logo CaMPDB: Calpain for Modulatory Proteolysis Database

CL0021 : Chain B, Catalytic Domain Of Human Calpain-1

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein NamesCalpain-1 catalytic subunit;; Calpain-1 large subunit; Calcium-activated neutral proteinase 1; CANP 1; Calpain mu-type; muCANP; Micromolar-calpain; Cell proliferation-inducing gene 30 protein
Gene NamesPIG30; CANPL1
Gene LocusNot available
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
2ARY_B N/A N/A P07384 N/A N/A N/A hsa:823

* Information From OMIM

Not Available.

* Structure Information

1. Primary Information

Length: 351 aa

Average Mass: 39.532 kDa

Monoisotopic Mass: 39.507 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Peptidase_C2 1. 46345814.66.2e-242

3. Sequence Information

Fasta Sequence: CL0021.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1ZCM (X-ray; 200 A; A=33-353), 2ARY (X-ray; 240 A; A/B=27-360)

* References

[PubMed ID: 17157313] Davis TL, Walker JR, Finerty PJ Jr, Mackenzie F, Newman EM, Dhe-Paganon S, The crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition. J Mol Biol. 2007 Feb 9;366(1):216-29. Epub 2006 Nov 14.