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Q9MZV6 (CASP1_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 85. 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
OrganismFelis catus (Cat) (Felis silvestris catus) [Reference proteome]
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraFeliformiaFelidaeFelinaeFelis

Protein attributes

Sequence length410 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_0000004513
Chain120 – 296177Caspase-1 subunit p20
PRO_0000004514
Propeptide297 – 32226 Potential
PRO_0000004515
Chain323 – 41088Caspase-1 subunit p10
PRO_0000004516

Regions

Domain1 – 9191CARD

Sites

Active site2351 By similarity
Active site2841 By similarity

Natural variations

Natural variant1361H → R.

Sequences

Sequence LengthMass (Da)Tools
Q9MZV6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2B8BB99C007A40C5

FASTA41046,052
        10         20         30         40         50         60 
MADKVLKGKR KQFINSVGMG TVNGLLDELF EKNVLNQEEM ERVKCENATV MDKARALIDS 

        70         80         90        100        110        120 
VLRKGPRACQ IFICHICEED THLAETLGLS SSPQSGNSQN TTDSEVAFPP LPASVNNMPG 

       130        140        150        160        170        180 
PAEPEESVDA LKLCPHENFV KLCKQRAEEI YPIKERKDRT RLALIICNTT FDHLSLRKGA 

       190        200        210        220        230        240 
DLDVAGMRRL LTDLGYSVHI KEELTAKDME SELRAFAARP EHKSSDSTFL VFMSHGILSG 

       250        260        270        280        290        300 
ICGTKYSAEG DPDVLAYDTI FQIFNNRNCL SLKDKPKVII VQACRGENLG ELLISDSPAA 

       310        320        330        340        350        360 
PMDSTSQMGS SLSQVGDNLE DDAIYKVHVE KDFIAFCSST PHHVSWRDVN KGSLFITQLI 

       370        380        390        400        410 
TCFQKYSWCF HLEEVFRKVQ QSFEKPNVRA QMPTIERLSM TRYFYLFPGH 

« Hide

References

[1]"Cloning and sequencing of feline and canine ice-related cDNAs encoding hybrid caspase-1/caspase-13-like propeptides."
Taylor S., Hanlon L., McGillivray C., Gault E.A., Argyle D.J., Onions D.E., Nicolson L.
DNA Seq. 10:387-394(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF135968 mRNA. Translation: AAF64389.1.
RefSeqNP_001009365.1. NM_001009365.1.

3D structure databases

ProteinModelPortalQ9MZV6.
SMRQ9MZV6. Positions 2-90, 149-296, 323-410.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493961.
KEGGfca:493961.

Organism-specific databases

CTD834.

Phylogenomic databases

HOVERGENHBG076981.
KOK01370.

Enzyme and pathway databases

BRENDA3.4.22.36. 2240.

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...

Entry information

Entry nameCASP1_FELCA
AccessionPrimary (citable) accession number: Q9MZV6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 85 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