRLEICNLTPDALKS
RTIRKWNTTLYEGTWRRGSTAGGCRNYPATFWVNPQFKIRLDETDDPDDYGDRESGCSFV
LALMQKHRRRERRFGRDMETIGFAVYEVPPELVGQPAVHLKRDFFLANASRARSEQFINL
REVSTRFRLPPGEYVVVPSTFEPNKEGDFVLRFFSEKSAGTVELDDQIQANLPDEQVLSE
EEIDENFKALFRQLAGEDMEISVKELRTILNRIISKHKDLRTKGFSLESCRSMVNLMDRD
GNGKLGLVEFNILWNRIRNYLSIFRKFDLDKSGSMSAYEMRMAIESAGFKLNKKLYELII
TRYSEPDLAVDFDNFVCCLVRLETMFRFFKTLDTDLDGVVTFDLFKWLQLTMFA

Number of residues

714

Molecular Weight

81889.325

Theoretical pI

5.35

GO Classification

Functions

calcium ion binding / calcium-dependent cysteine-type endopeptidase activity

Processes

extracellular matrix disassembly / extracellular matrix organization / mammary gland involution / positive regulation of cell proliferation / protein autoprocessing / proteolysis / receptor catabolic process

Components

cytoplasm / cytosol / extracellular exosome / focal adhesion / lysosome / membrane / mitochondrion / plasma membrane

General Function

Calcium-dependent cysteine-type endopeptidase activity

Specific Function

Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.

Pfam Domain Function

• Calpain_III (PF01067)
• Peptidase_C2 (PF00648)
• EF-hand_8 (PF13833)

Transmembrane Regions

Not Available

Cellular Location

Cytoplasm

Gene sequence

>lcl|BSEQ0017071|Calpain-1 catalytic subunit (CAPN1)
ATGTCGGAGGAGATCATCACGCCGGTGTACTGCACTGGGGTGTCAGCCCAAGTGCAGAAG
CAGCGGGCCAGGGAGCTGGGCCTGGGCCGCCATGAGAATGCCATCAAGTACCTGGGCCAG
GATTATGAGCAGCTGCGGGTGCGATGCCTGCAGAGTGGGACCCTCTTCCGTGATGAGGCC
TTCCCCCCGGTACCCCAGAGCCTGGGTTACAAGGACCTGGGTCCCAATTCCTCCAAGACC
TATGGCATCAAGTGGAAGCGTCCCACGGAACTGCTGTCAAACCCCCAGTTCATTGTGGAT
GGAGCTACCCGCACAGACATCTGCCAGGGAGCACTGGGGGACTGCTGGCTCTTGGCGGCC
ATCGCCTCCCTCACTCTCAACGACACCCTCCTGCACCGAGTGGTTCCGCACGGCCAGAGC
TTCCAGAATGGCTATGCCGGCATCTTCCATTTCCAGCTGTGGCAATTTGGGGAGTGGGTG
GACGTGGTCGTGGATGACCTGCTGCCCATCAAGGACGGGAAGCTAGTGTTCGTGCACTCT
GCCGAAGGCAACGAGTTCTGGAGCGCCCTGCTTGAGAAGGCCTATGCCAAGGTAAATGGC
AGCTACGAGGCCCTGTCAGGGGGCAGCACCTCAGAGGGCTTTGAGGACTTCACAGGCGGG
GTTACCGAGTGGTACGAGTTGCGCAAGGCTCCCAGTGACCTCTACCAGATCATCCTCAAG
GCGCTGGAGCGGGGCTCCCTGCTGGGCTGCTCCATAGACATCTCCAGCGTTCTAGACATG
GAGGCCATCACTTTCAAGAAGTTGGTGAAGGGCCATGCCTACTCTGTGACCGGGGCCAAG
CAGGTGAACTACCGAGGCCAGGTGGTGAGCCTGATCCGGATGCGGAACCCCTGGGGCGAG
GTGGAGTGGACGGGAGCCTGGAGCGACAGCTCCTCAGAGTGGAACAACGTGGACCCATAT
GAACGGGACCAGCTCCGGGTCAAGATGGAGGACGGGGAGTTCTGGATGTCATTCCGAGAC
TTCATGCGGGAGTTCACCCGCCTGGAGATCTGCAACCTCACACCCGACGCCCTCAAGAGC
CGGACCATCCGCAAATGGAACACCACACTCTACGAAGGCACCTGGCGGCGGGGGAGCACC
GCGGGGGGCTGCCGAAACTACCCAGCCACCTTCTGGGTGAACCCTCAGTTCAAGATCCGG
CTGGATGAGACGGATGACCCGGACGACTACGGGGACCGCGAGTCAGGCTGCAGCTTCGTG
CTCGCCCTTATGCAGAAGCACCGTCGCCGCGAGCGCCGCTTCGGCCGCGACATGGAGACT
ATTGGCTTCGCGGTCTACGAGGTCCCTCCGGAGCTGGTGGGCCAGCCGGCCGTACACTTG
AAGCGTGACTTCTTCCTGGCCAATGCGTCTCGGGCGCGCTCAGAGCAGTTCATCAACCTG
CGAGAGGTCAGCACCCGCTTCCGCCTGCCACCCGGGGAGTATGTGGTGGTGCCCTCCACC
TTCGAGCCCAACAAGGAGGGCGACTTCGTGCTGCGCTTCTTCTCAGAGAAGAGTGCTGGG
ACTGTGGAGCTGGATGACCAGATCCAGGCCAATCTCCCCGATGAGCAAGTGCTCTCAGAA
GAGGAGATTGACGAGAACTTCAAGGCCCTCTTCAGGCAGCTGGCAGGGGAGGACATGGAG
ATCAGCGTGAAGGAGTTGCGGACAATCCTCAATAGGATCATCAGCAAACACAAAGACCTG
CGGACCAAGGGCTTCAGCCTAGAGTCGTGCCGCAGCATGGTGAACCTCATGGATCGTGAT
GGCAATGGGAAGCTGGGCCTGGTGGAGTTCAACATCCTGTGGAACCGCATCCGGAATTAC
CTGTCCATCTTCCGGAAGTTTGACCTGGACAAGTCGGGCAGCATGAGTGCCTACGAGATG
CGGATGGCCATTGAGTCGGCAGGCTTCAAGCTCAACAAGAAGCTGTACGAGCTCATCATC
ACCCGCTACTCGGAGCCCGACCTGGCGGTCGACTTTGACAATTTCGTTTGCTGCCTGGTG
CGGCTAGAGACCATGTTCCGATTTTTCAAAACTCTGGACACAGATCTGGATGGAGTTGTG
ACCTTTGACTTGTTTAAGTGGTTGCAGCTGACCATGTTTGCATGA

Chromosome Location

11

Locus

11q13

External Identifiers

Resource	Link
UniProtKB ID	P07384
UniProtKB Entry Name	CAN1_HUMAN
GenBank Gene ID	X04366
GenAtlas ID	CAPN1
HGNC ID	HGNC:1476

General References

1. Aoki K, Imajoh S, Ohno S, Emori Y, Koike M, Kosaki G, Suzuki K: 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. 1986 Sep 15;205(2):313-7. [Article]
2. Sorimachi H, Ohmi S, Emori Y, Kawasaki H, Saido TC, Ohno S, Minami Y, Suzuki K: A novel member of the calcium-dependent cysteine protease family. Biol Chem Hoppe Seyler. 1990 May;371 Suppl:171-6. [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. Melloni E, Michetti M, Salamino F, Minafra R, Pontremoli S: Modulation of the calpain autoproteolysis by calpastatin and phospholipids. Biochem Biophys Res Commun. 1996 Dec 4;229(1):193-7. [Article]
5. Michetti M, Salamino F, Tedesco I, Averna M, Minafra R, Melloni E, Pontremoli S: Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization. FEBS Lett. 1996 Aug 19;392(1):11-5. [Article]
6. Michetti M, Salamino F, Minafra R, Melloni E, Pontremoli S: Calcium-binding properties of human erythrocyte calpain. Biochem J. 1997 Aug 1;325 ( Pt 3):721-6. [Article]
7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [Article]
8. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
9. Hsu CY, Henry J, Raymond AA, Mechin MC, Pendaries V, Nassar D, Hansmann B, Balica S, Burlet-Schiltz O, Schmitt AM, Takahara H, Paul C, Serre G, Simon M: Deimination of human filaggrin-2 promotes its proteolysis by calpain 1. J Biol Chem. 2011 Jul 1;286(26):23222-33. doi: 10.1074/jbc.M110.197400. Epub 2011 Apr 29. [Article]
10. Bienvenut WV, Sumpton D, Martinez A, Lilla S, Espagne C, Meinnel T, Giglione C: Comparative large scale characterization of plant versus mammal proteins reveals similar and idiosyncratic N-alpha-acetylation features. Mol Cell Proteomics. 2012 Jun;11(6):M111.015131. doi: 10.1074/mcp.M111.015131. Epub 2012 Jan 5. [Article]
11. Van Damme P, Lasa M, Polevoda B, Gazquez C, Elosegui-Artola A, Kim DS, De Juan-Pardo E, Demeyer K, Hole K, Larrea E, Timmerman E, Prieto J, Arnesen T, Sherman F, Gevaert K, Aldabe R: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54. doi: 10.1073/pnas.1210303109. Epub 2012 Jul 18. [Article]
12. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
13. Li Q, Hanzlik RP, Weaver RF, Schonbrunn E: Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core. Biochemistry. 2006 Jan 24;45(3):701-8. [Article]

Drug Relations

Drug Relations

DrugBank ID	Name	Drug group	Pharmacological action?	Actions	Details
DB04276	4-[[(2S)-2-[[(2S)-3-Carboxy-2-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]butyl-(diaminomethylidene)azanium	experimental	unknown		Details
DB04653	N-[(benzyloxy)carbonyl]-L-leucyl-N-[(1S)-3-fluoro-1-(4-hydroxybenzyl)-2-oxopropyl]-L-leucinamide	experimental	unknown		Details
DB07627	(2S)-4-METHYL-2-(3-PHENYLTHIOUREIDO)-N-((3S)-TETRAHYDRO-2-HYDROXY-3-FURANYL)PENTANAMIDE	experimental	unknown		Details