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P29452 (CASP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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

Cleaved into the following 2 chains:

  1. Caspase-1 subunit p20
  2. Caspase-1 subunit p10
Gene names
Name:Casp1
Synonyms:Il1bc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 whichthen 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. Both the p20 and p10 subunits interact with MEFV By similarity. 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 processApoptosis
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from direct assay. Source: MGI

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to organic substance

Inferred from sequence orthology PubMed 19158679. Source: MGI

execution phase of apoptosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

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 signaling

Inferred from direct assay PubMed 16585594. Source: UniProtKB

positive regulation of cytokine secretion

Inferred from mutant phenotype PubMed 18490713. Source: MGI

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 11016935PubMed 15190255. Source: MGI

pyroptosis

Inferred from mutant phenotype PubMed 22002608. Source: MGI

regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

regulation of inflammatory response

Inferred from mutant phenotype PubMed 22297845. Source: MGI

response to ATP

Inferred from mutant phenotype PubMed 18490713. Source: MGI

response to hypoxia

Inferred from mutant phenotype PubMed 14663141. Source: MGI

response to lipopolysaccharide

Inferred from direct assay PubMed 16301672. Source: MGI

   Cellular_componentAIM2 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

cytoplasm

Traceable author statement PubMed 15190255. Source: MGI

cytosol

Traceable author statement. Source: Reactome

extracellular region

Inferred from direct assay PubMed 15190255. Source: MGI

   Molecular_functioncysteine-type endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

peptidase activity

Inferred from direct assay PubMed 18490713. Source: MGI

protein binding

Inferred from physical interaction PubMed 10051653PubMed 8670890. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ipaBP180113EBI-489700,EBI-490239From a different organism.
sipBQ561342EBI-489700,EBI-489689From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – ?118118 Potential
PRO_0000004525
Chain?119 – 296178Caspase-1 subunit p20
PRO_0000004526
Propeptide297 – 31418 Potential
PRO_0000004527
Chain315 – 40288Caspase-1 subunit p10
PRO_0000004528

Regions

Domain1 – 9191CARD

Sites

Active site2361 By similarity
Active site2841 By similarity

Experimental info

Sequence conflict3 – 64DKIL → V in AAA56992. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P29452 [UniParc].

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

FASTA40245,640
        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' 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.
CCDSCCDS22798.1.
PIRA46495.
RefSeqNP_033937.2. NM_009807.2.
UniGeneMm.1051.

3D structure databases

ProteinModelPortalP29452.
SMRP29452. Positions 2-90, 127-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-34659N.
IntActP29452. 2 interactions.
STRING10090.ENSMUSP00000027015.

Chemistry

BindingDBP29452.
ChEMBLCHEMBL4800.

Protein family/group databases

MEROPSC14.001.

PTM databases

PhosphoSiteP29452.

Proteomic databases

MaxQBP29452.
PaxDbP29452.
PRIDEP29452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027015; ENSMUSP00000027015; ENSMUSG00000025888.
GeneID12362.
KEGGmmu:12362.
UCSCuc009obr.1. mouse.

Organism-specific databases

CTD834.
MGIMGI:96544. Casp1.

Phylogenomic databases

eggNOGNOG326166.
GeneTreeENSGT00700000104134.
HOGENOMHOG000234399.
HOVERGENHBG076981.
InParanoidP29452.
KOK01370.
OMAKSAEIYP.
OrthoDBEOG7FXZZ6.
PhylomeDBP29452.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.36. 3474.

Gene expression databases

BgeeP29452.
CleanExMM_CASP1.
GenevestigatorP29452.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
3.40.50.1460. 1 hit.
InterProIPR001315. CARD.
IPR029030. Caspase-like_dom.
IPR017350. Caspase_ICE-type.
IPR011029. DEATH-like_dom.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
PfamPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PIRSFPIRSF038001. Caspase_ICE. 1 hit.
PRINTSPR00376. IL1BCENZYME.
SMARTSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50209. 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]
ProtoNetSearch...

Other

NextBio281032.
PROP29452.
SOURCESearch...

Entry information

Entry nameCASP1_MOUSE
AccessionPrimary (citable) accession number: P29452
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

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