logo CaMPDB: Calpain for Modulatory Proteolysis Database

SB0001 : CAPN2, m-calpain catalytic subunit, mCL

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namescalpain 2, large subunit [Homo sapiens]; calpain 2, large subunit; calpain, large polypeptide L2; calcium-activated neutral proteinase; Calpain 2, large [catalytic] subunit; Calpain-2 catalytic subunit;; Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; Calpain large polypeptide L2; Calpain-2 large subunit; Millimolar-calpain; M-calpain
Gene NamesCAPN2; CANPL2; calpain 2, (m/II) large subunit
Gene Locus1q41-q42; chromosome 1
GO FunctionGO:0004198 - calpain activity [Evidence IEA]; GO:0005509 - calcium ion binding [Evidence IEA]
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_001739 NM_001748 824 P17655 114230 HGNC:1479 00254 hsa:824

* Information From OMIM

Description: The calpains, or calcium-activated neutral proteases (EC, are nonlysosomal intracellular cysteine proteases. The mammalian calpains include 2 ubiquitous isoforms, calpain I (mu-calpain) and calpain II (m-calpain), 2 stomach-specific proteins, and CAPN3 (OMIM:114240), which is muscle-specific. Calpain I and calpain II are heterodimers with distinct large subunits, encoded by the CAPN1 (OMIM:114220) and CAPN2 genes, respectively, associated with a common small subunit (CAPNS1; OMIM:114170).

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* Structure Information

1. Primary Information

Length: 700 aa

Average Mass: 80.006 kDa

Monoisotopic Mass: 79.956 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
--- cleavage 9 ---
--- cleavage 19 ---
Calpain family cysteine protease 1. 463421.00.0
Calpain large subunit, domain III 1. 3565061.00.0
EF-hand domain pair 1. 55259820.00.0
EF-hand domain pair 2. 61062131.00.0
EF hand 1. 65766817.00.0
EF hand 2. 6756804.00.0

3. Sequence Information

Fasta Sequence: SB0001.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1KFU (X-ray; 250 A; L=2-700), 1KFX (X-ray; 315 A; L=2-700), 2NQA (X-ray; 220 A; A/B=48-346)

* Cleavage Information

2 [sites] cleaved by Calpain 2

Source Reference: [PubMed ID: 8482370] Brown N, Crawford C, Structural modifications associated with the change in Ca2+ sensitivity on activation of m-calpain. FEBS Lett. 1993 May 3;322(1):65-8.

Cleavage sites (±10aa)


Ala9 Lys

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

Sequence conservation (by blast)


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: 17359359] Medana IM, Day NP, Hien TT, Mai NT, Bethell D, Phu NH, Turner GD, Farrar J, White NJ, Esiri MM, Cerebral calpain in fatal falciparum malaria. Neuropathol Appl Neurobiol. 2007 Apr;33(2):179-92.

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