logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0020 : CAPN1, [mu]-calpain catalytic subunit, [mu]CL

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namescalpain-1 catalytic subunit [Homo sapiens]; calpain-1 catalytic subunit; calpain, large polypeptide L1; cell proliferation-inducing protein 30; CANP 1; calpain mu-type; micromolar-calpain; calpain-1 large subunit; calcium-activated neutral proteinase 1; cell proliferation-inducing gene 30 protein; Calpain-1 catalytic subunit;; Calcium-activated neutral proteinase 1; Calpain mu-type; Calpain-1 large subunit; Cell proliferation-inducing gene 30 protein; Micromolar-calpain; muCANP
Gene NamesCAPN1; PIG30; CANPL1; calpain 1, (mu/I) large subunit
Gene Locus11q13; chromosome 11
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_005177 NM_005186 823 P07384 114220 HGNC:1476 00253 hsa:823

* Information From OMIM

Description: Calpain (calcium-dependent protease; EC is an intracellular protease that requires calcium for its catalytic activity. Two isozymes, calpain I (mu-calpain) and calpain II (m-calpain), with different calcium requirements, have been identified. Both are heterodimers composed of L (large, catalytic, 80 kD) and S (small, regulatory, 30 kD) subunits. The isozymes share an identical S subunit (CAPNS1; OMIM:114170), with the differences arising from the L subunits, L1 (CAPN1) and L2 (CAPN2; OMIM:114230) (summary by Ohno et al., 1990).

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* Structure Information

1. Primary Information

Length: 714 aa

Average Mass: 81.889 kDa

Monoisotopic Mass: 81.838 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
--- cleavage 15 ---
--- cleavage 27 ---
Calpain large subunit, domain III 1. 8710022.00.0
Calpain family cysteine protease 1. 49653274.00.0
EF-hand domain pair 1. 53654821.00.0
EF-hand domain pair 2. 56161116.00.1
EF-hand domain pair 3. 62263430.00.0
EF-hand domain pair 4. 68670329.00.6

3. Sequence Information

Fasta Sequence: SB0020.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1ZCM (X-ray; 200 A; A=33-353), 2ARY (X-ray; 240 A; A/B=29-360)

* Cleavage Information

2 [sites] cleaved by Calpain 1

Source Reference: [PubMed ID: 2065086] Zimmerman UJ, Schlaepfer WW, Two-stage autolysis of the catalytic subunit initiates activation of calpain I. Biochim Biophys Acta. 1991 Jun 24;1078(2):192-8.

Cleavage sites (±10aa)


Ser15 Ala

iTraq-117 Signal 83088.7 () for AQVQKQRARE

iTraq-117 Signal 2676.5 () for QVQKQRARE

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Gly27 Leu

iTraq-117 Signal 11038.2 () for VQKQRARELG

iTraq-117 Signal 151277.7 () for LGRHENAIKY

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 24416790] Kim H, Kang AY, Ko AR, Park HC, So I, Park JH, Cheong HI, Hwang YH, Ahn C, Calpain-mediated proteolysis of polycystin-1 C-terminus induces JAK2 and ERK signal alterations. Exp Cell Res. 2014 Jan 1;320(1):62-8.

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