[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1038/312566a0; PubMed=6095110 [NCBI, ExPASy, EBI, Israel, Japan] Ohno S., Emori Y., Imajoh S., Kawasaki H., Kisaragi M., Suzuki K.; "Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?"; Nature 312:566-570(1984).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-5793(86)80094-1; PubMed=3000828 [NCBI, ExPASy, EBI, Israel, Japan] Emori Y., Ohno S., Tobita M., Suzuki K.; "Gene structure of calcium-dependent protease retains the ancestral organization of the calcium-binding protein gene."; FEBS Lett. 194:249-252(1986).
[3]	CALCIUM-BINDING DATA. PubMed=3038855 [NCBI, ExPASy, EBI, Israel, Japan] 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. 101:889-895(1987).
[4]	CHARACTERIZATION. DOI=10.1016/0167-4781(95)00027-E; PubMed=7742367 [NCBI, ExPASy, EBI, Israel, Japan] Sorimachi H., Tsukahara T., Okada-Ban M., Sugita H., Ishiura S., Suzuki K.; "Identification of a third ubiquitous calpain species -- chicken muscle expresses four distinct calpains."; Biochim. Biophys. Acta 1261:381-393(1995).

Comments

FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
CATALYTIC ACTIVITY: Broad endopeptidase specificity.
COFACTOR: Binds 3 calcium ions.
ENZYME REGULATION: Activated by micromolar concentrations of calcium and inhibited by calpastatin.
SUBUNIT: Heterodimer of large (catalytic) and a small (regulatory) subunit.
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocates to the plasma membrane upon Ca(2+) binding (By similarity).
TISSUE SPECIFICITY: Ubiquitously expressed.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the peptidase C2 family [view classification].
SIMILARITY: Contains 1 calpain catalytic domain.
SIMILARITY: Contains 3 EF-hand domains.
CAUTION: This protein was previously thought to be M-calpain but has since been found to be an intermediate form between the M and Mu types.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X01415; CAA25658.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A00979; CICHH.

NP_990634.1; -.

3D structure databases

HSSP

Q07009; 1MDW. [HSSP ENTRY / PDB]

ModBase

P00789.

Protein family/group databases

MEROPS

C02.003; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011992; EF-Hand_type.
IPR002048; EF_hand_Ca_bd.
IPR000169; Pept_cys_AS.
IPR001300; Peptidase_C2.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.238.10; EF-Hand_type; 1.

Pfam

PF01067; Calpain_III; 1.
PF00036; efhand; 2.
PF00648; Peptidase_C2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00704; CALPAIN.

ProDom

PD000012; EF-hand; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00720; calpain_III; 1.
SM00230; CysPc; 1.
SM00054; EFh; 2.
SMART graphical view of domain structure.

PROSITE

PS50203; CALPAIN_CAT; 1.
PS00018; EF_HAND_1; 1.
PS50222; EF_HAND_2; 2.
PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
PS00139; THIOL_PROTEASE_CYS; 1.
PS00639; THIOL_PROTEASE_HIS; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSGALG00000010186; Gallus gallus. [Contig view]

GeneID

396240; -.

KEGG

gga:396240; -.

Phylogenomic databases

HOVERGEN

P00789; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Cell membrane; Cytoplasm; Hydrolase; Membrane; Protease; Repeat; Thiol protease.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 705`	`705`	`Calpain-1 catalytic subunit.`	`PRO_0000207701`
`DOMAIN`	`48 347`	`300`	`Calpain catalytic.`
`DOMAIN`	`530 565`	`36`	`EF-hand 1.`
`DOMAIN`	`606 641`	`36`	`EF-hand 2.`
`DOMAIN`	`671 705`	`35`	`EF-hand 3.`
`CA_BIND`	`545 556`	`12`	`1.`
`CA_BIND`	`589 600`	`12`	`2.`
`CA_BIND`	`619 630`	`12`	`3.`
`REGION`	`348 517`	`170`	`Domain III.`
`REGION`	`518 533`	`16`	`Linker.`
`REGION`	`534 704`	`171`	`Domain IV.`
`ACT_SITE`	`108 108`		`By similarity.`
`ACT_SITE`	`265 265`		`By similarity.`
`ACT_SITE`	`289 289`		`By similarity.`

Sequence information

Length: 705 AA [This is the length of the unprocessed precursor]

Molecular weight: 80352 Da [This is the MW of the unprocessed precursor]

CRC64: ABCDDC56298E48AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMPFGGIAAR LQRDRLRAEG VGEHNNAVKY LNQDYEALKQ ECIESGTLFR DPQFPAGPTA 

        70         80         90        100        110        120 
LGFKELGPYS SKTRGVEWKR PSELVDDPQF IVGGATRTDI CQGALGDCWL LAAIGSLTLN 

       130        140        150        160        170        180 
EELLHRVVPH GQSFQEDYAG IFHFQIWQFG EWVDVVVDDL LPTKDGELLF VHSAECTEFW 

       190        200        210        220        230        240 
SALLEKAYAK LNGCYESLSG GSTTEGFEDF TGGVAEMYDL KRAPRNMGHI IRKALERGSL 

       250        260        270        280        290        300 
LGCSIDITSA FDMEAVTFKK LVKGHAYSVT AFKDVNYRGQ QEQLIRIRNP WGQVEWTGAW 

       310        320        330        340        350        360 
SDGSSEWDNI DPSDREELQL KMEDGEFWMS FRDFMREFSR LEICNLTPDA LTKDELSRWH 

       370        380        390        400        410        420 
TQVFEGTWRR GSTAGGCRNN PATFWINPQF KIKLLEEDDD PGDDEVACSF LVALMQKHRR 

       430        440        450        460        470        480 
RERRVGGDMH TIGFAVYEVP EEAQGSQNVH LKKDFFLRNQ SRARSETFIN LREVSNQIRL 

       490        500        510        520        530        540 
PPGEYIVVPS TFEPHKEADF ILRVFTEKQS DTAELDEEIS ADLADEEEIT EDDIEDGFKN 

       550        560        570        580        590        600 
MFQQLAGEDM EISVFELKTI LNRVIARHKD LKTDGFSLDS CRNMVNLMDK DGSARLGLVE 

       610        620        630        640        650        660 
FQILWNKIRS WLTIFRQYDL DKSGTMSSYE MRMALESAGF KLNNKLHQVV VARYADAETG 

       670        680        690        700 
VDFDNFVCCL VKLETMFRFF HSMDRDGTGT AVMNLAEWLL LTMCG

P00789 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools