Caspase-1 precursor - Mus musculus (Mouse)

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P29452 (CASP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 130. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Caspase-1
Short name=CASP-1
EC=3.4.22.36

Alternative name(s):
Interleukin-1 beta convertase
Short name=IL-1BC
Interleukin-1 beta-converting enzyme
Short name=ICE
Short name=IL-1 beta-converting enzyme
p45

Gene names

Name:	Casp1
Synonyms:	Il1bc

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	402 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Can also promote apoptosis.
Catalytic activity	Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-\|-.
Subunit structure	Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunit. The p20 subunit can also form a heterodimer with the epsilon isoform which then has an inhibitory effect. May be a component of the inflammasome, a protein complex which also includes PYCARD, CARD8 and NALP2 and whose function would be the activation of proinflammatory caspases. Interacts with CARD17/INCA and CARD18 By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	High level expression seen in spleen and lung, low level expression seen in brain, heart, liver, kidney, testis and skeletal muscle.
Post-translational modification	The two subunits are derived from the precursor sequence by a autocatalytic mechanism.
Sequence similarities	Belongs to the peptidase C14A family. Contains 1 CARD domain.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
PTM	Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell death Inferred from direct assay PubMed 16429160. Source: MGI cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara cellular response to organic substance Inferred from sequence orthology PubMed 19158679. Source: MGI induction of apoptosis Inferred from direct assay PubMed 15190255. Source: MGI interleukin-1 beta production Inferred from genetic interaction PubMed 19158679. Source: MGI membrane hyperpolarization Inferred from mutant phenotype PubMed 23028046. Source: MGI mitochondrial depolarization Inferred from mutant phenotype PubMed 23028046. Source: MGI positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 16585594. Source: UniProtKB positive regulation of interleukin-1 alpha secretion Inferred from mutant phenotype PubMed 18490713. Source: MGI positive regulation of interleukin-1 beta secretion Inferred from mutant phenotype PubMed 18490713. Source: MGI protein processing Inferred from direct assay PubMed 11016935 PubMed 15190255. Source: MGI proteolysis Inferred from electronic annotation. Source: UniProtKB-KW response to ATP Inferred from mutant phenotype PubMed 18490713. Source: MGI response to hypoxia Inferred from mutant phenotype PubMed 14663141. Source: MGI
Cellular_component	AIM2 inflammasome complex Inferred from sequence or structural similarity. Source: UniProtKB IPAF inflammasome complex Inferred from direct assay PubMed 21874021. Source: UniProtKB NLRP1 inflammasome complex Inferred from sequence or structural similarity. Source: UniProtKB NLRP3 inflammasome complex Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome extracellular region Inferred from direct assay PubMed 15190255. Source: MGI
Molecular_function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro peptidase activity Inferred from direct assay PubMed 18490713. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ipaB	P18011	3	EBI-489700,EBI-490239	From a different organism.
sipB	Q56134	2	EBI-489700,EBI-489689	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – ?118

118

Potential

PRO_0000004525

Chain

?119 – 296

178

Caspase-1 subunit p20

PRO_0000004526

Propeptide

297 – 314

Potential

PRO_0000004527

Chain

315 – 402

Caspase-1 subunit p10

PRO_0000004528

Regions

Domain

1 – 91

CARD

Sites

Active site

236

By similarity

Active site

284

By similarity

Experimental info

Sequence conflict

3 – 6

DKIL → V in AAA56992. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P29452 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 3BEBCEFA67C69B03
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FASTA

402

45,640

        10         20         30         40         50         60 
MADKILRAKR KQFINSVSIG TINGLLDELL EKRVLNQEEM DKIKLANITA MDKARDLCDH 

        70         80         90        100        110        120 
VSKKGPQASQ IFITYICNED CYLAGILELQ SAPSAETFVA TEDSKGGHPS SSETKEEQNK 

       130        140        150        160        170        180 
EDGTFPGLTG TLKFCPLEKA QKLWKENPSE IYPIMNTTTR TRLALIICNT EFQHLSPRVG 

       190        200        210        220        230        240 
AQVDLREMKL LLEDLGYTVK VKENLTALEM VKEVKEFAAC PEHKTSDSTF LVFMSHGIQE 

       250        260        270        280        290        300 
GICGTTYSNE VSDILKVDTI FQMMNTLKCP SLKDKPKVII IQACRGEKQG VVLLKDSVRD 

       310        320        330        340        350        360 
SEEDFLTDAI FEDDGIKKAH IEKDFIAFCS STPDNVSWRH PVRGSLFIES LIKHMKEYAW 

       370        380        390        400 
SCDLEDIFRK VRFSFEQPEF RLQMPTADRV TLTKRFYLFP GH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the murine IL-1 beta converting enzyme cDNA." Nett-Fiordalisi M.A., Cerretti D.P., Berson D.R., Gilbert D.J., Jenkins N.A., Copeland N.G., Black R.A., Chaplin D.D. J. Immunol. 149:3254-3259(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Interleukin 1 beta (IL-1 beta) processing in murine macrophages requires a structurally conserved homologue of human IL-1 beta converting enzyme." Molineaux S.M., Casano F.J., Rolando A.M., Peterson E.P., Limjuco G., Chin J., Griffin P.R., Calaycay J.R., Ding G.J.-F., Yamin T.-T., Palyha O.C., Luell S., Fletcher D., Miller D.K., Howard A.D., Thornberry N.A., Kostura M.J. Proc. Natl. Acad. Sci. U.S.A. 90:1809-1813(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The structure and complete nucleotide sequence of the murine gene encoding interleukin-1 beta converting enzyme (ICE)." Casano F.J., Rolando A.M., Mudgett J.S., Molineaux S.M. Genomics 20:474-481(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[5]	"Characterization of seven murine caspase family members." van de Craen M., Vandenabeele P., Declercq W., van den Brande I., van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R., Fiers W. FEBS Lett. 403:61-69(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION. Strain: C3H/An.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L03799 mRNA. Translation: AAA39306.1. L28095 mRNA. Translation: AAA20209.1. U04269 Genomic DNA. Translation: AAA56992.1. BC008152 mRNA. Translation: AAH08152.1.
IPI	IPI00125676.
PIR	A46495.
RefSeq	NP_033937.2. NM_009807.2.
UniGene	Mm.1051.
3D structure databases
ProteinModelPortal	P29452.
SMR	P29452. Positions 2-90, 127-402.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34659N.
IntAct	P29452. 2 interactions.
STRING	10090.ENSMUSP00000027015.
Protein family/group databases
MEROPS	C14.001.
PTM databases
PhosphoSite	P29452.
Proteomic databases
PaxDb	P29452.
PRIDE	P29452.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000027015; ENSMUSP00000027015; ENSMUSG00000025888.
GeneID	12362.
KEGG	mmu:12362.
UCSC	uc009obr.1. mouse.
Organism-specific databases
CTD	834.
MGI	MGI:96544. Casp1.
Phylogenomic databases
eggNOG	NOG326166.
GeneTree	ENSGT00700000104134.
HOGENOM	HOG000234399.
HOVERGEN	HBG076981.
InParanoid	P29452.
KO	K01370.
OMA	KSAEIYP.
OrthoDB	EOG49W2FS.
Enzyme and pathway databases
BRENDA	3.4.22.36. 3474.
Reactome	REACT_107772. Immune System.
Gene expression databases
Bgee	P29452.
CleanEx	MM_CASP1.
Genevestigator	P29452.
GermOnline	ENSMUSG00000025888. Mus musculus.
Family and domain databases
Gene3D	1.10.533.10. 1 hit.
InterPro	IPR001315. CARD. IPR017350. Caspase_IL-1_beta. IPR011029. DEATH-like_dom. 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]
PANTHER	PTHR10454. PTHR10454. 1 hit.
Pfam	PF00619. CARD. 1 hit. PF00656. Peptidase_C14. 1 hit. [Graphical view]
PIRSF	PIRSF038001. Caspase_ICE. 1 hit.
PRINTS	PR00376. IL1BCENZYME.
SMART	SM00114. CARD. 1 hit. SM00115. CASc. 1 hit. [Graphical view]
SUPFAM	SSF47986. DEATH_like. 1 hit.
PROSITE	PS50209. CARD. 1 hit. PS01122. CASPASE_CYS. 1 hit. PS01121. CASPASE_HIS. 1 hit. PS50207. CASPASE_P10. 1 hit. PS50208. CASPASE_P20. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P29452.
ChEMBL	CHEMBL4800.
NextBio	281032.
SOURCE	Search...

Entry information

Entry name

CASP1_MOUSE

Accession

Primary (citable) accession number: P29452

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 29, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents