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NACHT, LRR and PYD domains-containing protein 3 (Cold autoinflammatory syndrome 1 protein homolog) (Cryopyrin) (Mast cell maturation-associated-inducible protein 1) (PYRIN-containing APAF1-like protein 1)

 NLRP3_MOUSE             Reviewed;        1033 AA.
Q8R4B8; Q1JQ87; Q1JQ88; Q6JEL0; T1W2H6;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
22-NOV-2017, entry version 150.
RecName: Full=NACHT, LRR and PYD domains-containing protein 3;
AltName: Full=Cold autoinflammatory syndrome 1 protein homolog;
AltName: Full=Cryopyrin;
AltName: Full=Mast cell maturation-associated-inducible protein 1;
AltName: Full=PYRIN-containing APAF1-like protein 1;
Name=Nlrp3; Synonyms=Cias1, Mmig1, Nalp3, Pypaf1;
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] (ISOFORMS 1; 2; 3 AND 4), AND SUBCELLULAR
LOCATION.
STRAIN=BALB/cJ;
PubMed=14688236; DOI=10.1093/jb/mvg195;
Kikuchi-Yanoshita R., Taketomi Y., Koga K., Sugiki T., Atsumi Y.,
Saito T., Ishii S., Hisada M., Suzuki-Nishimura T., Uchida M.K.,
Moon T.-C., Chang H.-W., Sawada M., Inagaki N., Nagai H., Murakami M.,
Kudo I.;
"Induction of PYPAF1 during in vitro maturation of mouse mast cells.";
J. Biochem. 134:699-709(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
STRAIN=129/Sv, BALB/cJ, and C57BL/6J;
PubMed=15302403; DOI=10.1016/j.gene.2004.05.002;
Anderson J.P., Mueller J.L., Rosengren S., Boyle D.L., Schaner P.,
Cannon S.B., Goodyear C.S., Hoffman H.M.;
"Structural, expression, and evolutionary analysis of mouse CIAS1.";
Gene 338:25-34(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
Martinon F., Hofmann K., Tschopp J.;
"Murine NALPs: a family of proteins involved in inflammation.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=BALB/cJ;
Huang Z.Q., Yu M., Tong S.;
Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
[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 MRNA] (ISOFORMS 1 AND 4).
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).
[7]
FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LPS, DEVELOPMENTAL STAGE,
AND DISRUPTION PHENOTYPE.
PubMed=16546100; DOI=10.1016/j.immuni.2006.02.004;
Sutterwala F.S., Ogura Y., Szczepanik M., Lara-Tejero M.,
Lichtenberger G.S., Grant E.P., Bertin J., Coyle A.J., Galan J.E.,
Askenase P.W., Flavell R.A.;
"Critical role for NALP3/CIAS1/Cryopyrin in innate and adaptive
immunity through its regulation of caspase-1.";
Immunity 24:317-327(2006).
[8]
FUNCTION.
PubMed=17008311; DOI=10.1074/jbc.M607594200;
Kanneganti T.-D., Body-Malapel M., Amer A., Park J.-H., Whitfield J.,
Franchi L., Taraporewala Z.F., Miller D., Patton J.T., Inohara N.,
Nunez G.;
"Critical role for cryopyrin/Nalp3 in activation of caspase-1 in
response to viral infection and double-stranded RNA.";
J. Biol. Chem. 281:36560-36568(2006).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16407890; DOI=10.1038/nature04515;
Mariathasan S., Weiss D.S., Newton K., McBride J., O'Rourke K.,
Roose-Girma M., Lee W.P., Weinrauch Y., Monack D.M., Dixit V.M.;
"Cryopyrin activates the inflammasome in response to toxins and ATP.";
Nature 440:228-232(2006).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16407888; DOI=10.1038/nature04517;
Kanneganti T.-D., Oezoeren N., Body-Malapel M., Amer A., Park J.-H.,
Franchi L., Whitfield J., Barchet W., Colonna M., Vandenabeele P.,
Bertin J., Coyle A., Grant E.P., Akira S., Nunez G.;
"Bacterial RNA and small antiviral compounds activate caspase-1
through cryopyrin/Nalp3.";
Nature 440:233-236(2006).
[11]
TISSUE SPECIFICITY, INDUCTION BY SALMONELLA, AND INTERACTION WITH
PYCARD.
PubMed=17907925; DOI=10.1359/jbmr.071002;
McCall S.H., Sahraei M., Young A.B., Worley C.S., Duncan J.A.,
Ting J.P., Marriott I.;
"Osteoblasts express NLRP3, a nucleotide-binding domain and leucine-
rich repeat region containing receptor implicated in bacterially
induced cell death.";
J. Bone Miner. Res. 23:30-40(2008).
[12]
FUNCTION.
PubMed=20802146; DOI=10.4049/jimmunol.1000803;
Lamkanfi M., Sarkar A., Vande Walle L., Vitari A.C., Amer A.O.,
Wewers M.D., Tracey K.J., Kanneganti T.D., Dixit V.M.;
"Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia.";
J. Immunol. 185:4385-4392(2010).
[13]
UBIQUITINATION, AND DEUBIQUITINATION.
PubMed=22948162; DOI=10.1074/jbc.M112.407130;
Juliana C., Fernandes-Alnemri T., Kang S., Farias A., Qin F.,
Alnemri E.S.;
"Non-transcriptional priming and deubiquitination regulate NLRP3
inflammasome activation.";
J. Biol. Chem. 287:36617-36622(2012).
[14]
FUNCTION, AND INTERACTION WITH EIF2AK2.
PubMed=22801494; DOI=10.1038/nature11290;
Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundbaeck P.,
Valdes-Ferrer S.I., Olofsson P.S., Kalb T., Roth J., Zou Y.,
Erlandsson-Harris H., Yang H., Ting J.P., Wang H., Andersson U.,
Antoine D.J., Chavan S.S., Hotamisligil G.S., Tracey K.J.;
"Novel role of PKR in inflammasome activation and HMGB1 release.";
Nature 488:670-674(2012).
[15]
UBIQUITINATION, AND DEUBIQUITINATION BY BRCC3.
PubMed=23246432; DOI=10.1016/j.molcel.2012.11.009;
Py B.F., Kim M.S., Vakifahmetoglu-Norberg H., Yuan J.;
"Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome
activity.";
Mol. Cell 49:331-338(2013).
[16]
SUBCELLULAR LOCATION.
PubMed=23502856; DOI=10.1038/ni.2550;
Misawa T., Takahama M., Kozaki T., Lee H., Zou J., Saitoh T.,
Akira S.;
"Microtubule-driven spatial arrangement of mitochondria promotes
activation of the NLRP3 inflammasome.";
Nat. Immunol. 14:454-460(2013).
[17]
MECHANISM OF INFLAMMASOME ASSEMBLY.
PubMed=24630723; DOI=10.1016/j.cell.2014.01.063;
Cai X., Chen J., Xu H., Liu S., Jiang Q.X., Halfmann R., Chen Z.J.;
"Prion-like polymerization underlies signal transduction in antiviral
immune defense and inflammasome activation.";
Cell 156:1207-1222(2014).
[18]
SUBCELLULAR LOCATION, AND SECRETION OF INFLAMMASOME POLYMERS.
PubMed=24952505; DOI=10.1038/ni.2913;
Franklin B.S., Bossaller L., De Nardo D., Ratter J.M., Stutz A.,
Engels G., Brenker C., Nordhoff M., Mirandola S.R., Al-Amoudi A.,
Mangan M.S., Zimmer S., Monks B.G., Fricke M., Schmidt R.E.,
Espevik T., Jones B., Jarnicki A.G., Hansbro P.M., Busto P.,
Marshak-Rothstein A., Hornemann S., Aguzzi A., Kastenmuller W.,
Latz E.;
"The adaptor ASC has extracellular and 'prionoid' activities that
propagate inflammation.";
Nat. Immunol. 15:727-737(2014).
[19]
SUBCELLULAR LOCATION.
PubMed=24952504; DOI=10.1038/ni.2919;
Baroja-Mazo A., Martin-Sanchez F., Gomez A.I., Martinez C.M.,
Amores-Iniesta J., Compan V., Barbera-Cremades M., Yaguee J.,
Ruiz-Ortiz E., Anton J., Bujan S., Couillin I., Brough D.,
Arostegui J.I., Pelegrin P.;
"The NLRP3 inflammasome is released as a particulate danger signal
that amplifies the inflammatory response.";
Nat. Immunol. 15:738-748(2014).
[20]
FUNCTION IN TH2 CELLS, INTERACTION WITH IRF4, SUBCELLULAR LOCATION,
INDUCTION BY IL2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
DISRUPTION PHENOTYPE.
PubMed=26098997; DOI=10.1038/ni.3202;
Bruchard M., Rebe C., Derangere V., Togbe D., Ryffel B., Boidot R.,
Humblin E., Hamman A., Chalmin F., Berger H., Chevriaux A.,
Limagne E., Apetoh L., Vegran F., Ghiringhelli F.;
"The receptor NLRP3 is a transcriptional regulator of TH2
differentiation.";
Nat. Immunol. 16:859-870(2015).
-!- FUNCTION: As the sensor component of the NLRP3 inflammasome, plays
a crucial role in innate immunity and inflammation. In response to
pathogens and other damage-associated signals, initiates the
formation of the inflammasome polymeric complex, made of NLRP3,
PYCARD and CASP1 (or possibly CASP4/CASP11). Recruitment of
proCASP1 to the inflammasome promotes its activation and CASP1-
catalyzed IL1B and IL18 maturation and secretion in the
extracellular milieu. Activation of NLRP3 inflammasome is also
required for HMGB1 secretion (PubMed:22801494). The active
cytokines and HMGB1 stimulate inflammatory responses.
Inflammasomes can also induce pyroptosis, an inflammatory form of
programmed cell death. Under resting conditions, NLRP3 is
autoinhibited. NLRP3 activation stimuli include extracellular ATP,
reactive oxygen species, K(+) efflux, crystals of monosodium urate
or cholesterol, amyloid-beta fibers, environmental or industrial
particles and nanoparticles, etc. However, it is unclear what
constitutes the direct NLRP3 activator. Independently of
inflammasome activation, regulates the differentiation of T helper
2 (Th2) cells and has a role in Th2 cell-dependent asthma and
tumor growth. During Th2 differentiation, required for optimal
IRF4 binding to IL4 promoter and for IRF4-dependent IL4
transcription. Binds to the consensus DNA sequence 5'-GRRGGNRGAG-
3'. May also participate in the transcription of IL5, IL13, GATA3,
CCR3, CCR4 and MAF (PubMed:26098997).
{ECO:0000269|PubMed:16407888, ECO:0000269|PubMed:16407890,
ECO:0000269|PubMed:16546100, ECO:0000269|PubMed:17008311,
ECO:0000269|PubMed:22801494, ECO:0000269|PubMed:26098997}.
-!- SUBUNIT: Sensor component of NLRP3 inflammasomes. Inflammasomes
are supramolecular complexes that assemble in the cytosol in
response to pathogens and other damage-associated signals and play
critical roles in innate immunity and inflammation. The core of
NLRP3 inflammasomes consists of a signal sensor component (NLRP3),
an adapter (ASC/PYCARD), which recruits an effector
proinflammatory caspase (CASP1 and, possibly, CASP4 and CASP5).
Within the complex, NLRP3 and PYCARD interact via their respective
pyrin domains. This interaction initiates speck formation
(nucleation) which greatly enhances further addition of soluble
PYCARD molecules to the speck in a prion-like polymerization
process. NLRP3 localizes at the end of each PYCARD filament.
Clustered PYCARD nucleates the formation of CASP1 filaments
through the interaction of their respective CARD domains, acting
as a platform for CASP1 polymerization. CASP1 filament formation
increases local enzyme concentration, resulting in trans-
autocleavage and activation. Active CASP1 then processes IL1B and
IL18 precursors, leading to the release of mature cytokines in the
extracellular milieu and inflammatory response. Reconstituted
ternary inflammasomes show star-shaped structures, in which
multiple filaments, containing CASP1, protrude radially from a
single central hub, containing the sensor protein and PYCARD. In
this complex, the sensor protein is sub-stoichiometric to PYCARD,
and PYCARD is further substoichiometric to CASP1, suggesting
amplifications of signal transduction from the sensor, via the
adapter, to the effector (By similarity). Interacts with MEFV;
this interaction targets NLRP3 to degradation by autophagy, hence
preventing excessive IL1B- and IL18-mediated inflammation (By
similarity). Interacts with GBP5 (via DAPIN domain); this
interaction promotes inflammasome assembly in response to
microbial and soluble, but not crystalline, agents (By
similarity). Interacts with EIF2AK2/PKR; this interaction requires
EIF2AK2 activity, is accompanied by EIF2AK2 autophosphorylation
and promotes inflammasome assembly in response to specific stimuli
(PubMed:22801494). Interacts with PML (isoform PML-1) (via the LRR
region); PML-mediated increase in NLRP3 inflammasome activation
does not depend upon this interaction. Directly interacts with
IRF4 (via LRR region); this interaction is required for optimal
IRF4 binding to IL4 promoter and efficient IL4 transactivation
during differentiation of Th2 helper T-cells (PubMed:26098997).
{ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:22801494,
ECO:0000269|PubMed:26098997}.
-!- INTERACTION:
Q03963:Eif2ak2; NbExp=3; IntAct=EBI-6910832, EBI-2603444;
Q9ES74:Nek7; NbExp=2; IntAct=EBI-6910832, EBI-16193749;
Q9EPB4:Pycard; NbExp=3; IntAct=EBI-6910832, EBI-6253348;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:14688236, ECO:0000269|PubMed:23502856,
ECO:0000269|PubMed:26098997}. Inflammasome
{ECO:0000269|PubMed:14688236, ECO:0000269|PubMed:23502856,
ECO:0000269|PubMed:26098997}. Endoplasmic reticulum
{ECO:0000269|PubMed:23502856}. Secreted
{ECO:0000269|PubMed:24952504}. Nucleus
{ECO:0000269|PubMed:26098997}. Note=In macrophages, under resting
conditions, mainly located in the cytosol, on the endoplasmic
reticulum. After stimulation with inducers of the NLRP3
inflammasome, mitochondria redistribute in the vicinity of the
endoplasmic reticulum in the perinuclear region, which results in
colocalization of NLRP3 on the endoplasmic reticulum and PYCARD on
mitochondria, allowing the activation of inflammasome assembly
(PubMed:23502856). After the induction of pyroptosis, inflammasome
specks are released into the extracellular space where they can
further promote IL1B processing and where they can be engulfed by
macrophages. Phagocytosis induces lysosomal damage and
inflammasome activation in the recipient cells
(PubMed:24952505)(PubMed:24952504). In the Th2 subset of CD4(+)
helper T-cells, mainly located in the nucleus. Nuclear
localization depends upon KPNA2 (PubMed:26098997). In the Th1
subset of CD4(+) helper T-cells, mainly cytoplasmic
(PubMed:26098997). {ECO:0000269|PubMed:23502856,
ECO:0000269|PubMed:24952504, ECO:0000269|PubMed:24952505}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=MMIG-1a;
IsoId=Q8R4B8-1; Sequence=Displayed;
Name=2; Synonyms=MMIG-1b;
IsoId=Q8R4B8-2; Sequence=VSP_014927;
Name=3; Synonyms=MMIG-1c;
IsoId=Q8R4B8-3; Sequence=VSP_014925;
Name=4; Synonyms=MMIG-1d;
IsoId=Q8R4B8-4; Sequence=VSP_014926;
-!- TISSUE SPECIFICITY: Expressed with high levels in peripheral blood
leukocytes, including Th2 lymphocytes and macrophages
(PubMed:15302403) (PubMed:26098997) (PubMed:16546100). Expressed
at low levels in resting osteoblasts (at protein level)
(PubMed:17907925). {ECO:0000269|PubMed:15302403,
ECO:0000269|PubMed:16546100, ECO:0000269|PubMed:17907925,
ECO:0000269|PubMed:26098997}.
-!- DEVELOPMENTAL STAGE: Up-regulated during CD4(+) T-lymphocyte
differentiation, in Th0, Th1 and Th2 cells. Not detected in naive
CD4(+) T-lymphocytes (at protein level).
{ECO:0000269|PubMed:16546100, ECO:0000269|PubMed:26098997}.
-!- INDUCTION: By activators of Toll-like receptors, such as
lipoteichoic acid (LTA) (TLR2), polyinosine-polycytidylic acid
(poly(I:C), a synthetic analog of dsRNA) (TLR3) and bacterial
lipopolysaccharides (LPS) (TLR4) (PubMed:16546100). Up-regulated
by IL2 via STAT5 signaling (PubMed:26098997). Slightly up-
regulated in osteoblasts after exposure to invasive, but not
invasion-defective, strains of Salmonella typhimurium (at protein
level) (PubMed:17907925). {ECO:0000269|PubMed:16546100,
ECO:0000269|PubMed:17907925, ECO:0000269|PubMed:26098997}.
-!- DOMAIN: The LRR domain mediates the interaction with IRF4 and PML.
{ECO:0000250|UniProtKB:Q96P20, ECO:0000269|PubMed:26098997}.
-!- DOMAIN: Intramolecular interactions between NACHT and leucine-rich
repeat (LRR) domains may be important for autoinhibition in the
absence of activating signal. {ECO:0000250|UniProtKB:Q9EPB4}.
-!- DOMAIN: The pyrin domain (also called DAPIN domain or PYD) is
involved in PYCARD-binding.
-!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitination. Ubiquitination does not lead to degradation,
but inhibits inflammasome activation (PubMed:23246432).
Deubiquitination is catalyzed by BRCC3 and associated with NLRP3
activation and inflammasome assembly. This process can be induced
by the activation of Toll-like receptors (by LPS), through a non-
transcriptional pathway dependent on the mitochondrial production
of reactive oxygen species, and by ATP.
{ECO:0000269|PubMed:22948162, ECO:0000269|PubMed:23246432}.
-!- PTM: The disulfide bond in the pyrin domain might play a role in
reactive oxygen species-mediated activation.
{ECO:0000250|UniProtKB:Q96P20}.
-!- DISRUPTION PHENOTYPE: Knockout mice are fertile and appear healthy
when housed in a standard specific pathogen-free environment. They
do not exhibit any increase in serum IL1B after administration of
R837 (an analog to guanosine and TLR7 agonist) and/or LPS
(PubMed:16407890) (PubMed:16407888). When challenged with LPS,
mutant mice are partially resistant to endotoxic shock
(PubMed:16546100) (PubMed:16407890). Mutant mice display impaired
contact hypersensitivity, a T-cell-mediated cellular immune
response to repeated epicutaneous exposure to contact allergens,
such as trinitrophenylchloride (PubMed:16546100). In a model of
allergic asthma that promotes strictly Th2 responses, mutant
animals show less infiltration of eosinophils and lymphocytes into
the lungs than their wild-type counterparts, as well as less
accumulation of mucus and lymphoid infiltrates. The concentration
of Th2 cell-related cytokines, including IL-5 and IL-4, is also
lower in lungs from mutant mice compared to wild-type
(PubMed:26098997). {ECO:0000269|PubMed:16407888,
ECO:0000269|PubMed:16407890, ECO:0000269|PubMed:16546100,
ECO:0000269|PubMed:26098997}.
-!- MISCELLANEOUS: Expression is increased in mice with experimental
atopic dermatitis.
-!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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EMBL; AF486632; AAL90874.1; -; mRNA.
EMBL; AY495376; AAS75794.1; -; mRNA.
EMBL; AY495377; AAS75795.1; -; mRNA.
EMBL; AY337285; AAR03540.1; -; mRNA.
EMBL; AY337292; AAR03541.1; -; Genomic_DNA.
EMBL; AY337286; AAR03541.1; JOINED; Genomic_DNA.
EMBL; AY337287; AAR03541.1; JOINED; Genomic_DNA.
EMBL; AY337288; AAR03541.1; JOINED; Genomic_DNA.
EMBL; AY337289; AAR03541.1; JOINED; Genomic_DNA.
EMBL; AY337290; AAR03541.1; JOINED; Genomic_DNA.
EMBL; AY337291; AAR03541.1; JOINED; Genomic_DNA.
EMBL; AY337299; AAR03542.1; -; Genomic_DNA.
EMBL; AY337293; AAR03542.1; JOINED; Genomic_DNA.
EMBL; AY337294; AAR03542.1; JOINED; Genomic_DNA.
EMBL; AY337295; AAR03542.1; JOINED; Genomic_DNA.
EMBL; AY337296; AAR03542.1; JOINED; Genomic_DNA.
EMBL; AY337297; AAR03542.1; JOINED; Genomic_DNA.
EMBL; AY337298; AAR03542.1; JOINED; Genomic_DNA.
EMBL; AY337306; AAR03543.1; -; Genomic_DNA.
EMBL; AY337300; AAR03543.1; JOINED; Genomic_DNA.
EMBL; AY337301; AAR03543.1; JOINED; Genomic_DNA.
EMBL; AY337302; AAR03543.1; JOINED; Genomic_DNA.
EMBL; AY337303; AAR03543.1; JOINED; Genomic_DNA.
EMBL; AY337304; AAR03543.1; JOINED; Genomic_DNA.
EMBL; AY337305; AAR03543.1; JOINED; Genomic_DNA.
EMBL; AY355340; AAR14737.1; -; mRNA.
EMBL; KF032621; AGU01502.1; -; mRNA.
EMBL; AL592522; CAI24551.1; -; Genomic_DNA.
EMBL; BC116174; AAI16175.1; -; mRNA.
EMBL; BC116175; AAI16176.1; -; mRNA.
CCDS; CCDS24771.1; -. [Q8R4B8-1]
RefSeq; NP_665826.1; NM_145827.3. [Q8R4B8-1]
RefSeq; XP_006532920.1; XM_006532857.1. [Q8R4B8-1]
RefSeq; XP_006532921.1; XM_006532858.1. [Q8R4B8-1]
UniGene; Mm.54174; -.
ProteinModelPortal; Q8R4B8; -.
SMR; Q8R4B8; -.
DIP; DIP-60132N; -.
IntAct; Q8R4B8; 5.
STRING; 10090.ENSMUSP00000078440; -.
ChEMBL; CHEMBL3779755; -.
iPTMnet; Q8R4B8; -.
PhosphoSitePlus; Q8R4B8; -.
PaxDb; Q8R4B8; -.
PRIDE; Q8R4B8; -.
Ensembl; ENSMUST00000079476; ENSMUSP00000078440; ENSMUSG00000032691. [Q8R4B8-1]
Ensembl; ENSMUST00000101148; ENSMUSP00000098707; ENSMUSG00000032691. [Q8R4B8-1]
GeneID; 216799; -.
KEGG; mmu:216799; -.
UCSC; uc007jeh.1; mouse. [Q8R4B8-1]
CTD; 114548; -.
MGI; MGI:2653833; Nlrp3.
eggNOG; ENOG410IE5X; Eukaryota.
eggNOG; ENOG4111H3D; LUCA.
GeneTree; ENSGT00900000140813; -.
HOGENOM; HOG000294064; -.
HOVERGEN; HBG063656; -.
InParanoid; Q8R4B8; -.
KO; K12800; -.
OMA; PVHTVVF; -.
OrthoDB; EOG091G01CG; -.
PhylomeDB; Q8R4B8; -.
Reactome; R-MMU-5689901; Metalloprotease DUBs.
Reactome; R-MMU-844456; The NLRP3 inflammasome.
PRO; PR:Q8R4B8; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000032691; -.
CleanEx; MM_NLRP3; -.
ExpressionAtlas; Q8R4B8; baseline and differential.
Genevisible; Q8R4B8; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072559; C:NLRP3 inflammasome complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0051607; P:defense response to virus; IMP:MGI.
GO; GO:0006954; P:inflammatory response; ISS:HGNC.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0032611; P:interleukin-1 beta production; IMP:MGI.
GO; GO:0050701; P:interleukin-1 secretion; IMP:MGI.
GO; GO:0032621; P:interleukin-18 production; IMP:MGI.
GO; GO:0002674; P:negative regulation of acute inflammatory response; ISO:MGI.
GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; ISO:MGI.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; ISS:HGNC.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:HGNC.
GO; GO:0044546; P:NLRP3 inflammasome complex assembly; IMP:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:HGNC.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IGI:MGI.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IMP:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:2000321; P:positive regulation of T-helper 17 cell differentiation; IMP:UniProtKB.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:UniProtKB.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0002830; P:positive regulation of type 2 immune response; IMP:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR004020; DAPIN.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR029495; NACHT-assoc.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF14484; FISNA; 1.
Pfam; PF13516; LRR_6; 5.
Pfam; PF02758; PYRIN; 1.
SMART; SM01288; FISNA; 1.
SMART; SM01289; PYRIN; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS50824; DAPIN; 1.
PROSITE; PS51450; LRR; 5.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
Activator; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Disulfide bond; Endoplasmic reticulum; Immunity;
Inflammasome; Inflammatory response; Innate immunity;
Leucine-rich repeat; Nucleotide-binding; Nucleus; Reference proteome;
Repeat; Secreted; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 1033 NACHT, LRR and PYD domains-containing
protein 3.
/FTId=PRO_0000080887.
DOMAIN 1 91 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 216 532 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 739 759 LRR 1.
REPEAT 768 789 LRR 2.
REPEAT 796 816 LRR 3.
REPEAT 825 846 LRR 4.
REPEAT 853 873 LRR 5.
REPEAT 882 903 LRR 6.
REPEAT 910 930 LRR 7.
REPEAT 939 960 LRR 8.
REPEAT 967 988 LRR 9.
NP_BIND 222 229 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
DISULFID 6 104 Redox-active.
{ECO:0000250|UniProtKB:Q96P20}.
VAR_SEQ 774 830 Missing (in isoform 3).
{ECO:0000303|PubMed:14688236}.
/FTId=VSP_014925.
VAR_SEQ 830 1033 Missing (in isoform 4).
{ECO:0000303|PubMed:14688236,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_014926.
VAR_SEQ 888 944 Missing (in isoform 2).
{ECO:0000303|PubMed:14688236}.
/FTId=VSP_014927.
CONFLICT 491 491 Q -> R (in Ref. 4; AGU01502).
{ECO:0000305}.
SEQUENCE 1033 AA; 118275 MW; 5924690966B12117 CRC64;
MTSVRCKLAQ YLEDLEDVDL KKFKMHLEDY PPEKGCIPVP RGQMEKADHL DLATLMIDFN
GEEKAWAMAV WIFAAINRRD LWEKAKKDQP EWNDTCTSHS SMVCQEDSLE EEWMGLLGYL
SRISICKKKK DYCKMYRRHV RSRFYSIKDR NARLGESVDL NSRYTQLQLV KEHPSKQERE
HELLTIGRTK MRDSPMSSLK LELLFEPEDG HSEPVHTVVF QGAAGIGKTI LARKIMLDWA
LGKLFKDKFD YLFFIHCREV SLRTPRSLAD LIVSCWPDPN PPVCKILRKP SRILFLMDGF
DELQGAFDEH IGEVCTDWQK AVRGDILLSS LIRKKLLPKA SLLITTRPVA LEKLQHLLDH
PRHVEILGFS EAKRKEYFFK YFSNELQARE AFRLIQENEV LFTMCFIPLV CWIVCTGLKQ
QMETGKSLAQ TSKTTTAVYV FFLSSLLQSR GGIEEHLFSD YLQGLCSLAA DGIWNQKILF
EECDLRKHGL QKTDVSAFLR MNVFQKEVDC ERFYSFSHMT FQEFFAAMYY LLEEEAEGET
VRKGPGGCSD LLNRDVKVLL ENYGKFEKGY LIFVVRFLFG LVNQERTSYL EKKLSCKISQ
QVRLELLKWI EVKAKAKKLQ WQPSQLELFY CLYEMQEEDF VQSAMDHFPK IEINLSTRMD
HVVSSFCIKN CHRVKTLSLG FFHNSPKEEE EERRGGRPLD QVQCVFPDTH VACSSRLVNC
CLTSSFCRGL FSSLSTNRSL TELDLSDNTL GDPGMRVLCE ALQHPGCNIQ RLWLGRCGLS
HQCCFDISSV LSSSQKLVEL DLSDNALGDF GIRLLCVGLK HLLCNLQKLW LVSCCLTSAC
CQDLALVLSS NHSLTRLYIG ENALGDSGVQ VLCEKMKDPQ CNLQKLGLVN SGLTSICCSA
LTSVLKTNQN FTHLYLRSNA LGDTGLRLLC EGLLHPDCKL QMLELDNCSL TSHSCWNLST
ILTHNHSLRK LNLGNNDLGD LCVVTLCEVL KQQGCLLQSL QLGEMYLNRE TKRALEALQE
EKPELTIVFE ISW


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