[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2424911 [NCBI, ExPASy, EBI, Israel, Japan] Emori Y., Kawasaki H., Sugihara H., Imajoh S., Kawashima S., Suzuki K.; "Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease."; J. Biol. Chem. 261:9465-9471(1986).
[2]	AMINO-ACID COMPOSITION. PubMed=3667575 [NCBI, ExPASy, EBI, Israel, Japan] Kawasaki H., Imajoh S., Suzuki K.; "Separation of peptides on the basis of the difference in positive charge: simultaneous isolation of C-terminal and blocked N-terminal peptides from tryptic digests."; J. Biochem. 102:393-400(1987).
[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).

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 (By similarity).
ENZYME REGULATION: Activated by micromolar concentrations of calcium and inhibited by calpastatin.
SUBUNIT: Forms a heterodimer with a small (regulatory) subunit (CAPNS1).
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocates to the plasma membrane upon Ca(2+) binding (By similarity).
TISSUE SPECIFICITY: Ubiquitous.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the peptidase C2 family [view classification].
SIMILARITY: Contains 3 EF-hand domains.

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

M13363; AAA31456.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24815; A24815.

UniGene

Ocu.1955

3D structure databases

HSSP

P17655; 1KFX. [HSSP ENTRY / PDB]

ModBase

P06815.

Protein family/group databases

MEROPS

C02.001; -.

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.
Pfam graphical view of domain structure.

ProDom

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

SMART

SM00720; calpain_III; 1.
SM00054; EFh; 3.
SMART graphical view of domain structure.

PROSITE

PS00018; EF_HAND_1; 2.
PS50222; EF_HAND_2; 3.
PS00640; THIOL_PROTEASE_ASN; PARTIAL.
PS00139; THIOL_PROTEASE_CYS; PARTIAL.
PS00639; THIOL_PROTEASE_HIS; PARTIAL.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

P06815; -.

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`	`<1 302`	`>302`	`Calpain-1 catalytic subunit.`	`PRO_0000207699`
`DOMAIN`	`173 206`	`34`	`EF-hand 1.`
`DOMAIN`	`203 238`	`36`	`EF-hand 2.`
`DOMAIN`	`268 302`	`35`	`EF-hand 3.`
`CA_BIND`	`186 197`	`12`	`1.`
`CA_BIND`	`216 227`	`12`	`2.`
`REGION`	`<1 114`	`>114`	`Domain III.`
`REGION`	`115 130`	`16`	`Linker.`
`REGION`	`131 301`	`171`	`Domain IV.`
`NON_TER`	`1 1`

Sequence information

Length: 302 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 35275 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 178BFEF4216C6EAB [This is a checksum on the sequence]

        10         20         30         40         50         60 
RESGCSFVLA LMQKHRRRER RFGRDMETIG FAVYEVPREL VGQPALHLKR DFFLANASRA 

        70         80         90        100        110        120 
RSEQFINLRE VSTRFRLPPG EYVVVPSTFE PNKEGDFVLR FFSEKRAGTQ ELDDQIQANL 

       130        140        150        160        170        180 
PDEQVLSAEE IDENFKALFR QLAGEDLEIS VRELQTILNR ITSKHKDLRT KGFSMESCRS 

       190        200        210        220        230        240 
MVNLMDRDGN GKLGLVEFNI LWNRIRNYLA IFRKFDLDKS GSMSAYEMRM AIESAGFKLN 

       250        260        270        280        290        300 
KKLYELIITR YSEPDLAVDF DNFVCCLVRL ETMFRFFKTL DTDLDGVVTF DLFKWLQLTM 


FA

P06815 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