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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_RAT               Reviewed;        1035 AA.
D4A523;
10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 2.
20-JUN-2018, entry version 77.
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=Nalp3, Pypaf1;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
-!- 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 (By similarity). 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,
cytosolic dsRNA, etc. However, it is unclear what constitutes the
direct NLRP3 activator. Activation in presence of cytosolic dsRNA
is mediated by DHX33 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q8R4B8,
ECO:0000250|UniProtKB:Q96P20}.
-!- 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. 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 (By similarity). Interacts
(via NACHT domain) with DHX33 (via DEAH box) (By similarity).
{ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q8R4B8}. Inflammasome
{ECO:0000250|UniProtKB:Q8R4B8}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q8R4B8}. Secreted
{ECO:0000250|UniProtKB:Q8R4B8}. Nucleus
{ECO:0000250|UniProtKB:Q8R4B8}. 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.
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. In the Th2 subset
of CD4(+) helper T-cells, mainly located in the nucleus. Nuclear
localization depends upon KPNA2. In the Th1 subset of CD4(+)
helper T-cells, mainly cytoplasmic.
{ECO:0000250|UniProtKB:Q8R4B8}.
-!- DOMAIN: The LRR domain mediates the interaction with IRF4 and PML.
{ECO:0000250|UniProtKB:Q8R4B8, ECO:0000250|UniProtKB:Q96P20}.
-!- 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. {ECO:0000250|UniProtKB:Q8R4B8}.
-!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitination. Ubiquitination does not lead to degradation,
but inhibits inflammasome activation. 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:0000250|UniProtKB:Q8R4B8}.
-!- PTM: The disulfide bond in the pyrin domain might play a role in
reactive oxygen species-mediated activation.
{ECO:0000250|UniProtKB:Q96P20}.
-!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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EMBL; AC123316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001178571.1; NM_001191642.1.
RefSeq; XP_006246515.1; XM_006246453.3.
RefSeq; XP_017452567.1; XM_017597078.1.
UniGene; Rn.214177; -.
ProteinModelPortal; D4A523; -.
SMR; D4A523; -.
STRING; 10116.ENSRNOP00000004280; -.
PaxDb; D4A523; -.
PeptideAtlas; D4A523; -.
Ensembl; ENSRNOT00000004280; ENSRNOP00000004280; ENSRNOG00000003170.
GeneID; 287362; -.
KEGG; rno:287362; -.
UCSC; RGD:1308314; rat.
CTD; 114548; -.
RGD; 1308314; Nlrp3.
eggNOG; ENOG410IE5X; Eukaryota.
eggNOG; ENOG4111H3D; LUCA.
GeneTree; ENSGT00900000140813; -.
InParanoid; D4A523; -.
KO; K12800; -.
OMA; PVHTVVF; -.
OrthoDB; EOG091G01CG; -.
Reactome; R-RNO-5689901; Metalloprotease DUBs.
Reactome; R-RNO-844456; The NLRP3 inflammasome.
PRO; PR:D4A523; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000003170; -.
ExpressionAtlas; D4A523; baseline and differential.
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; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071224; P:cellular response to peptidoglycan; IEA:Ensembl.
GO; GO:0002374; P:cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0032611; P:interleukin-1 beta production; IEA:Ensembl.
GO; GO:0050701; P:interleukin-1 secretion; IEA:Ensembl.
GO; GO:0032621; P:interleukin-18 production; IEA:Ensembl.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0044546; P:NLRP3 inflammasome complex assembly; IEA:Ensembl.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:2000321; P:positive regulation of T-helper 17 cell differentiation; IEA:Ensembl.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IEA:Ensembl.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR004020; DAPIN.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR029495; NACHT-assoc.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF14484; FISNA; 1.
Pfam; PF13516; LRR_6; 5.
Pfam; PF05729; NACHT; 1.
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.
3: Inferred from homology;
Activator; 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 1035 NACHT, LRR and PYD domains-containing
protein 3.
/FTId=PRO_0000439878.
DOMAIN 1 93 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 218 534 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 741 761 LRR 1. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 770 791 LRR 2. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 798 818 LRR 3. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 827 848 LRR 4. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 855 875 LRR 5. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 884 905 LRR 6. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 912 932 LRR 7. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 941 962 LRR 8. {ECO:0000250|UniProtKB:Q8R4B8}.
REPEAT 969 990 LRR 9. {ECO:0000250|UniProtKB:Q8R4B8}.
NP_BIND 224 231 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
DISULFID 8 106 Redox-active.
{ECO:0000250|UniProtKB:Q96P20}.
SEQUENCE 1035 AA; 118540 MW; F182827924821C92 CRC64;
MKMMSVRCKL AQYLEDLEDV DLKKFKMHLE DYPPEKGCVP IPRGQMEKAD HLDLATLMID
FNGEEKAWGM AVWIFAAINR RDLWEKAKKD QPEWNDACTS NLSMVCQEDS LEEEWIGLLG
YLSRISICKK KKDYCKIYRR HVRSRFYSIK DRNARLGESV DLNRRYTQLQ LVKEHPSKQE
REHELLTIGR TKMWDRPMSS LKLELLFEPE DEHLEPVHTV VFQGAAGIGK TILARKIMLD
WALGKLFKDK FDYLFFIHCR EVSLRAPKSL ADLIISCWPD PNPPVCKILC KPSRILFLMD
GFDELQGAFD EHIEEVCTDW QKAVRGDILL SSLIRKKLLP KASLLITTRP VALEKLQHLL
DHPRHVEILG FSEAKRKEYF FKYFSNELQA REAFRLIQEN EILFTMCFIP LVCWIVCTGL
KQQMETGKSL AQTSKTTTAV YVFFLSSLLQ SRGGIEEHLF SAYLPGLCSL AADGIWNQKI
LFEECDLRKH GLQKTDVSAF LRMNVFQKEV DCERFYSFSH MTFQEFFAAM YYLLEEEEEG
VTVRKGPEGC SDLLNRDVKV LLENYGKFEK GYLIFVVRFL FGLVNQERTS YLEKKLSCKI
SQQVRLELLK WIEVKAKAKK LQRQPSQLEL FYCLYEMQEE DFVQSAMGHF PKIEINLSTR
MDHVVSSFCI KNCHRVKTLS LGFLHNSPKE EEEEKRGSQP LDQVQCVFPD PHVACSSRLV
NCCLTSSFCR GLFSSLSTNQ SLTELDLSDN TLGDPGMRVL CEALQHPGCN IQRLWLGRCG
LTHQCCFNIS SVLSSSQKLV ELDLSDNALG DFGVRLLCVG LKHLLCNLQK LWLVSCCLTS
ACCQDLALVL SSNHSLTRLY IGENALGDSG VQVLCEKMKD PQCNLQKLGL VNSGLTSLCC
SALTSVLKTN QNLTHLYLRS NALGDMGLKL LCEGLLHPDC KLQMLELDNC SLTSHSCWDL
STILTHNQSL RKLNLSNNDL GDLCVVTLCE VLKQQGCLLQ SLQLGEMYLN CETKRTLEAL
QEEKPELTVV FEISW


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Tel 01 43 25 01 50

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GENTAUR GmbH
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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