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Caspase-4 (CASP-4) (EC 3.4.22.57) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]

 CASP4_BOVIN             Reviewed;         377 AA.
Q5E9C1;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 1.
28-FEB-2018, entry version 93.
RecName: Full=Caspase-4;
Short=CASP-4;
EC=3.4.22.57 {ECO:0000250|UniProtKB:P49662};
Contains:
RecName: Full=Caspase-4 subunit 1;
Contains:
RecName: Full=Caspase-4 subunit 2;
Flags: Precursor;
Name=CASP4;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Hypothalamus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Inflammatory caspase. Essential effector of NLRP3
inflammasome-dependent CASP1 activation and IL1B and IL18
secretion in response to non-canonical activators, such as UVB
radiation, cholera enterotoxin subunit B and cytosolic LPS.
Independently of NLRP3 inflammasome and CASP1, promotes
pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18
and HMGB1 release in response to non-canonical inflammasome
activators. Plays a crucial role in the restriction of Salmonella
typhimurium replication in colonic epithelial cells during
infection. In later stages of the infection, LPS from cytosolic
Salmonella triggers CASP4 activation, which ultimately results in
pyroptosis of infected cells and their extrusion into the gut
lumen, as well as in IL18 secretion. Pyroptosis limits bacterial
replication, while cytokine secretion promotes the recruitment and
activation of immune cells and triggers mucosal inflammation.
Involved in LPS-induced IL6 secretion; this activity may not
require caspase enzymatic activity. Involved in cell death induced
by endoplasmic reticulum stress. Activated by direct binding to
LPS without the need of an upstream sensor. Does not directly
process IL1B. During non-canonical inflammasome activation, cuts
CGAS and may play a role in the regulation of antiviral innate
immune activation (By similarity). {ECO:0000250|UniProtKB:P49662,
ECO:0000250|UniProtKB:P70343}.
-!- CATALYTIC ACTIVITY: Strict requirement for Asp at the P1 position.
It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but
also cleaves at Asp-Glu-Val-Asp-|-.
{ECO:0000250|UniProtKB:P49662}.
-!- ENZYME REGULATION: Activated by homooligomerization induced by
direct binding to cytosolic LPS, in a TLR4-independent manner.
{ECO:0000250|UniProtKB:P49662}.
-!- SUBUNIT: Upon direct LPS-binding, forms large homooligomers,
resulting in its activation. These oligomers are often referred to
as 'non-canonical inflammasomes' (By similarity). Active as a
heterotetramer consisting of two anti-parallel arranged
heterodimers, each one formed by a small and a large subunit (By
similarity). In its precursor form, interacts with TMEM214; this
interaction is required for association with the endoplasmic
reticulum membrane. Interacts with CASP1. Interacts with NOD2.
{ECO:0000250, ECO:0000250|UniProtKB:P49662}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P49662}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P49662}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P49662}; Cytoplasmic side
{ECO:0000250|UniProtKB:P49662}. Mitochondrion
{ECO:0000250|UniProtKB:P49662}. Inflammasome
{ECO:0000250|UniProtKB:P49662}. Secreted
{ECO:0000250|UniProtKB:P49662}. Note=Predominantly localizes to
the endoplasmic reticulum (ER). Association with the ER membrane
requires TMEM214. Released in the extracellular milieu by
keratinocytes following UVB irradiation.
{ECO:0000250|UniProtKB:P49662}.
-!- PTM: The two subunits are derived from the precursor sequence by
an autocatalytic mechanism or by cleavage by Caspase-8.
{ECO:0000250}.
-!- PTM: In response to activation signals, undergoes autoproteolytic
cleavage. {ECO:0000250|UniProtKB:P49662}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; BT020999; AAX09016.1; -; mRNA.
EMBL; BC112708; AAI12709.1; -; mRNA.
RefSeq; NP_788811.1; NM_176638.5.
UniGene; Bt.16018; -.
ProteinModelPortal; Q5E9C1; -.
SMR; Q5E9C1; -.
STRING; 9913.ENSBTAP00000027820; -.
PaxDb; Q5E9C1; -.
PRIDE; Q5E9C1; -.
Ensembl; ENSBTAT00000027820; ENSBTAP00000027820; ENSBTAG00000020884.
GeneID; 338039; -.
KEGG; bta:338039; -.
CTD; 837; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00910000144131; -.
HOGENOM; HOG000234399; -.
HOVERGEN; HBG076981; -.
KO; K04394; -.
OMA; FFNIDQI; -.
OrthoDB; EOG091G07NO; -.
Reactome; R-BTA-168638; NOD1/2 Signaling Pathway.
Proteomes; UP000009136; Chromosome 15.
Bgee; ENSBTAG00000020884; -.
ExpressionAtlas; Q5E9C1; baseline and differential.
GO; GO:0097169; C:AIM2 inflammasome complex; IBA:GO_Central.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072557; C:IPAF inflammasome complex; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0072559; C:NLRP3 inflammasome complex; IBA:GO_Central.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0070269; P:pyroptosis; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
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; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
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;
Complete proteome; Cytoplasm; Endoplasmic reticulum; Hydrolase;
Immunity; Inflammasome; Inflammatory response; Innate immunity;
Membrane; Mitochondrion; Necrosis; Phosphoprotein; Protease;
Reference proteome; Secreted; Thiol protease; Zymogen.
PROPEP 1 ?80 {ECO:0000255}.
/FTId=PRO_0000244735.
CHAIN ?81 270 Caspase-4 subunit 1.
/FTId=PRO_0000244736.
PROPEP 271 289 {ECO:0000255}.
/FTId=PRO_0000244737.
CHAIN 290 377 Caspase-4 subunit 2.
/FTId=PRO_0000244738.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
REGION 1 59 Required for LPS-binding.
{ECO:0000250|UniProtKB:P70343}.
ACT_SITE 210 210 {ECO:0000250}.
ACT_SITE 258 258 {ECO:0000250|UniProtKB:P49662}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000250|UniProtKB:P49662}.
SEQUENCE 377 AA; 43012 MW; 959A59424DAECBF4 CRC64;
MAEDKHNKNP LKMLESLGKE LISGLLDDFV EKNVLKLEEE EKKKIYDAKL QDKARVLVDS
IRQKNQEAGQ VFVQTFLNID KNSTSIKAPE ETVAGPDESV GSAATLKLCP HEEFLKLCKE
RAGEIYPIKE RKDRTRLALI ICNTEFDHMP PRNGAALDIL GMKQLLEGLG YTVEVEEKLT
ARDMESVLWK FAAREEHKSS DSTFLVFMSH GILDGICGTM HSEEEPDVLP YDTIFRTFNN
RNCLSLKDKP KVIIVQACRG ANRGELWVSD SPPALADSFS QSSENLEEDA VYKTHVEKDF
IAFCSSTPHN VSWRDIKKGS LFITRLITCF QKYAWCCHLE EVFRKVQQSF EKPNVKAQMP
TVERLSMTRY FYLFPGN


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