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Q9TV13 (CASP1_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 95. 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
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

Protein attributes

Sequence length405 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_0000004517
Chain120 – 298179Caspase-1 subunit p20
PRO_0000004518
Propeptide299 – 31719 Potential
PRO_0000004519
Chain318 – 40588Caspase-1 subunit p10
PRO_0000004520

Regions

Domain1 – 9191CARD

Sites

Active site2381 By similarity
Active site2861 By similarity

Natural variations

Natural variant2031V → L.
Natural variant3051N → S.

Sequences

Sequence LengthMass (Da)Tools
Q9TV13 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 7CE8729BB359CC17

FASTA40545,331
        10         20         30         40         50         60 
MADKVLKEKR RLFIRSVGTG TVNSLLDELL EKRVLNQEEM EKVRDENATV MDKARALIDA 

        70         80         90        100        110        120 
VIRKGPQACQ IFIGHICEDD PHLAETLRLS SGPQSGNFLK TQDSQAVVHS SPALQAMPDD 

       130        140        150        160        170        180 
LAKLALSGPK VSLKLCSPEV VERIWKEKSA EMYPIMGKSM TRTRLALIIC NTEFDNLSRR 

       190        200        210        220        230        240 
AGAEVDIASM KVLLEGLGYS VEVKENLTAL DMTTELKAFA ARPEHRSSDS TFLVFMSHGI 

       250        260        270        280        290        300 
REGICGKKFS EKVPDVLEVN TIFQIFNTRN CPNLRDKPKV IIIQACRGEN QGVVWLKDST 

       310        320        330        340        350        360 
GTSGNSSSLA PDDFEDDAIK KAHVEKDFIA FCSSTPDTVS WRSPTTGSVF IEKLIENLQE 

       370        380        390        400 
YAWSCDLEEI FRKVRLSFEL PDARAQMPTA ERVTLTRRFY LFPGH 

« Hide

References

[1]"Nucleotide sequence of equine caspase-1 cDNA."
Wardlow S., Penha-Goncalves M.N., Argyle D.J., Onions D.E., Nicolson L.
DNA Seq. 10:133-137(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090119 mRNA. Translation: AAD46400.1.
RefSeqNP_001075311.1. NM_001081842.1.
UniGeneEca.13025.

3D structure databases

ProteinModelPortalQ9TV13.
SMRQ9TV13. Positions 2-89, 127-298, 318-405.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9TV13.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100033888.
KEGGecb:100033888.

Organism-specific databases

CTD834.

Phylogenomic databases

eggNOGNOG326166.
HOGENOMHOG000234399.
HOVERGENHBG076981.
InParanoidQ9TV13.
KOK01370.

Enzyme and pathway databases

BRENDA3.4.22.36. 2120.

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_HORSE
AccessionPrimary (citable) accession number: Q9TV13
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 95 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