P43367 · CAN2_PIG
- ProteinCalpain-2 catalytic subunit
- GeneCAPN2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids324 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs.
Cofactor
Note: Binds 7 Ca2+ ions.
Activity regulation
Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 166 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 169 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 171 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 176 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 209 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 211 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 213 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 215 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 220 | Ca2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 239 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 241 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 243 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 245 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 250 | Ca2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 282 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 285 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | dendrite | |
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent cysteine-type endopeptidase activity | |
Biological Process | cellular response to amino acid stimulus | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCalpain-2 catalytic subunit
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionP43367
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: Translocates to the plasma membrane upon Ca2+ binding.
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000207703 | 1-324 | Calpain-2 catalytic subunit | |||
Sequence: YPNTFWMNPQYLIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLSKNFFLTHRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQVVDDEIEADLEENDASEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCRIMVDMLDSDGSAKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFRISKQLDSENTGTIELDLISWLCFSVL |
Proteomic databases
Expression
Tissue specificity
Ubiquitous.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-138 | Domain III | ||||
Sequence: YPNTFWMNPQYLIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLSKNFFLTHRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQVVDD | ||||||
Region | 139-153 | Linker | ||||
Sequence: EIEADLEENDASEDD | ||||||
Region | 158-324 | Domain IV | ||||
Sequence: FRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCRIMVDMLDSDGSAKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFRISKQLDSENTGTIELDLISWLCFSVL | ||||||
Domain | 190-224 | EF-hand 1 | ||||
Sequence: DIKSDGFSIETCRIMVDMLDSDGSAKLGLKEFYIL | ||||||
Domain | 226-261 | EF-hand 2 | ||||
Sequence: TKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFK |
Sequence similarities
Belongs to the peptidase C2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Length324
- Mass (Da)37,809
- Last updated1997-11-01 v2
- Checksum3929553239E123CF
Features
Showing features for non-terminal residue, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: Y | ||||||
Sequence conflict | 202 | in Ref. 2; AAB17381 | ||||
Sequence: R → K |
Keywords
- Technical term