[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0014-5793(86)80919-X; PubMed=3017764 [NCBI, ExPASy, EBI, Israel, Japan] Aoki K., Imajoh S., Ohno S., Emori Y., Koike M., Kosaki G., Suzuki K.; "Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence."; FEBS Lett. 205:313-317(1986).
[2]	NUCLEOTIDE SEQUENCE. PubMed=2400579 [NCBI, ExPASy, EBI, Israel, Japan] Sorimachi H., Ohmi S., Emori Y., Kawasaki H., Saido T.C., Ohno S., Minami Y., Suzuki K.; "A novel member of the calcium-dependent cysteine protease family."; Biol. Chem. Hoppe-Seyler 371:171-176(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-103; PRO-433; ARG-492 AND ILE-676. Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.; "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Kidney, and Placenta; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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: Forms a heterodimer with a small (regulatory) subunit (CAPNS1).
INTERACTION:
P53805-2:RCAN1; NbExp=1; IntAct=EBI-1542113, EBI-1541912;
SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By similarity). Note=Translocates to the plasma membrane upon Ca(2+) binding (By similarity).
TISSUE SPECIFICITY: Ubiquitous.
SIMILARITY: Belongs to the peptidase C2 family [view classification].
SIMILARITY: Contains 1 calpain catalytic domain.
SIMILARITY: Contains 4 EF-hand domains.
WEB RESOURCE: Name=CaBP; Note=Calpain; URL="http://structbio.vanderbilt.edu/cabp_database/general/prot_pages/calpain.html";.
WEB RESOURCE: Name=Calpains homepage; URL="http://ag.arizona.edu/calpains/";.

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

X04366; CAA27881.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY796340; AAV41878.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008751; AAH08751.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017200; AAH17200.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A26213; CIHUH.

NP_005177.2; -.

3D structure databases

PDB

1ZCM; X-ray; 2.00 A; A=33-353.	[ExPASy / RCSB / EBI]
2ARY; X-ray; 2.40 A; A/B=27-360.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1ZCM; -.
2ARY; -.

ModBase

P07384.

Protein-protein interaction databases

IntAct

P07384; -.

Protein family/group databases

MEROPS

C02.001; -.

Polymorphism databases

NIEHS-SNPs

CAPN1.

Organism-specific databases

HIX0009788; -.

HGNC:1476; CAPN1.

HPA005992; -.

114220; gene. [NCBI / EBI]

PharmGKB

PA26057; -.

GeneCards

P07384.

Gene expression databases

ArrayExpress

P07384; -.

CleanEx

HS_CAPN1; -.

GermOnline

ENSG00000014216; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008284;	Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
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; 3.
SMART graphical view of domain structure.

PROSITE

PS50203; CALPAIN_CAT; 1.
PS00018; EF_HAND_1; 2.
PS50222; EF_HAND_2; 4.
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

ENSG00000014216; Homo sapiens. [Contig view]

GeneID

823; -.

KEGG

hsa:823; -.

Phylogenomic databases

HOGENOM

P07384; -.

HOVERGEN

P07384; -.

Other

NextBio

3370; -.

SOURCE

CAPN1; Homo sapiens.

UniRef

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

Keywords

3D-structure; Calcium; Cell membrane; Cytoplasm; Hydrolase; Membrane; Polymorphism; Protease; Repeat; Thiol protease.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 714`	`714`	`Calpain-1 catalytic subunit.`	`PRO_0000207694`
`DOMAIN`	`55 354`	`300`	`Calpain catalytic.`
`DOMAIN`	`541 576`	`36`	`EF-hand 1.`
`DOMAIN`	`585 618`	`34`	`EF-hand 2.`
`DOMAIN`	`615 650`	`36`	`EF-hand 3.`
`DOMAIN`	`680 714`	`35`	`EF-hand 4.`
`CA_BIND`	`598 609`	`12`	`1.`
`CA_BIND`	`628 639`	`12`	`2.`
`REGION`	`355 526`	`172`	`Domain III.`
`REGION`	`527 542`	`16`	`Linker.`
`REGION`	`543 713`	`171`	`Domain IV.`
`ACT_SITE`	`115 115`		`By similarity.`
`ACT_SITE`	`272 272`		`By similarity.`
`ACT_SITE`	`296 296`		`By similarity.`
`VARIANT`	`103 103`	`1`	`T -> A (in dbSNP:rs17885718 [NCBI]).`	`VAR_021085 [3D]`
`VARIANT`	`433 433`	`1`	`R -> P (in dbSNP:rs10895991 [NCBI]).`	`VAR_021086`
`VARIANT`	`492 492`	`1`	`G -> R (in dbSNP:rs17883283 [NCBI]).`	`VAR_021087`
`VARIANT`	`676 676`	`1`	`V -> I (in dbSNP:rs17884773 [NCBI]).`	`VAR_021088`
`CONFLICT`	`548 548`		`K -> N (in Ref. 4; AAH08751).`
`HELIX`	`37 39`	`3`
`HELIX`	`42 51`	`10`
`HELIX`	`65 68`	`4`
`HELIX`	`78 80`	`3`
`STRAND`	`84 86`	`3`
`HELIX`	`88 91`	`4`
`STRAND`	`99 102`	`4`
`HELIX`	`104 106`	`3`
`STRAND`	`111 113`	`3`
`HELIX`	`115 124`	`10`
`HELIX`	`128 134`	`7`
`STRAND`	`147 155`	`9`
`STRAND`	`158 166`	`9`
`STRAND`	`168 171`	`4`
`STRAND`	`174 177`	`4`
`HELIX`	`187 198`	`12`
`HELIX`	`203 205`	`3`
`HELIX`	`210 216`	`7`
`STRAND`	`221 226`	`6`
`HELIX`	`227 229`	`3`
`HELIX`	`234 244`	`11`
`STRAND`	`247 251`	`5`
`STRAND`	`256 258`	`3`
`STRAND`	`274 284`	`11`
`STRAND`	`287 295`	`9`
`HELIX`	`312 316`	`5`
`HELIX`	`319 325`	`7`
`STRAND`	`331 337`	`7`
`HELIX`	`338 344`	`7`
`STRAND`	`347 352`	`6`

Sequence information

Length: 714 AA [This is the length of the unprocessed precursor]

Molecular weight: 81890 Da [This is the MW of the unprocessed precursor]

CRC64: 1CB6D7C56D063498 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSEEIITPVY CTGVSAQVQK QRARELGLGR HENAIKYLGQ DYEQLRVRCL QSGTLFRDEA 

        70         80         90        100        110        120 
FPPVPQSLGY KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD GATRTDICQG ALGDCWLLAA 

       130        140        150        160        170        180 
IASLTLNDTL LHRVVPHGQS FQNGYAGIFH FQLWQFGEWV DVVVDDLLPI KDGKLVFVHS 

       190        200        210        220        230        240 
AEGNEFWSAL LEKAYAKVNG SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK 

       250        260        270        280        290        300 
ALERGSLLGC SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQVVS LIRMRNPWGE 

       310        320        330        340        350        360 
VEWTGAWSDS SSEWNNVDPY ERDQLRVKME DGEFWMSFRD FMREFTRLEI CNLTPDALKS 

       370        380        390        400        410        420 
RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LDETDDPDDY GDRESGCSFV 

       430        440        450        460        470        480 
LALMQKHRRR ERRFGRDMET IGFAVYEVPP ELVGQPAVHL KRDFFLANAS RARSEQFINL 

       490        500        510        520        530        540 
REVSTRFRLP PGEYVVVPST FEPNKEGDFV LRFFSEKSAG TVELDDQIQA NLPDEQVLSE 

       550        560        570        580        590        600 
EEIDENFKAL FRQLAGEDME ISVKELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD 

       610        620        630        640        650        660 
GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK LNKKLYELII 

       670        680        690        700        710 
TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV TFDLFKWLQL TMFA

P07384 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