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NACHT, LRR and PYD domains-containing protein 1b allele 5

 NL1B5_MOUSE             Reviewed;        1196 AA.
Q0GKD5; Q2LKV0;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
03-OCT-2006, sequence version 1.
20-JUN-2018, entry version 71.
RecName: Full=NACHT, LRR and PYD domains-containing protein 1b allele 5 {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 {ECO:0000312|EMBL:ABI18116.1};
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND MISCELLANEOUS.
STRAIN=129S1/SvImJ;
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]
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).
[3]
ACTIVATION BY ANTHRAX LETHAL TOXIN AND METABOLIC INHIBITORS.
PubMed=24935976; DOI=10.1128/IAI.02167-14;
Neiman-Zenevich J., Liao K.C., Mogridge J.;
"Distinct regions of NLRP1B are required to respond to anthrax lethal
toxin and metabolic inhibition.";
Infect. Immun. 82:3697-3703(2014).
-!- 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. Activated by cleavage
by Bacillus anthracis lethal toxin (LT) endopeptidase component.
Activated by metabolic inhibitors, such as 2-deoxy-D-glucose and
sodium azide (PubMed:24935976). Not activated by muramyl
dipeptide, nor by full-length bacterial peptidoglycan. Primary
mediator of macrophage susceptibility to LT. In response to
Bacillus anthracis infection, macrophages and dendritic cells
release IL1B and undergo pyroptosis, an inflammatory form of
programmed cell death. This early inflammatory response to the
toxin increases resistance to infection by B. anthracis spores.
Binds ATP. {ECO:0000250|UniProtKB:Q2LKW6,
ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:16429160,
ECO:0000269|PubMed:24935976}.
-!- 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 (By similarity). Interacts with NOD2; this
interaction may lead to increased IL1B release (By similarity).
Interacts with EIF2AK2/PKR; this interaction requires EIF2AK2
activity, is accompanied by EIF2AK2 autophosphorylation and
promotes inflammasome assembly in response to Bacillus anthracis
lethal toxin (By similarity). 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q0GKD5-1; Sequence=Displayed;
Name=2;
IsoId=Q0GKD5-2; Sequence=VSP_058010;
-!- 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 is
involved in homomerization, but not in CASP1-binding.
Autocatalytic cleavage in this region occurs constitutively, prior
to activation signals, and is required for inflammasome activity
(IL1B release), possibly by facilitating CASP1 binding. Both
N- and C-terminal fragments remain associated.
{ECO:0000250|UniProtKB:Q2LKW6}.
-!- 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 1 (carried by strains 129S1/SvImJ, BALB/cJ, C3H/HeJ,
CBA/J, FVB/NJ, NON/ShiLtJ, NZO (NZO/HlLtJ) and SWR/J) and 5
(CAST/EiJ) confer macrophage susceptibility to LT. Strains with
macrophages resistant to anthrax LT carry alleles 2 (A/J, C57BL/6J
and I/LnJ), 3 (AKR/J, NOD/LtJ and SJL/J) or 4 (DBA/2J, P/J and
SM/J). Sensitivity to LT leads to IL1B release, macrophage
pyroptosis and neutrophil recruitment. This early inflammatory
response confers increased resistance to infection by B. anthracis
spores (PubMed:16429160). The sequence shown in this entry is that
of allele 5 (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. Neither Nlrp1a, nor Nrlp1c are expressed in anthrax
lethal toxin susceptible strains, hence neither of them is thought
to play an important role in this phenotype.
{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; DQ117600; AAZ40526.1; -; mRNA.
EMBL; DQ860103; ABI18116.1; -; mRNA.
EMBL; DQ860104; ABI18117.1; -; mRNA.
UniGene; Mm.390402; -.
MEROPS; S79.002; -.
PRIDE; Q0GKD5; -.
Ensembl; ENSMUST00000229006; ENSMUSP00000155822; ENSMUSG00000116526. [Q0GKD5-2]
Ensembl; ENSMUST00000229032; ENSMUSP00000154954; ENSMUSG00000116526. [Q0GKD5-1]
Ensembl; ENSMUST00000229202; ENSMUSP00000155297; ENSMUSG00000116526. [Q0GKD5-2]
Ensembl; ENSMUST00000230890; ENSMUSP00000155728; ENSMUSG00000116526. [Q0GKD5-1]
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.
Pfam; PF05729; NACHT; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS50209; CARD; 1.
PROSITE; PS51830; FIIND; 1.
PROSITE; PS50837; NACHT; 1.
2: Evidence at transcript level;
Alternative splicing; ATP-binding; Cytoplasm; Immunity; Inflammasome;
Inflammatory response; Innate immunity; Leucine-rich repeat;
Nucleotide-binding; Repeat.
CHAIN 1 1196 NACHT, LRR and PYD domains-containing
protein 1b allele 5.
/FTId=PRO_0000435107.
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 1106 1189 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
NP_BIND 132 139 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
SITE 44 45 Probable cleavage; by anthrax lethal
toxin endopeptidase component.
{ECO:0000250|UniProtKB:Q2LKW6}.
SITE 922 923 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:Q9C000,
ECO:0000255|PROSITE-ProRule:PRU01174}.
VAR_SEQ 1061 1084 Missing (in isoform 2).
/FTId=VSP_058010.
SEQUENCE 1196 AA; 136518 MW; E7AE9B4DA716D0A0 CRC64;
MEESPPKQKS NTKVTQHEGQ QDLNTTRHMN VELKHRPKLE RHLKLGMIPV VYMKQGEEIL
YPAQSLREEN LIQNFTSLLL LQKLCPKDPE NMVRKSWASC VPEEGGHMIN IQDLFGPNIG
TQKEPQLVII EGAAGIGKST LARLVKRAWK EGQLYRDHFQ HVFFFSCREL AQCKKLSLAE
LIAQGQEVPT APINQILSHP EKLLFILDGI DEPAWVLADQ NPELCLHWSQ RQPVHTLLGS
LLGKSIFPEA FFLLTTRTTA LQKFIPSLPM PCQVEVLGFS GIERENYFYK YFANQRHAIT
AFMMVESNPV LLTLCEVPWV CWLVCTCLKK QMEQGRVLSL KSQTTTALCL KYLSLTIPDK
HRRTQVKALC SLAAEGIWKR RTLFSESDLC KQGLDEDAVA TFLKTGVLQK QASSLSYSFA
HLCLQEFFAA ISCILEDSEE RHGNMEMDRI VETLVERYGR QNLFEAPTVR FLFGLLGKEG
VKGMEKLFSC SLHGKTNLKL LWHILVKSQP HQPPCLGLLH CLYENQDMEL LTHVMHDLQG
TIVPGPNDIA HTVLQTNVKH LVVQTDMELM VATFCIQFYC HVRTLQLNME KQQGYALISP
RMVLYRWTPI TNASWEILFY NLKFTRNLEG LDLSGNSLRY SVVQSLCNTL RYPGCQLKTL
WLVKCGLTSR HCSLLASVLS AHSSLTELYL QLNDLGDDGV RMLCEGLRNP VCNLSILWLD
LYSLSAQVIT ELRTLEEKNP KLYIRSIWMP HMMVPTENMD EEAILTTFKQ QRQEPGDKPM
EILGTEEDFW GPTGPVATEL VDRVRNLYRV QLPMAGSYHC PSTGLHFVVT RAVTIEIEFC
AWSQFLDKTP LQQSHMVVGP LFDIKAEQGA VTAVYLPHFV SLKDTEASTF DFKVAHFQEH
GMVLETPDRV KPGYTVLKNP SFSPMGVVLR IIPAARHFIP ITSITLIYYR LNLEEVTLHL
YLVPNDCTIQ KAIDDEEMKF QFVRINKPPP VDNLFIGSRY IVSGSENLEI TPKELELCYR
SSKEFQLFSE IYVGNMGSEI KLQIKNKKHM KLIWEALLKP EFKFDHLCDQ EFCTILKNIM
ISPAGDLRPA LPRIAQALKD APSLLHFMDQ HREQLVARVT SVDPLLDKLH GLVLNEESYE
AVRAENTNQD KMRKLFNLSR SWSRACKDLF YQALKETHPH LVMDLFEKSG GVSLGS


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