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Caspase-1 (CASP-1) (EC 3.4.22.36) (Interleukin-1 beta convertase) (IL-1BC) (Interleukin-1 beta-converting enzyme) (ICE) (IL-1 beta-converting enzyme) (p45) [Cleaved into: Caspase-1 subunit p20; Caspase-1 subunit p10]

 CASP1_RAT               Reviewed;         402 AA.
P43527;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
03-JUL-2019, entry version 149.
RecName: Full=Caspase-1;
Short=CASP-1;
EC=3.4.22.36;
AltName: Full=Interleukin-1 beta convertase;
Short=IL-1BC;
AltName: Full=Interleukin-1 beta-converting enzyme;
Short=ICE;
Short=IL-1 beta-converting enzyme;
AltName: Full=p45;
Contains:
RecName: Full=Caspase-1 subunit p20;
Contains:
RecName: Full=Caspase-1 subunit p10;
Flags: Precursor;
Name=Casp1; Synonyms=Il1bc, Il1bce;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=7780029; DOI=10.1006/cyto.1995.1014;
Keane K.M., Giegel D.A., Lipinski W.J., Callahan M.J., Shivers B.D.;
"Cloning, tissue expression and regulation of rat interleukin 1 beta
converting enzyme.";
Cytokine 7:105-110(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 228-362.
TISSUE=Ovary;
PubMed=7588240; DOI=10.1210/endo.136.11.7588240;
Flaws J.A., Kugu K., Trbovich A.M., Desanti A., Tilly K.I.,
Hirshfield A.N., Tilly J.L.;
"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.";
Endocrinology 136:5042-5053(1995).
-!- 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. Upon inflammasome
activation, during DNA virus infection but not RNA virus
challenge, controls antiviral immunity through the cleavage of
CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2
which is released from cells and remains enzymatically active
extracellularly (By similarity). {ECO:0000250|UniProtKB:P29452,
ECO:0000250|UniProtKB:P29466}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at position P1 and
has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.;
EC=3.4.22.36;
-!- SUBUNIT: 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 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. Both the p20 and p10
subunits interact with MEFV. Interacts with CARD17/INCA and
CARD18. Interacts with SERPINB1; this interaction regulates CASP1
activity. {ECO:0000250|UniProtKB:P29466}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29466}.
Cell membrane {ECO:0000250|UniProtKB:P29466}.
-!- PTM: The two subunits are derived from the precursor sequence by a
autocatalytic mechanism.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U14647; AAA85812.1; -; mRNA.
EMBL; U34621; AAC52259.1; -; mRNA.
EMBL; S79676; AAB35431.1; -; mRNA.
SMR; P43527; -.
DIP; DIP-29840N; -.
IntAct; P43527; 1.
STRING; 10116.ENSRNOP00000009993; -.
MEROPS; C14.001; -.
PhosphoSitePlus; P43527; -.
PaxDb; P43527; -.
PRIDE; P43527; -.
UCSC; RGD:2274; rat.
RGD; 2274; Casp1.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
HOGENOM; HOG000234399; -.
InParanoid; P43527; -.
PhylomeDB; P43527; -.
BRENDA; 3.4.22.36; 5301.
Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
Reactome; R-RNO-448706; Interleukin-1 processing.
PRO; PR:P43527; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0097169; C:AIM2 inflammasome complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0072557; C:IPAF inflammasome complex; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0072558; C:NLRP1 inflammasome complex; ISS:UniProtKB.
GO; GO:0072559; C:NLRP3 inflammasome complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0097110; F:scaffold protein binding; IPI:RGD.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEP:RGD.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0030324; P:lung development; IEP:RGD.
GO; GO:0007613; P:memory; IMP:RGD.
GO; GO:0001774; P:microglial cell activation; IMP:RGD.
GO; GO:0007494; P:midgut development; IEP:RGD.
GO; GO:0007520; P:myoblast fusion; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0046010; P:positive regulation of circadian sleep/wake cycle, non-REM sleep; IMP:RGD.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:RGD.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IMP:RGD.
GO; GO:0042493; P:response to drug; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IDA:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IDA:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
2: Evidence at transcript level;
Apoptosis; Cell membrane; Complete proteome; Cytoplasm; Hydrolase;
Membrane; Phosphoprotein; Protease; Reference proteome;
Thiol protease; Zymogen.
PROPEP 1 ?118 {ECO:0000255}.
/FTId=PRO_0000004533.
CHAIN ?119 296 Caspase-1 subunit p20.
/FTId=PRO_0000004534.
PROPEP 297 314 {ECO:0000255}.
/FTId=PRO_0000004535.
CHAIN 315 402 Caspase-1 subunit p10.
/FTId=PRO_0000004536.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 236 236 {ECO:0000250}.
ACT_SITE 284 284 {ECO:0000250}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000250|UniProtKB:P29452}.
CONFLICT 252 252 A -> G (in Ref. 2; AAC52259/AAB35431).
{ECO:0000305}.
CONFLICT 256 256 K -> E (in Ref. 2; AAC52259/AAB35431).
{ECO:0000305}.
CONFLICT 260 260 I -> L (in Ref. 2; AAC52259/AAB35431).
{ECO:0000305}.
CONFLICT 262 262 Q -> H (in Ref. 2; AAC52259/AAB35431).
{ECO:0000305}.
CONFLICT 343 343 R -> Q (in Ref. 2; AAC52259/AAB35431).
{ECO:0000305}.
SEQUENCE 402 AA; 45576 MW; D2E8FA2BEA76FD40 CRC64;
MADKVLRAKR KQFINSVSVG TINGLLDELL EKRVLNQEEM DTIKLANITV MEKARDLCDH
VTKKGPRASQ MFITYICNED CYLAEILELQ SGPSAETVFV TEDSKGGHPF SSETKEKLNK
EGGAFPGPSG SLKFCPLEIA QKLWKENHSE IYPIMKTPTR TRLALIICNT DFQHLSRRVG
ADVDLREMKL LLQDLGYTVK VKENLTALEM TKELKEFAAC PEHKTSDSTF LVFMSHGLQE
GICGITYSNE VADILKVDTI FQMMNTLKCP SLKDKPKVII IQACRGEKQG VVLLKDSVGN
SEEGFLTDAI FEDDGIKKAH IEKDFIAFCS STPDNVSWRH PVRGSLFIES LIKHMKEYAW
SCDLEDIFRK VRFSFEQPDS RLQMPTTERV TLTKRFYLFP GH


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