[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]	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 (By similarity).
CATALYTIC ACTIVITY: Broad endopeptidase specificity.
COFACTOR: Binds 3 calcium ions.
ENZYME REGULATION: Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.
SUBUNIT: Forms a heterodimer with a small (regulatory) subunit (CAPNS1).
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.
TISSUE SPECIFICITY: Ubiquitous.
SIMILARITY: Belongs to the peptidase C2 family [view classification].
SIMILARITY: Contains 1 calpain catalytic domain.
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

M13797; AAA31455.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B24815; B24815.

UniGene

Ocu.1954

3D structure databases

HSSP

P17655; 1KFX. [HSSP ENTRY / PDB]

SMR

P06814; 1-422.

ModBase

P06814.

Protein family/group databases

MEROPS

C02.002; -.

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.

SMART

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

PROSITE

PS50203; CALPAIN_CAT; 1.
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

P06814; -.

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`	`<1 422`	`>422`	`Calpain-2 catalytic subunit.`	`PRO_0000207704`
`DOMAIN`	`<1 66`	`>66`	`Calpain catalytic.`
`DOMAIN`	`294 327`	`34`	`EF-hand 1.`
`DOMAIN`	`324 359`	`36`	`EF-hand 2.`
`DOMAIN`	`389 422`	`34`	`EF-hand 3.`
`CA_BIND`	`307 318`	`12`	`1.`
`CA_BIND`	`337 348`	`12`	`2.`
`REGION`	`67 236`	`170`	`Domain III.`
`REGION`	`237 251`	`15`	`Linker.`
`REGION`	`252 422`	`171`	`Domain IV.`
`ACT_SITE`	`8 8`		`By similarity.`
`NON_TER`	`1 1`

Sequence information

Length: 422 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 49494 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: AE4FA3C48A333C41 [This is a checksum on the sequence]

        10         20         30         40         50         60 
QKLIRIRNPW GEVEWTGRWN DNCPNWNTVD PEVRERLAER HEDGEFWMSF SDFLRHYSRL 

        70         80         90        100        110        120 
EICNLTPDTL TSDTYKKWKL TKMDGNWRRG STAGGCRNYP NTFWMNPQYV IKLEEEDEDQ 

       130        140        150        160        170        180 
EDGESGCTFL VGLIQKHRRR QRKMGEDMHT IGFGIYEVPE ELRGQTNIHL GKNFFLTTRA 

       190        200        210        220        230        240 
RERSDTFINL REVLNRFKLP PGEYILVPST FEPNKNGDFC VRVFSEKKAD YQAVDDEIEA 

       250        260        270        280        290        300 
DLEEADVSED DIDDGFRRLF AQLAGEDAEI SAFELQNILR RVLAKRQDIK TDGLSIETCK 

       310        320        330        340        350        360 
IMVDMLDSDG TGKLGLKEFY VLWTKIQKYQ KIYREIDVDR SGTMNSYEMR KALEEAGFKL 

       370        380        390        400        410        420 
PCQLHEVIVA RFADDQLIID FDNFVRCLVR LETLFKIFKQ LDPDNTGMIQ LDLISWLCFS 


VL

P06814 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