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calpain-1 catalytic [large] subunit (calpain large polypeptide L1, CAPN1)
Function:
- Ca+2-regulated non-lysosomal thiol-protease
- catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling & signal transduction
- forms a heterodimer with a small (regulatory) subunit (CAPNS1)
- activated by micromolar concentrations of Ca+2
- inhibited by calpastatin
- broad endopeptidase specificity
Cofactor: binds 3 Ca+2
Structure:
- belongs to the peptidase C2 family
- contains 1 calpain catalytic domain
- contains 4 EF-hand domains
Compartment:
- cytoplasm (putative)
- cell membrane
- translocates to the plasma membrane upon Ca+2 binding (putative)
Expression: ubiquitous
General
calpain catalytic or large subunit
Properties
SIZE: entity length = 714 aa
MW = 82 kD
COMPARTMENT: cytoplasm
MOTIF: catalytic domain
SITE: 55-354
MOTIF: cysteine residue {C115}
histidine residue {H272}
asparagine residue {N296}
Domain III {355-526}
Linker {527-542}
EF hand
SITE: 541-576
Domain IV {543-713}
MOTIF: EF hand
SITE: 585-618
Ca+2-binding site
SITE: 598-609
EF hand
SITE: 615-650
Ca+2-binding site
SITE: 628-639
EF hand
SITE: 680-714
Database Correlations
OMIM 114220
UniProt P07384
PFAM correlations
Entrez Gene 823
KEGG correlations
ENZYME 3.4.22.52
References
- UniProt :accession P07384
- CaBP; Note: calpain
http://structbio.vanderbilt.edu/cabp_database/general/prot_pages/calpain.html
- calpains homepage
http://ag.arizona.edu/calpains/
- Melloni E & Pontremoli S
The calpains.
Trends Neurosci. 1989 Nov;12(11):438-44. Review.
PMID: 2479145
Component-of
calpain-1 or calcium-activated neutral protease-mu type