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Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]

 CASP4_MOUSE             Reviewed;         373 AA.
P70343; C6L648; O08735; Q3TAF3; Q6P8H1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
13-FEB-2019, entry version 167.
RecName: Full=Caspase-4;
Short=CASP-4;
EC=3.4.22.64 {ECO:0000250|UniProtKB:P49662};
AltName: Full=Caspase-11;
Short=CASP-11;
AltName: Full=Protease ICH-3 {ECO:0000303|PubMed:8702803};
Contains:
RecName: Full=Caspase-4 subunit p10;
Contains:
RecName: Full=Caspase-4 subunit p20;
Flags: Precursor;
Name=Casp4; Synonyms=Casp11, Caspl, Ich3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION BY LPS,
AND TISSUE SPECIFICITY.
STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
PubMed=8702803; DOI=10.1074/jbc.271.34.20580;
Wang S., Miura M., Jung Y.-K., Zhu H., Gagliardini V., Shi L.,
Greenberg A.H., Yuan J.;
"Identification and characterization of Ich-3, a member of the
interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream
regulator of ICE.";
J. Biol. Chem. 271:20580-20587(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
STRAIN=C3H/An; TISSUE=Fibrosarcoma;
PubMed=9038361; DOI=10.1016/S0014-5793(97)00026-4;
van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
Fiers W.;
"Characterization of seven murine caspase family members.";
FEBS Lett. 403:61-69(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
STRAIN=C57BL/6J;
Endo M., Nakayama Y., Mori M., Oike Y., Gotoh T.;
"ER stress-mediated caspase-11 induction is regulated with alternative
splicing.";
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INDUCTION BY LPS.
PubMed=10986288; DOI=10.1074/jbc.M007255200;
Lin X.Y., Choi M.S., Porter A.G.;
"Expression analysis of the human caspase-1 subfamily reveals specific
regulation of the CASP5 gene by lipopolysaccharide and interferon-
gamma.";
J. Biol. Chem. 275:39920-39926(2000).
[9]
INDUCTION BY LPS AND ER STRESS, AND SUBCELLULAR LOCATION.
PubMed=16670335; DOI=10.4049/jimmunol.176.10.6245;
Endo M., Mori M., Akira S., Gotoh T.;
"C/EBP homologous protein (CHOP) is crucial for the induction of
caspase-11 and the pathogenesis of lipopolysaccharide-induced
inflammation.";
J. Immunol. 176:6245-6253(2006).
[10]
FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY LPS AND LIVE E.COLI,
STRAIN-SPECIFIC VARIANT, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF
CYS-254.
PubMed=22002608; DOI=10.1038/nature10558;
Kayagaki N., Warming S., Lamkanfi M., Vande Walle L., Louie S.,
Dong J., Newton K., Qu Y., Liu J., Heldens S., Zhang J., Lee W.P.,
Roose-Girma M., Dixit V.M.;
"Non-canonical inflammasome activation targets caspase-11.";
Nature 479:117-121(2011).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND PROTEOLYTIC CLEAVAGE.
PubMed=25121752; DOI=10.1016/j.chom.2014.07.002;
Knodler L.A., Crowley S.M., Sham H.P., Yang H., Wrande M., Ma C.,
Ernst R.K., Steele-Mortimer O., Celli J., Vallance B.A.;
"Noncanonical inflammasome activation of caspase-4/caspase-11 mediates
epithelial defenses against enteric bacterial pathogens.";
Cell Host Microbe 16:249-256(2014).
[12]
FUNCTION, ACTIVITY REGULATION, OLIGOMERIZATION, INTERACTION WITH LPS,
DOMAIN, AND MUTAGENESIS OF LYS-19; LYS-38; GLU-40; LYS-53; ARG-54;
TRP-55; LYS-62; LYS-63; LYS-64 AND CYS-254.
PubMed=25119034; DOI=10.1038/nature13683;
Shi J., Zhao Y., Wang Y., Gao W., Ding J., Li P., Hu L., Shao F.;
"Inflammatory caspases are innate immune receptors for intracellular
LPS.";
Nature 514:187-192(2014).
[13]
DISRUPTION PHENOTYPE, AND INDUCTION BY POLY(I:C).
PubMed=26320999; DOI=10.1016/j.chom.2015.07.016;
Aachoui Y., Kajiwara Y., Leaf I.A., Mao D., Ting J.P., Coers J.,
Aderem A., Buxbaum J.D., Miao E.A.;
"Canonical inflammasomes drive IFN-gamma to prime caspase-11 in
defense against a cytosol-invasive bacterium.";
Cell Host Microbe 18:320-332(2015).
[14]
FUNCTION, AND GSDMD CLEAVAGE.
PubMed=26375003; DOI=10.1038/nature15514;
Shi J., Zhao Y., Wang K., Shi X., Wang Y., Huang H., Zhuang Y.,
Cai T., Wang F., Shao F.;
"Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell
death.";
Nature 526:660-665(2015).
[15]
INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=26375259; DOI=10.1038/nature15541;
Kayagaki N., Stowe I.B., Lee B.L., O'Rourke K., Anderson K.,
Warming S., Cuellar T., Haley B., Roose-Girma M., Phung Q.T.,
Liu P.S., Lill J.R., Li H., Wu J., Kummerfeld S., Zhang J., Lee W.P.,
Snipas S.J., Salvesen G.S., Morris L.X., Fitzgerald L., Zhang Y.,
Bertram E.M., Goodnow C.C., Dixit V.M.;
"Caspase-11 cleaves gasdermin D for non-canonical inflammasome
signalling.";
Nature 526:666-671(2015).
[16]
FUNCTION, AND MUTAGENESIS OF CYS-254.
PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J.,
Fang R., Meng G., Su X., Jiang Z.;
"Inflammasome activation triggers caspase-1-mediated cleavage of cGAS
to regulate responses to DNA virus infection.";
Immunity 46:393-404(2017).
-!- FUNCTION: Proinflammatory caspase (PubMed:8702803, PubMed:9038361,
PubMed:25119034). 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, as well as infection with
Gram-negative bacteria (PubMed:22002608). 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
(PubMed:22002608, PubMed:26320999, PubMed:26375003). Plays a
crucial role in the restriction of Salmonella typhimurium
replication in colonic epithelial cells during infection. In later
stages of the infection (>3 days post infection), LPS from
cytosolic Salmonella triggers CASP4 activation, which ultimately
results in the pyroptosis of the 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 (PubMed:25121752). Involved in LPS-
induced IL6 secretion; this activity may not require caspase
enzymatic activity (By similarity). Involved in cell death induced
by endoplasmic reticulum stress (By similarity). Activated by
direct binding to LPS without the need of an upstream sensor
(PubMed:25119034). Does not directly process IL1B (PubMed:8702803,
PubMed:9038361). During non-canonical inflammasome activation,
cuts CGAS and may play a role in the regulation of antiviral
innate immune activation (PubMed:28314590).
{ECO:0000250|UniProtKB:P49662, ECO:0000269|PubMed:22002608,
ECO:0000269|PubMed:25119034, ECO:0000269|PubMed:25121752,
ECO:0000269|PubMed:26320999, ECO:0000269|PubMed:26375003,
ECO:0000269|PubMed:28314590, ECO:0000269|PubMed:8702803,
ECO:0000269|PubMed:9038361}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for Asp at the P1 position and has a
preferred cleavage sequence of (Ile/Leu/Val/Phe)-Gly-His-
Asp-|-.; EC=3.4.22.64; Evidence={ECO:0000250|UniProtKB:P49662};
-!- ACTIVITY REGULATION: Activated by homooligomerization induced by
direct binding to cytosolic LPS, in a TLR4-independent manner.
{ECO:0000269|PubMed:25119034}.
-!- SUBUNIT: Upon direct LPS-binding, forms large homooligomers,
resulting in its activation. These oligomers are often referred to
as 'non-canonical inflammasomes' (PubMed:25119034). 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,
ECO:0000269|PubMed:25119034}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P49662}. Cytoplasm
{ECO:0000269|PubMed:16670335}. 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:0000269|PubMed:25119034}. 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70343-1; Sequence=Displayed;
Name=2;
IsoId=P70343-2; Sequence=VSP_058183, VSP_058184;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay. No
experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed, including in thymus, lung
and spleen (at protein level). Very low levels, if any, in the
brain. {ECO:0000269|PubMed:8702803, ECO:0000269|PubMed:9038361}.
-!- INDUCTION: Up-regulated by LPS and E.coli (PubMed:8702803,
PubMed:10986288, PubMed:22002608, PubMed:26375259). In LPS-induced
lung inflammation, markedly up-regulated after 6 hours of
treatment and decreases at 24 hours. The induction is dependent
upon DDIT3/CHOP-mediated ER stress (at protein level)
(PubMed:16670335). In the spleen and in bone marrow-derived
macrophages, up-regulated by poly(I:C), a synthetic analog of
double-stranded RNA (at protein level) (PubMed:26320999,
PubMed:26375259). Also induced by IFNG and interferon-alpha. Up-
regulated by R848, a TLR7 synthetic activator, and Pam3CysK4, a
synthetic activator of TLR1/TLR2 (PubMed:26375259).
{ECO:0000269|PubMed:10986288, ECO:0000269|PubMed:16670335,
ECO:0000269|PubMed:22002608, ECO:0000269|PubMed:26320999,
ECO:0000269|PubMed:26375259, ECO:0000269|PubMed:8702803}.
-!- DOMAIN: The CARD domain mediates LPS recognition and
homooligomerization. {ECO:0000269|PubMed:25119034}.
-!- PTM: In response to activation signals, including cholera
enterotoxin subunit B, infection by E. coli or S. typhimurium or
endoplasmic reticulum stress, undergoes autoproteolytic cleavage.
{ECO:0000269|PubMed:22002608, ECO:0000269|PubMed:25121752}.
-!- POLYMORPHISM: A variant of this gene has been observed in several
129 substrains, including 129/SvJ, 129S1/Sv, 129P3/J and
129S6/SvEvTac. This variant displays a 5-bp deletion encompassing
the exon 7 splice acceptor junction. As a result, exon 7 is
spliced out. Joining of exon 6 to exon 8 creates a frameshift
after Pro-304 and a stop codon occurs after 5 aberrant amino
acids. The mRNA may be the target of nonsense-mediated mRNA decay.
It is detected only at low levels, while the corresponding protein
is not detected at all in any of the 129 substrains tested.
{ECO:0000269|PubMed:22002608}.
-!- DISRUPTION PHENOTYPE: Mutant animals are largely resistant to LPS-
induced lethal septic shock (PubMed:22002608, PubMed:26375259).
However, they are susceptible to Burkholderia thailandensis
infection, even at low bacterial doses (PubMed:26320999). During
intestinal Salmonella Typhimurium infection, mutant animals
display higher pathogen loads in their cecal tissues and lumen and
lower levels of IL18 in cecal explants, associated with a
significant reduction in cecal inflammation (PubMed:25121752).
Bone-marrow-derived macrophages from knockout mice respond
normally, in terms of IL1B secretion, to canonical inflammasome
activators, such as ATP, monosodium urate, poly(dA:dT) double-
stranded DNA, Francisella tularensis, flagellin or Pseudomonas
aeruginosa, but fail to secrete IL1B in response to cholera
enterotoxin subunit B. They also do not respond to live E. coli,
C. rodentium and V. cholerae, with or without LPS priming
(PubMed:22002608). {ECO:0000269|PubMed:22002608,
ECO:0000269|PubMed:25121752, ECO:0000269|PubMed:26320999,
ECO:0000269|PubMed:26375259}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; U59463; AAB09469.1; -; mRNA.
EMBL; Y13089; CAA73531.1; -; mRNA.
EMBL; AB480706; BAH96541.1; -; mRNA.
EMBL; AK151547; BAE30493.1; -; mRNA.
EMBL; AK171877; BAE42715.1; -; mRNA.
EMBL; AC141637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466636; EDL09318.1; -; Genomic_DNA.
EMBL; BC061255; AAH61255.1; -; mRNA.
CCDS; CCDS22799.1; -. [P70343-1]
RefSeq; NP_031635.2; NM_007609.3. [P70343-1]
UniGene; Mm.1569; -.
ProteinModelPortal; P70343; -.
SMR; P70343; -.
DIP; DIP-61776N; -.
IntAct; P70343; 2.
STRING; 10090.ENSMUSP00000027012; -.
BindingDB; P70343; -.
ChEMBL; CHEMBL1075276; -.
MEROPS; C14.012; -.
PhosphoSitePlus; P70343; -.
MaxQB; P70343; -.
PaxDb; P70343; -.
PRIDE; P70343; -.
Ensembl; ENSMUST00000027012; ENSMUSP00000027012; ENSMUSG00000033538. [P70343-1]
Ensembl; ENSMUST00000160064; ENSMUSP00000124249; ENSMUSG00000033538. [P70343-2]
GeneID; 12363; -.
KEGG; mmu:12363; -.
UCSC; uc009obt.3; mouse. [P70343-1]
CTD; 837; -.
MGI; MGI:107700; Casp4.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000162428; -.
HOGENOM; HOG000234399; -.
HOVERGEN; HBG076981; -.
InParanoid; P70343; -.
KO; K04394; -.
OMA; YSWRCHL; -.
OrthoDB; 1327703at2759; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.57; 3474.
BRENDA; 3.4.22.64; 3474.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
PRO; PR:P70343; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000033538; Expressed in 105 organ(s), highest expression level in left lung.
ExpressionAtlas; P70343; baseline and differential.
Genevisible; P70343; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0061702; C:inflammasome complex; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0050700; F:CARD domain binding; ISO:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0007015; P:actin filament organization; TAS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IBA:GO_Central.
GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:MGI.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IGI:MGI.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
GO; GO:0070269; P:pyroptosis; IMP:MGI.
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.
1: Evidence at protein level;
Alternative splicing; 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_0000004600.
CHAIN 81 266 Caspase-4 subunit p20.
/FTId=PRO_0000004601.
PROPEP 267 285 {ECO:0000255}.
/FTId=PRO_0000004602.
CHAIN 286 373 Caspase-4 subunit p10.
/FTId=PRO_0000004603.
DOMAIN 1 91 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
REGION 1 59 Required for LPS-binding.
{ECO:0000269|PubMed:25119034}.
ACT_SITE 206 206 {ECO:0000250}.
ACT_SITE 254 254 {ECO:0000250|UniProtKB:P49662}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000250|UniProtKB:P49662}.
VAR_SEQ 88 118 ANLEMEEPEESLNTLKLCSPEEFTRLCREKT -> DLPNKG
GQWPYTKGSYHMQYRVQTSLTEVWG (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_058183.
VAR_SEQ 119 373 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_058184.
MUTAGEN 19 19 K->E: Severely attenuated LPS-binding,
LPS-induced oligomerization and
activation, and LPS-induced pyroptosis.
{ECO:0000269|PubMed:25119034}.
MUTAGEN 38 38 K->E: No effect on LPS-binding, LPS-
induced oligomerization, and LPS-induced
pyroptosis; when associated with M-40.
{ECO:0000269|PubMed:25119034}.
MUTAGEN 40 40 E->M: No effect on LPS-binding, LPS-
induced oligomerization, and LPS-induced
pyroptosis; when associated with E-38.
{ECO:0000269|PubMed:25119034}.
MUTAGEN 53 53 K->E: Complete loss of LPS-binding, LPS-
induced oligomerization, and LPS-induced
pyroptosis; when associated with E-54 and
A-55. {ECO:0000269|PubMed:25119034}.
MUTAGEN 54 54 R->E: Complete loss of LPS-binding, LPS-
induced oligomerization, and LPS-induced
pyroptosis; when associated with E-53 and
A-55. {ECO:0000269|PubMed:25119034}.
MUTAGEN 55 55 W->A: Complete loss of LPS-binding, LPS-
induced oligomerization, and LPS-induced
pyroptosis; when associated with E-54 and
A-55. {ECO:0000269|PubMed:25119034}.
MUTAGEN 62 62 K->E: Severely attenuated LPS-binding,
LPS-induced oligomerization and
activation, and LPS-induced pyroptosis;
when associated with E-63 and E-64.
{ECO:0000269|PubMed:25119034}.
MUTAGEN 63 63 K->E: Severely attenuated LPS-binding,
LPS-induced oligomerization and
activation, and LPS-induced pyroptosis;
when associated with E-62 and E-64.
{ECO:0000269|PubMed:25119034}.
MUTAGEN 64 64 K->E: Severely attenuated LPS-binding,
LPS-induced oligomerization and
activation, and LPS-induced pyroptosis;
when associated with E-62 and E-63.
{ECO:0000269|PubMed:25119034}.
MUTAGEN 254 254 C->A: Loss of catalytic activity and of
autocatalytic processing. Loss of LPS-
induced pyroptosis. No effect on the
interaction with LPS.
{ECO:0000269|PubMed:22002608,
ECO:0000269|PubMed:25119034,
ECO:0000269|PubMed:28314590}.
MUTAGEN 254 254 C->G: No cell death.
CONFLICT 126 126 E -> K (in Ref. 7; AAH61255).
{ECO:0000305}.
CONFLICT 152 152 N -> K (in Ref. 1; AAB09469).
{ECO:0000305}.
SEQUENCE 373 AA; 42742 MW; 110D7AA75E71C2B3 CRC64;
MAENKHPDKP LKVLEQLGKE VLTEYLEKLV QSNVLKLKEE DKQKFNNAER SDKRWVFVDA
MKKKHSKVGE MLLQTFFSVD PGSHHGEANL EMEEPEESLN TLKLCSPEEF TRLCREKTQE
IYPIKEANGR TRKALIICNT EFKHLSLRYG ANFDIIGMKG LLEDLGYDVV VKEELTAEGM
ESEMKDFAAL SEHQTSDSTF LVLMSHGTLH GICGTMHSEK TPDVLQYDTI YQIFNNCHCP
GLRDKPKVII VQACRGGNSG EMWIRESSKP QLCRGVDLPR NMEADAVKLS HVEKDFIAFY
STTPHHLSYR DKTGGSYFIT RLISCFRKHA CSCHLFDIFL KVQQSFEKAS IHSQMPTIDR
ATLTRYFYLF PGN


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Pathways :
WP1965: VEGF-receptor Signal Transduction
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP88: Toll Like Receptor signaling
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1644: DNA replication
WP1655: Geraniol degradation
WP1663: Homologous recombination
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1711: Trinitrotoluene degradation
WP1718: Vitamin B6 metabolism
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP2199: Seed Development
WP470: Proteasome Degradation

Related Genes :
[Casp4 Casp11 Caspl Ich3] Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]
[CASP14] Caspase-14 (CASP-14) (EC 3.4.22.-) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form]
[CASP8 MCH5] Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[CASP4 ICH2] Caspase-4 (CASP-4) (EC 3.4.22.57) (ICE and Ced-3 homolog 2) (ICH-2) (ICE(rel)-II) (Mih1) (Protease TX) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[CASP2 ICH1 NEDD2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp2 Ich1] Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[Casp6] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP6 MCH2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp6 Mch2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[CASP4] Caspase-4 (CASP-4) (EC 3.4.22.57) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[AMC4 AMC7 MCP2D At1g79340 YUP8H12R.4] Metacaspase-4 (AtMC4) (EC 3.4.22.-) (Metacaspase 2d) (AtMCP2d) (Metacaspase-7) [Cleaved into: Metacaspase-4 subunit p20; Metacaspase-4 subunit p10]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (ICE-like apoptotic protease 3) (ICE-LAP3) (SREBP cleavage activity 2) (SCA-2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]

Bibliography :