Reviewed, UniProtKB/Swiss-Prot Q9N2I1 (CASP1_PIG)

Names and origin

Protein names

Recommended 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=IL-1 beta-converting enzyme
      Short name=ICE
    p45
Cleaved into the following 2 chains:
    1- Recommended name:
            Caspase-1 subunit p20
    2- Recommended name:
            Caspase-1 subunit p10

Gene names

Name:	CASP1
Synonyms:	IL1BC

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	404 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 which then 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. 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.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm
Molecular function	Hydrolase Protease Thiol protease
PTM	Zymogen
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro regulation of apoptosis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 119	119	Potential		PRO_0000004529
	Chain	120 – 297	178	Caspase-1 subunit p20		PRO_0000004530
	Propeptide	298 – 316	19	Potential		PRO_0000004531
	Chain	317 – 404	88	Caspase-1 subunit p10		PRO_0000004532
Regions
	Domain	1 – 91	91	CARD
Sites
	Active site	237	1	By similarity
	Active site	285	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9N2I1-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 437DC787E85FB449	FASTA	404	44,882
	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

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: 10574622] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB027296 mRNA. Translation: BAA89531.1.
RefSeq	NP_999327.1.
UniGene	Ssc.16012
3D structure databases
HSSP	HSSP built from PDB template 1ICE based on UniProtKB P29466.
SMR	Q9N2I1. Positions 120-297, 317-404.
ModBase	Search...
Protein family/group databases
MEROPS	C14.001.
Genome annotation databases
GeneID	397319.
KEGG	ssc:397319.
Organism-specific databases
CTD	397319.
Phylogenomic databases
HOVERGEN	Q9N2I1.
Enzyme and pathway databases
BRENDA	3.4.22.36. 249.
Family and domain databases
InterPro	IPR001315. CARD. IPR017350. Caspase_IL-1_beta. IPR011029. DEATH-like. IPR011600. Pept_C14_cat. IPR001309. Pept_C14_ICE_p20. IPR016129. Pept_C14_ICE_p20_AS. IPR002138. Pept_C14_p10. IPR002398. Pept_C14_p45. IPR015917. Pept_C14_p45_core. [Graphical view]
Gene3D	G3DSA:1.10.533.10. DEATH_like. 1 hit.
PANTHER	PTHR10454. Pept_C14_p45. 1 hit.
Pfam	PF00619. CARD. 1 hit. PF00656. Peptidase_C14. 1 hit. [Graphical view]
PIRSF	PIRSF038001. Caspase_ICE. 1 hit.
PRINTS	PR00376. IL1BCENZYME.
SMART	SM00114. CARD. 1 hit. SM00115. CASc. 1 hit. [Graphical view]
PROSITE	PS50209. 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]
ProtoNet	Search...

Entry information

Entry name

CASP1_PIG

Accession

Primary (citable) accession number: Q9N2I1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 5, 2001
Last sequence update:	October 1, 2000
Last modified:	September 1, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)