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P43527 (CASP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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, Il1bce
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 bya 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. Interacts with CARD17/INCA and CARD18 By similarity.

Subcellular location

Cytoplasm.

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_processapoptotic process

Inferred from expression pattern PubMed 11404793. Source: RGD

execution phase of apoptosis

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung development

Inferred from expression pattern PubMed 12396474. Source: RGD

memory

Inferred from mutant phenotype PubMed 16197515. Source: RGD

microglial cell activation

Inferred from mutant phenotype PubMed 15149850. Source: RGD

midgut development

Inferred from expression pattern PubMed 12396474. Source: RGD

myoblast fusion

Inferred from mutant phenotype PubMed 12832042. Source: RGD

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 15663890. Source: RGD

positive regulation of circadian sleep/wake cycle, non-REM sleep

Inferred from mutant phenotype PubMed 16455762. Source: RGD

positive regulation of cytokine secretion

Inferred from mutant phenotype PubMed 17384935. Source: RGD

positive regulation of interleukin-1 beta secretion

Inferred from mutant phenotype PubMed 16942597. Source: RGD

regulation of inflammatory response

Inferred from Biological aspect of Ancestor. Source: RefGenome

response to drug

Inferred from direct assay PubMed 16165281. Source: RGD

response to hypoxia

Inferred from direct assay PubMed 12829320. Source: RGD

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 17384935. Source: RGD

response to organic cyclic compound

Inferred from direct assay PubMed 17561093. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 20638366. Source: RGD

   Cellular_componentAIM2 inflammasome complex

Inferred from sequence or structural similarity. Source: UniProtKB

IPAF inflammasome complex

Inferred from sequence or structural similarity. 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

Inferred from direct assay PubMed 18367607PubMed 19401709. Source: RGD

neuron projection

Inferred from direct assay PubMed 19401709. Source: RGD

nucleus

Inferred from direct assay PubMed 18367607. Source: RGD

protein complex

Inferred from direct assay PubMed 19416975. Source: RGD

   Molecular_functioncysteine-type endopeptidase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 18367607PubMed 19416975. Source: RGD

scaffold protein binding

Inferred from physical interaction PubMed 19416975. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – ?118118 Potential
PRO_0000004533
Chain?119 – 296178Caspase-1 subunit p20
PRO_0000004534
Propeptide297 – 31418 Potential
PRO_0000004535
Chain315 – 40288Caspase-1 subunit p10
PRO_0000004536

Regions

Domain1 – 9191CARD

Sites

Active site2361 By similarity
Active site2841 By similarity

Experimental info

Sequence conflict2521A → G in AAC52259. Ref.2
Sequence conflict2521A → G in AAB35431. Ref.2
Sequence conflict2561K → E in AAC52259. Ref.2
Sequence conflict2561K → E in AAB35431. Ref.2
Sequence conflict2601I → L in AAC52259. Ref.2
Sequence conflict2601I → L in AAB35431. Ref.2
Sequence conflict2621Q → H in AAC52259. Ref.2
Sequence conflict2621Q → H in AAB35431. Ref.2
Sequence conflict3431R → Q in AAC52259. Ref.2
Sequence conflict3431R → Q in AAB35431. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P43527 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: D2E8FA2BEA76FD40

FASTA40245,576
        10         20         30         40         50         60 
MADKVLRAKR KQFINSVSVG TINGLLDELL EKRVLNQEEM DTIKLANITV MEKARDLCDH 

        70         80         90        100        110        120 
VTKKGPRASQ MFITYICNED CYLAEILELQ SGPSAETVFV TEDSKGGHPF SSETKEKLNK 

       130        140        150        160        170        180 
EGGAFPGPSG SLKFCPLEIA QKLWKENHSE IYPIMKTPTR TRLALIICNT DFQHLSRRVG 

       190        200        210        220        230        240 
ADVDLREMKL LLQDLGYTVK VKENLTALEM TKELKEFAAC PEHKTSDSTF LVFMSHGLQE 

       250        260        270        280        290        300 
GICGITYSNE VADILKVDTI FQMMNTLKCP SLKDKPKVII IQACRGEKQG VVLLKDSVGN 

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

       370        380        390        400 
SCDLEDIFRK VRFSFEQPDS RLQMPTTERV TLTKRFYLFP GH 

« Hide

References

[1]"Cloning, tissue expression and regulation of rat interleukin 1 beta converting enzyme."
Keane K.M., Giegel D.A., Lipinski W.J., Callahan M.J., Shivers B.D.
Cytokine 7:105-110(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Spleen.
[2]"Interleukin-1 beta-converting enzyme-related proteases (IRPs) and mammalian cell death: dissociation of IRP-induced oligonucleosomal endonuclease activity from morphological apoptosis in granulosa cells of the ovarian follicle."
Flaws J.A., Kugu K., Trbovich A.M., Desanti A., Tilly K.I., Hirshfield A.N., Tilly J.L.
Endocrinology 136:5042-5053(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 228-362.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14647 mRNA. Translation: AAA85812.1.
U34621 mRNA. Translation: AAC52259.1.
S79676 mRNA. Translation: AAB35431.1.
UniGeneRn.37508.

3D structure databases

ProteinModelPortalP43527.
SMRP43527. Positions 2-90, 127-296, 315-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29840N.
STRING10116.ENSRNOP00000009993.

Protein family/group databases

MEROPSC14.001.

Proteomic databases

PaxDbP43527.
PRIDEP43527.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:2274. rat.

Organism-specific databases

RGD2274. Casp1.

Phylogenomic databases

eggNOGNOG326166.
HOGENOMHOG000234399.
HOVERGENHBG076981.
InParanoidP43527.
PhylomeDBP43527.

Enzyme and pathway databases

BRENDA3.4.22.36. 5301.

Gene expression databases

GenevestigatorP43527.

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

PROP43527.

Entry information

Entry nameCASP1_RAT
AccessionPrimary (citable) accession number: P43527
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 11, 2014
This is version 114 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