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NACHT, LRR and PYD domains-containing protein 1b allele 3

 NL1B3_MOUSE             Reviewed;        1172 AA.
Q2LKV5;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
21-FEB-2006, sequence version 1.
28-MAR-2018, entry version 83.
RecName: Full=NACHT, LRR and PYD domains-containing protein 1b allele 3 {ECO:0000303|PubMed:16429160};
Name=Nlrp1b; Synonyms=Nalp1b;
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], FUNCTION, TISSUE SPECIFICITY, AND
MISCELLANEOUS.
STRAIN=AKR/J, NOD/LtJ, and SJL/J;
PubMed=16429160; DOI=10.1038/ng1724;
Boyden E.D., Dietrich W.F.;
"Nalp1b controls mouse macrophage susceptibility to anthrax lethal
toxin.";
Nat. Genet. 38:240-244(2006).
[2]
FUNCTION, AND LACK OF RESPONSE TO BACILLUS ANTHRACIS LETHAL TOXIN.
PubMed=19651869; DOI=10.1128/IAI.00276-09;
Liao K.C., Mogridge J.;
"Expression of Nlrp1b inflammasome components in human fibroblasts
confers susceptibility to anthrax lethal toxin.";
Infect. Immun. 77:4455-4462(2009).
[3]
TISSUE SPECIFICITY, AND MISCELLANEOUS.
PubMed=23506131; DOI=10.1186/1471-2164-14-188;
Sastalla I., Crown D., Masters S.L., McKenzie A., Leppla S.H.,
Moayeri M.;
"Transcriptional analysis of the three Nlrp1 paralogs in mice.";
BMC Genomics 14:188-188(2013).
[4]
MUTAGENESIS OF ASP-927; ASP-935 AND SER-965.
PubMed=22536155; DOI=10.1371/journal.ppat.1002659;
Frew B.C., Joag V.R., Mogridge J.;
"Proteolytic processing of Nlrp1b is required for inflammasome
activity.";
PLoS Pathog. 8:E1002659-E1002659(2012).
[5]
LACK OF RESPONSE TO ANTHRAX LETHAL TOXIN AND METABOLIC INHIBITORS, AND
MUTAGENESIS OF ASP-927.
PubMed=23230290; DOI=10.1128/IAI.01003-12;
Liao K.C., Mogridge J.;
"Activation of the Nlrp1b inflammasome by reduction of cytosolic
ATP.";
Infect. Immun. 81:570-579(2013).
-!- FUNCTION: As the sensor component of the NLRP1 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 Nlrp1b,
CASP1, and possibly PYCARD. Recruitment of proCASP1 to the
inflammasome promotes its activation and CASP1-catalyzed IL1B and
IL18 maturation and secretion in the extracellular milieu.
Activation of NLRP1 inflammasome is also required for HMGB1
secretion. The active cytokines and HMGB1 stimulate inflammatory
responses. Inflammasomes can also induce pyroptosis, an
inflammatory form of programmed cell death (By similarity).
Contrary to Nlrp1b allele 1, allele 3 is not activated by Bacillus
anthracis lethal toxin, nor by metabolic inhibitors, such as 2-
deoxy-D-glucose and sodium azide (PubMed:16429160,
PubMed:19651869, PubMed:23230290). {ECO:0000250|UniProtKB:Q2LKW6,
ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:19651869,
ECO:0000269|PubMed:23230290}.
-!- SUBUNIT: Sensor component of NLRP1 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. Classical
inflammasomes consist of a signal sensor component, an adapter
(ASC/PYCARD), which recruits an effector proinflammatory caspase
(CASP1 and possibly CASP4/CASP11). 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. In NLRP1
inflammasome, the role of PYCARD is not clear. Following
activation, Nlrp1b may directly interact with CASP1 (through the
CARD domain) to form a functional inflammasome. Hence PYCARD may
not be necessary for NLRP1 and CASP1 interaction, but is required
for speck formation and full inflammasome activity (By
similarity). Homomer (By similarity). Interacts (via LRR repeats)
with BCL2 and BCL2L1 (via the loop between motifs BH4 and BH3);
these interactions reduce NLRP1 inflammasome-induced CASP1
activation and IL1B release, possibly by impairing NLRP1
interaction with PYCARD. Interacts with NOD2; this interaction may
increase IL1B release. Interacts with EIF2AK2/PKR; this
interaction requires EIF2AK2 activity, is accompanied by EIF2AK2
autophosphorylation and promotes inflammasome assembly in response
to danger-associated signals. Interacts with MEFV; this
interaction targets NLRP1 to degradation by autophagy, hence
preventing excessive IL1B- and IL18-mediated inflammation (By
similarity). {ECO:0000250|UniProtKB:Q2LKW6,
ECO:0000250|UniProtKB:Q9C000}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C000}.
Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Inflammasome
{ECO:0000250|UniProtKB:Q2LKW6}.
-!- TISSUE SPECIFICITY: Expressed in macrophages.
{ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23506131}.
-!- DOMAIN: The CARD domain is involved in the interaction with
PYCARD, CASP1 and CASP4/CASP11. {ECO:0000250|UniProtKB:Q9C000}.
-!- DOMAIN: The leucine-rich repeat (LRR) domain may be involved in
autoinhibition in the absence of activating signal, possibly
through intramolecular interaction with the NACHT domain.
{ECO:0000250|UniProtKB:Q2LKW6}.
-!- DOMAIN: The FIIND (domain with function to find) region may be
involved in homomerization, but not in CASP1-binding. Contrary to
allele 1, allele 3 does not undergo autocatalytic cleavage in this
region. {ECO:0000269|PubMed:22536155}.
-!- POLYMORPHISM: Nlrp1b gene is extremely polymorphic. 5 alleles have
been described in 18 inbred strains: 1, 2, 3, 4 and 5. These
alleles define susceptibility to Bacillus anthracis lethal toxin
(LT). Alleles 2 (carried by A/J, C57BL/6J and I/LnJ), 3 (AKR/J,
NOD/LtJ and SJL/J) or 4 (DBA/2J, P/J and SM/J) are not activated
by LT. Alleles 1 (carried by 129S1/SvImJ, BALB/cJ, C3H/HeJ, CBA/J,
FVB/NJ, NON/ShiLtJ, NZO (NZO/HlLtJ) and SWR/J strains) and 5
(CAST/EiJ) confer macrophage susceptibility to LT. In susceptible
strains, infection by Bacillus anthracis leads to IL1B release,
neutrophil recruitment and macrophage pyroptosis. This early
inflammatory response confers increased resistance to infection
(PubMed:16429160). The sequence shown in this entry is that of
allele 3 (PubMed:16429160). {ECO:0000269|PubMed:16429160,
ECO:0000303|PubMed:16429160}.
-!- MISCELLANEOUS: Three tandem Nrlp1 paralogs, Nrlp1a, Nrlp1b and
Nrlp1c, have been identified. Nlrp1c is predicted to be a
pseudogene. {ECO:0000269|PubMed:23506131,
ECO:0000305|PubMed:16429160}.
-!- MISCELLANEOUS: In macrophages and dendritic cells, NLRP1
inflammasome activation of CASP1 and IL1B maturation can be
dampened by direct contact with activated effector and memory T-
cells. This effect may be mediated by hexameric TNF ligands, such
as CD40LG. {ECO:0000250|UniProtKB:Q2LKW6}.
-!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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EMBL; DQ117594; AAZ40520.1; -; mRNA.
EMBL; DQ117595; AAZ40521.1; -; mRNA.
EMBL; DQ117596; AAZ40522.1; -; mRNA.
UniGene; Mm.390402; -.
MGI; MGI:3582959; Nlrp1b.
HOVERGEN; HBG052573; -.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0072558; C:NLRP1 inflammasome complex; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0032610; P:interleukin-1 alpha production; IMP:MGI.
GO; GO:0032611; P:interleukin-1 beta production; IDA:MGI.
GO; GO:0051402; P:neuron apoptotic process; ISO:MGI.
GO; GO:1904784; P:NLRP1 inflammasome complex assembly; ISO:MGI.
GO; GO:0030163; P:protein catabolic process; IMP:MGI.
GO; GO:0070269; P:pyroptosis; IMP:MGI.
CDD; cd08330; CARD_ASC_NALP1; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR001315; CARD.
InterPro; IPR033516; CARD8/ASC/NALP1_CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR025307; FIIND_dom.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00619; CARD; 1.
Pfam; PF13553; FIIND; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS50209; CARD; 1.
PROSITE; PS51830; FIIND; 1.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
ATP-binding; Cytoplasm; Immunity; Inflammasome; Inflammatory response;
Innate immunity; Leucine-rich repeat; Nucleotide-binding; Repeat.
CHAIN 1 1172 NACHT, LRR and PYD domains-containing
protein 1b allele 3.
/FTId=PRO_0000435105.
DOMAIN 126 435 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 627 647 LRR 1.
REPEAT 684 704 LRR 2.
DOMAIN 789 1072 FIIND. {ECO:0000255|PROSITE-
ProRule:PRU01174}.
DOMAIN 1082 1165 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
NP_BIND 132 139 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
SITE 922 923 Cleavage; by autolysis.
{ECO:0000255|PROSITE-ProRule:PRU01174}.
MUTAGEN 927 927 D->V: Restores autocatalytic cleavage, as
observed in allele 1, but not response to
anthrax lethal toxin (LT), nor to
metabolic inhibitors. Restores
autocatalytic cleavage and IL1B release
in response to LT; when associated with
A-935 and N-965.
{ECO:0000269|PubMed:22536155,
ECO:0000269|PubMed:23230290}.
MUTAGEN 935 935 D->A: No effect; when associated with N-
965. Restores autocatalytic cleavage and
IL1B release in response to anthrax
lethal toxin; when associated with V-927
and N-965. {ECO:0000269|PubMed:22536155}.
MUTAGEN 965 965 S->N: Restores autocatalytic cleavage, as
observed in allele 1, and produces
constitutive IL1B release; when
associated with V-927 and A-935.
{ECO:0000269|PubMed:22536155}.
SEQUENCE 1172 AA; 133631 MW; 8588C509568BE397 CRC64;
MEESPPKQKS NTKVAQHEGQ QDLNTTRHMN VELKHRPKLE RHLKLGMIPV VYMKQREEIL
YPAQSLKEEN LIQNFTSLPL LQKLYPKDPE NMVRKSWASC IPEEGGHMIN IQDLFGPNIG
TQKEPQLVII EGAAGIGKST LARLVKRAWK EGQLYRDHFQ HVFFFSCREL AQCKKLSLAE
LIAQGQEVPT APINQILSHP EKLLFILDGI DEPAWVLADQ NPELCLHWSQ RQPVHTLLGS
LLGKSILPEA FFLLTTRTTA LQKFIPSLPM PCQVEVLGFS GIERENYFYK YFANQRHAIT
AFMMVESNPV LLTLCEVPWV CWLVCTCLKK QMEQGRVLSL KSQTTTALCL KYPSLTIPDK
HRRTQVKALC SLAAEGIWKR RTLFSESDLC KQGLDEDAVA TFLKTGVLQK QASSLSYSFA
HLCLQEFFAA ISCILEDSEE RHGNMEMDRI VETLVERYGR QNLFEAPTVR FLFGLLGKEG
VKGMEKLFSC SLHGKTKLKL LWHILGKSQP HQPSCLGLLH CLYENQDMEL LTHVMHDLQG
TIVPGPNDIA HTVLQTNVKQ LVVQTDMELM VATFCIQFYC HVRTLQLNME KQQGYALTSP
RMVLYRWTPI TNASWEILFY NLKFTRNLEG LDLSGNSLRY SVVQSLCNTL RYPGCQLKTL
WLVKCGLTSR YCSLLASVLS AHSSLTELYL QLNDLGDDGV RMLCEGLRNP VCNLSILWLD
LSSLSAQVIT ELRTLEEKNP KLYIRSIWMP HMMVPTENMD EEAILTTFKQ QRQESGDKPM
EILGTEEDFW GPTGPVATEL VDRVRNLYRV QLPMAGSYHC PSTGLHFVVT RAVTIEIEFC
AWSQFLDKTP LQQSHMVVGP LFDIKAEQGA VTAVYLPHFV SLKDTEASTF DFKVAHFQEH
GIVLETPDRV KPGYTVLKNP SFSPMGDVLR IIPADRHFIP ITSITLIYYR LNLEEVTLHL
YLVPSDCTIQ KAIDDEEMKF QFVRINKPPP VDNLFIGSRY IVSGSENLEI TPKELELCYR
SSKEFQLFSE IYVGNMGSEI KLQIKNKKHM RLIWEALLKP GDLRPALPRI AQALKDAPSL
LHFMDQHREQ LVARVTSVDP LLDKLHGLVL NEESYEAVRA ENTNQDKMRK LFNLSRSWSR
ACKDLFYQAL KETHPHLVMD LLEKSGGVSL GS


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