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Q9N2I1 (CASP1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 82. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length404 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 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 p10 and p20 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 an autocatalytic mechanism.

Sequence similarities

Belongs to the peptidase C14A family.

Contains 1 CARD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 119119 Potential
PRO_0000004529
Chain120 – 297178Caspase-1 subunit p20
PRO_0000004530
Propeptide298 – 31619 Potential
PRO_0000004531
Chain317 – 40488Caspase-1 subunit p10
PRO_0000004532

Regions

Domain1 – 9191CARD

Sites

Active site2371 By similarity
Active site2851 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9N2I1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 437DC787E85FB449

FASTA40444,882
        10         20         30         40         50         60 
MADKVLKEKR RLFVRSVAMG TINGLLDELL ETRVLNQEEV EIVRGENATV MDKARALIDS 

        70         80         90        100        110        120 
VIRKGPQACQ ICINHICGDD PHLAGVLELS TGSQSGKCLT VQESQAVVPP FPAPQTVQDN 

       130        140        150        160        170        180 
PVKPASSEPR GSLKLCPPDI AQRLWKEKSA EIYPIMGKSI RTRLALIICN TEFENLPRRD 

       190        200        210        220        230        240 
GADVDIRDMK ILLEDLGYSV DVRENLTASD MAIELKAFAA RPEHKSSDST FLVLMSHGIQ 

       250        260        270        280        290        300 
AGICGKKYSE EVPDVLEVNT VFQILNTLNC PSLKDKPKVI IIQACRGEKQ GVVWIKDSVG 

       310        320        330        340        350        360 
PSGNSSLLAA EDFEYDAIKK AHIEKDFIAF CSSTPDNVSW RHPLLGSLFI IKLIKILQEH 

       370        380        390        400 
AWSCGLEEIF RKVRFSFELA DGRAQMPTAE RVTLTRSFYL FPGH 

« Hide

References

[1]"Molecular cloning of porcine interleukin-1beta converting enzyme and differential gene expression of IL-1beta converting enzyme, IL-1beta, and IL-18 in porcine alveolar macrophages."
Muneta Y., Shimoji Y., Yokomizo Y., Mori Y.
J. Interferon Cytokine Res. 19:1289-1296(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB027296 mRNA. Translation: BAA89531.1.
RefSeqNP_999327.1. NM_214162.1.
UniGeneSsc.16012.

3D structure databases

ProteinModelPortalQ9N2I1.
SMRQ9N2I1. Positions 2-89, 120-297, 317-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000015922.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397319.
KEGGssc:397319.

Organism-specific databases

CTD834.

Phylogenomic databases

eggNOGNOG326166.
HOVERGENHBG076981.
KOK01370.

Enzyme and pathway databases

BRENDA3.4.22.36. 6170.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
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...

Entry information

Entry nameCASP1_PIG
AccessionPrimary (citable) accession number: Q9N2I1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 82 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