NL1B4_MOUSE
ID NL1B4_MOUSE Reviewed; 906 AA.
AC Q2LKV2; Q2LK60;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=NACHT, LRR and PYD domains-containing protein 1b allele 4 {ECO:0000303|PubMed:16429160};
GN Name=Nlrp1b {ECO:0000303|PubMed:23506131};
GN Synonyms=Nalp1b {ECO:0000303|PubMed:16429160};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|EMBL:AAZ40524.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=DBA/2J, P/J, and SM/J;
RX PubMed=16429160; DOI=10.1038/ng1724;
RA Boyden E.D., Dietrich W.F.;
RT "Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin.";
RL Nat. Genet. 38:240-244(2006).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=23506131; DOI=10.1186/1471-2164-14-188;
RA Sastalla I., Crown D., Masters S.L., McKenzie A., Leppla S.H., Moayeri M.;
RT "Transcriptional analysis of the three Nlrp1 paralogs in mice.";
RL BMC Genomics 14:188-188(2013).
RN [3]
RP REVIEW.
RX PubMed=32558991; DOI=10.1111/imr.12884;
RA Taabazuing C.Y., Griswold A.R., Bachovchin D.A.;
RT "The NLRP1 and CARD8 inflammasomes.";
RL Immunol. Rev. 297:13-25(2020).
CC -!- FUNCTION: Probable inactive allele of Nlrp1b, which lacks a CARD
CC domain, suggesting that it is not able to form an inflammasome
CC (PubMed:16429160). Contrary to Nlrp1b allele 1, allele 4 is not
CC activated by B.anthracis lethal toxin and no other activation signal is
CC reported (PubMed:16429160). {ECO:0000269|PubMed:16429160}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9C000}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q2LKV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2LKV2-2; Sequence=VSP_058008, VSP_058009;
CC -!- TISSUE SPECIFICITY: Expressed in macrophages.
CC {ECO:0000269|PubMed:16429160, ECO:0000269|PubMed:23506131}.
CC -!- DOMAIN: Contrary to Nlrp1b alleles 1, 2, 3 and 5, allele 4 is missing a
CC CARD domain, which has been shown in other alleles to be involved in
CC the interaction with CASP1 and CASP4/CASP11. It is thus unclear if this
CC allele is able to promote inflammasome assembly.
CC {ECO:0000305|PubMed:16429160}.
CC -!- DOMAIN: The FIIND (domain with function to find) region may be involved
CC in homomerization, but not in CASP1-binding (PubMed:16429160). In
CC allele 4, the FIIND region is truncated and hence does not contain the
CC activating cleavage reported for allele 1 (PubMed:16429160).
CC Consequently, it may not undergo autocatalytic cleavage in this region
CC (PubMed:16429160). {ECO:0000269|PubMed:16429160}.
CC -!- POLYMORPHISM: Nlrp1b gene is extremely polymorphic. 5 alleles have been
CC described in 18 inbred strains: 1 (AC Q2LKW6), 2 (AC A1Z198), 3 (AC
CC Q2LKV5), 4 (this entry) and 5 (AC Q0GKD5). These alleles define
CC susceptibility to B.anthracis lethal toxin (LT). Alleles 2 (carried by
CC A/J, C57BL/6J and I/LnJ), 3 (AKR/J, NOD/LtJ and SJL/J) or 4 (DBA/2J,
CC P/J and SM/J) are not activated by LT. Alleles 1 (carried by
CC 129S1/SvImJ, BALB/cJ, C3H/HeJ, CBA/J, FVB/NJ, NON/ShiLtJ, NZO
CC (NZO/HlLtJ) and SWR/J strains) and 5 (CAST/EiJ) confer macrophage
CC susceptibility to LT. In susceptible strains, infection by Bacillus
CC anthracis leads to IL1B release, neutrophil recruitment and macrophage
CC pyroptosis. This early inflammatory response confers increased
CC resistance to infection (PubMed:16429160). The sequence shown in this
CC entry is that of allele 4 (PubMed:16429160).
CC {ECO:0000269|PubMed:16429160, ECO:0000303|PubMed:16429160}.
CC -!- MISCELLANEOUS: Three tandem Nrlp1 paralogs, Nrlp1a, Nrlp1b and Nrlp1c,
CC have been identified. Nlrp1c is predicted to be a pseudogene.
CC {ECO:0000269|PubMed:23506131, ECO:0000305|PubMed:16429160}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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DR EMBL; DQ117597; AAZ40523.1; -; mRNA.
DR EMBL; DQ117598; AAZ40524.1; -; mRNA.
DR EMBL; DQ117599; AAZ40525.1; -; mRNA.
DR EMBL; DQ153215; AAZ40530.1; -; mRNA.
DR AlphaFoldDB; Q2LKV2; -.
DR SMR; Q2LKV2; -.
DR IntAct; Q2LKV2; 1.
DR MEROPS; S79.A03; -.
DR PRIDE; Q2LKV2; -.
DR MGI; MGI:3582959; Nlrp1b.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0061702; C:inflammasome complex; ISO:MGI.
DR GO; GO:0072558; C:NLRP1 inflammasome complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0140608; F:cysteine-type endopeptidase activator activity; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0140374; P:antiviral innate immune response; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:MGI.
DR GO; GO:1904784; P:NLRP1 inflammasome complex assembly; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0070269; P:pyroptosis; IMP:MGI.
DR GO; GO:0097264; P:self proteolysis; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR025307; FIIND_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13553; FIIND; 1.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51830; FIIND; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cytoplasm; Leucine-rich repeat;
KW Nucleotide-binding; Repeat.
FT CHAIN 1..906
FT /note="NACHT, LRR and PYD domains-containing protein 1b
FT allele 4"
FT /id="PRO_0000435106"
FT DOMAIN 126..435
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT REPEAT 627..647
FT /note="LRR 1"
FT REPEAT 684..704
FT /note="LRR 2"
FT DOMAIN 789..906
FT /note="FIIND (incomplete)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01174"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT VAR_SEQ 718..730
FT /note="WLDLSSLSAQVIT -> CRKSGSDVSMHRN (in isoform 2)"
FT /id="VSP_058008"
FT VAR_SEQ 731..906
FT /note="Missing (in isoform 2)"
FT /id="VSP_058009"
SQ SEQUENCE 906 AA; 103119 MW; 53B983107BE268FF CRC64;
MEESPPKQKS NTKVAQHEGQ QDLNTTRHMN VELKHRPKLE RHLKLGMIPV VYMKQREEIL
YPAQSLKEEN LIQNFTSLPL LQKLCPKDPE NMVRKSWASC IPEEGGHMIN IQDLFGPNIG
TQKEPQLVII EGAAGIGKST LARLVKRAWK EGQLYRDHFQ HVFFFSCREL AQCKKLSLAE
LIAQGQEVPT APINQILSHP EKLLFILDGI DEPAWVLADQ NPELCLHWSQ RQPVHTLLGS
LLGKSILPEA FFLLTTRTTA LQKFIPSLPM PCQVEVLGFS GIEWENYFYK YFANQRHAIT
AFMMVESNPV LLTLCEVPWV CWLVCTCLKK QMKQGRVLSL KSQTTTALCL KYLSLTIPDK
HRRTQVKALC SLAAEGIWKR RTLFSESDLC KQGLDEDAVA TFLKTGVLQK QASSLSYSFA
HLCLQEFFAA ISCILEDSEE RHGNMEMDRI VETLVERYGR QNLFEAPTVR FLFGLLGKEG
VKGMEKLFSC SLPGKTKLKL LWHILGKSQP HQPPCLGLLH 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 DFKVTHFQEH
GSRNAR
