[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1074/jbc.270.26.15870; PubMed=7797592 [NCBI, ExPASy, EBI, Israel, Japan] Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K., Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.; "Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases."; J. Biol. Chem. 270:15870-15876(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 55-418. TISSUE=Placenta, and Spleen; PubMed=8617266 [NCBI, ExPASy, EBI, Israel, Japan] Faucheu C., Blanchet A.-M., Collard-Dutilleul V., Lalanne J.-L., Diu-Hercend A.; "Identification of a cysteine protease closely related to interleukin-1 beta-converting enzyme."; Eur. J. Biochem. 236:207-213(1996).

Comments

FUNCTION: Mediator of programmed cell death (apoptosis).
CATALYTIC ACTIVITY: Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-.
SUBUNIT: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunits.
INTERACTION:
Q9C000:NLRP1; NbExp=1; IntAct=EBI-1246700, EBI-1220518;
TISSUE SPECIFICITY: Expressed in barely detectable amounts in most tissues except brain, highest levels being found in lung, liver and skeletal muscle.
PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism.
SIMILARITY: Belongs to the peptidase C14 family [view classification].
SIMILARITY: Contains 1 CARD domain.

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

U28015; AAA75172.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X94993; CAA64450.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B57511; B57511.

UniGene

Hs.213327

3D structure databases

HSSP

P29466; 1ICE. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P51878.

Protein-protein interaction databases

IntAct

P51878; -.

Protein family/group databases

MEROPS

C14.008; -.

Organism-specific databases

HGNC:1506; CASP5.

602665; gene. [NCBI / EBI]

PharmGKB

PA26089; -.

GeneCards

P51878.

Gene expression databases

ArrayExpress

P51878; -.

CleanEx

HS_CASP5; -.

GermOnline

ENSG00000137757; Homo sapiens.

Ontologies

GO:0008234;	Molecular function: cysteine-type peptidase activity (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006915;	Biological process: apoptosis (traceable author statement from ProtInc).
GO:0006508;	Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001315; CARD.
IPR017350; Caspase_IL-1_beta.
IPR011029; DEATH_like.
IPR011600; Pept_C14_cat.
IPR001309; Pept_C14_ICE_p20.
IPR016129; Pept_C14_ICE_p20_AS.
IPR002138; Pept_C14_p10.
IPR002398; Pept_C14_p45.
IPR015917; Pept_C14_p45_core.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.533.10; DEATH_like; 1.

PANTHER

PTHR10454; Pept_C14_p45; 1.

Pfam

PF00619; CARD; 1.
PF00656; Peptidase_C14; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF038001; Caspase_ICE; 1.

PRINTS

PR00376; IL1BCENZYME.

SMART

SM00114; CARD; 1.
SM00115; CASc; 1.
SMART graphical view of domain structure.

PROSITE

PS50209; CARD; 1.
PS01122; CASPASE_CYS; 1.
PS01121; CASPASE_HIS; 1.
PS50207; CASPASE_P10; 1.
PS50208; CASPASE_P20; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P51878.

Genome annotation databases

Ensembl

ENSG00000137757; Homo sapiens. [Contig view]

Phylogenomic databases

HOVERGEN

P51878; -.

Other

P51878; -.

CASP5; Homo sapiens.

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

Keywords

Apoptosis; Hydrolase; Polymorphism; Protease; Thiol protease; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`PROPEP`	`1 120`	`120`	`Potential.`	`PRO_0000004604`
`CHAIN`	`121 311`	`191`	`Caspase-5 subunit p20.`	`PRO_0000004605`
`PROPEP`	`312 330`	`19`	`Potential.`	`PRO_0000004606`
`CHAIN`	`331 418`	`88`	`Caspase-5 subunit p10.`	`PRO_0000004607`
`DOMAIN`	`40 132`	`93`	`CARD.`
`ACT_SITE`	`251 251`		`By similarity.`
`ACT_SITE`	`299 299`
`VARIANT`	`13 13`	`1`	`F -> L (in dbSNP:rs3181320 [NCBI]).`	`VAR_024403`
`VARIANT`	`152 152`	`1`	`R -> H (in dbSNP:rs3181179 [NCBI]).`	`VAR_024404`
`VARIANT`	`201 201`	`1`	`V -> L (in dbSNP:rs3181326 [NCBI]).`	`VAR_024405`
`MUTAGEN`	`299 299`		`C->S: Loss of activity.`
`CONFLICT`	`318 318`		`V -> L (in Ref. 2; CAA64450).`

Sequence information

Length: 418 AA [This is the length of the unprocessed precursor]

Molecular weight: 47814 Da [This is the MW of the unprocessed precursor]

CRC64: 69B0922FE235126C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFKGILQSGL DNFVINHMLK NNVAGQTSIQ TLVPNTDQKS TSVKKDNHKK KTVKMLEYLG 

        70         80         90        100        110        120 
KDVLHGVFNY LAKHDVLTLK EEEKKKYYDA KIEDKALILV DSLRKNRVAH QMFTQTLLNM 

       130        140        150        160        170        180 
DQKITSVKPL LQIEAGPPES AESTNILKLC PREEFLRLCK KNHDEIYPIK KREDRRRLAL 

       190        200        210        220        230        240 
IICNTKFDHL PARNGAHYDI VGMKRLLQGL GYTVVDEKNL TARDMESVLR AFAARPEHKS 

       250        260        270        280        290        300 
SDSTFLVLMS HGILEGICGT AHKKKKPDVL LYDTIFQIFN NRNCLSLKDK PKVIIVQACR 

       310        320        330        340        350        360 
GEKHGELWVR DSPASLAVIS SQSSENLEAD SVCKIHEEKD FIAFCSSTPH NVSWRDRTRG 

       370        380        390        400        410 
SIFITELITC FQKYSCCCHL MEIFRKVQKS FEVPQAKAQM PTIERATLTR DFYLFPGN

P51878 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