P43367 · CAN2_PIG

  • Protein
    Calpain-2 catalytic subunit
  • Gene
    CAPN2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

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.

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

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.

132450100150200250300
TypeIDPosition(s)Description
Binding site166Ca2+ 5 (UniProtKB | ChEBI)
Binding site169Ca2+ 5 (UniProtKB | ChEBI)
Binding site171Ca2+ 5 (UniProtKB | ChEBI)
Binding site176Ca2+ 5 (UniProtKB | ChEBI)
Binding site209Ca2+ 6 (UniProtKB | ChEBI)
Binding site211Ca2+ 6 (UniProtKB | ChEBI)
Binding site213Ca2+ 6 (UniProtKB | ChEBI)
Binding site215Ca2+ 6 (UniProtKB | ChEBI)
Binding site220Ca2+ 6 (UniProtKB | ChEBI)
Binding site239Ca2+ 7 (UniProtKB | ChEBI)
Binding site241Ca2+ 7 (UniProtKB | ChEBI)
Binding site243Ca2+ 7 (UniProtKB | ChEBI)
Binding site245Ca2+ 7 (UniProtKB | ChEBI)
Binding site250Ca2+ 7 (UniProtKB | ChEBI)
Binding site282Ca2+ 1 (UniProtKB | ChEBI)
Binding site285Ca2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent cysteine-type endopeptidase activity
Biological Processcellular response to amino acid stimulus
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Calpain-2 catalytic subunit
  • EC number
  • Alternative names
    • Calcium-activated neutral proteinase 2 (CANP 2)
    • Calpain M-type
    • Calpain-2 large subunit
    • Millimolar-calpain (M-calpain)

Gene names

    • Name
      CAPN2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    P43367

Proteomes

Subcellular Location

Cytoplasm
Cell membrane
Note: Translocates to the plasma membrane upon Ca2+ binding.

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002077031-324Calpain-2 catalytic subunit

Proteomic databases

Expression

Tissue specificity

Ubiquitous.

Interaction

Subunit

Forms a heterodimer with a small (regulatory) subunit (CAPNS1). Interacts with CPEB3; this leads to cleavage of CPEB3.

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-138Domain III
Region139-153Linker
Region158-324Domain IV
Domain190-224EF-hand 1
Domain226-261EF-hand 2

Sequence similarities

Belongs to the peptidase C2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    324
  • Mass (Da)
    37,809
  • Last updated
    1997-11-01 v2
  • Checksum
    3929553239E123CF
YPNTFWMNPQYLIKLEEEDEDQEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLSKNFFLTHRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQVVDDEIEADLEENDASEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCRIMVDMLDSDGSAKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFRISKQLDSENTGTIELDLISWLCFSVL

Features

Showing features for non-terminal residue, sequence conflict.

TypeIDPosition(s)Description
Non-terminal residue1
Sequence conflict202in Ref. 2; AAB17381

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U01181
EMBL· GenBank· DDBJ
AAC48401.1
EMBL· GenBank· DDBJ
mRNA
U71320
EMBL· GenBank· DDBJ
AAB17381.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

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