logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0104 : CAPN2, m-calpain catalytic subunit, mCL

[ CaMP Format ]

* Basic Information

OrganismOryctolagus cuniculus (rabbit)
Protein Namescalpain-2 catalytic subunit [Oryctolagus cuniculus]; calpain-2 catalytic subunit; M-calpain; calpain M-type; millimolar-calpain; calpain-2 large subunit; calcium-activated neutral proteinase 2
Gene NamesCAPN2; calpain 2, (m/II) large subunit
Gene Locus16; chromosome 16
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001182651 NM_001195722 100009092 N/A N/A N/A N/A N/A

* Information From OMIM

Not Available.

* Structure Information

1. Primary Information

Length: 700 aa

Average Mass: 79.824 kDa

Monoisotopic Mass: 79.775 kDa

2. Domain Information

Annotated Domains: Not Available.

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
--- cleavage 19 ---
OST-HTH/LOTUS domain 1. 3073396.00.0
Calpain large subunit, domain III 1. 3565061.00.0
OST-HTH/LOTUS domain 2. 55056326.00.0
EF hand 1. 5836007.00.0
EF-hand domain pair 1. 61062131.00.0
EF hand 2. 65766817.00.0
OST-HTH/LOTUS domain 3. 67268433.00.0

3. Sequence Information

Fasta Sequence: SB0104.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Not Available.

* Cleavage Information

1 [sites] cleaved by Calpain 2

Source Reference: [PubMed ID: 3023314] Imajoh S, Kawasaki H, Suzuki K, Limited autolysis of calcium-activated neutral protease (CANP): reduction of the Ca2+-requirement is due to the NH2-terminal processing of the large subunit. J Biochem. 1986 Sep;100(3):633-42.

Cleavage sites (±10aa)


Gly19 Ser

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: 3038855] Minami Y, Emori Y, Kawasaki H, Suzuki K, E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions. J Biochem. 1987 Apr;101(4):889-95.

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