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

 NL1B1_MOUSE             Reviewed;        1233 AA.
Q2LKW6;
09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
21-FEB-2006, sequence version 1.
22-NOV-2017, entry version 83.
RecName: Full=NACHT, LRR and PYD domains-containing protein 1b allele 1 {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=129S1/SvImJ, BALB/cJ, C3H/HeJ, CBA/J, FVB/NJ, NON/ShiLtJ, NZO,
and SWR/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]
SUBCELLULAR LOCATION, ACTIVATION BY ANTHRAX LETHAL TOXIN, AND
INFLAMMASOME ASSEMBLY.
PubMed=19124602; DOI=10.1128/IAI.01032-08;
Nour A.M., Yeung Y.G., Santambrogio L., Boyden E.D., Stanley E.R.,
Brojatsch J.;
"Anthrax lethal toxin triggers the formation of a membrane-associated
inflammasome complex in murine macrophages.";
Infect. Immun. 77:1262-1271(2009).
[3]
FUNCTION, INTERACTION WITH CASP1, HOMOMERIZATION, ACTIVATION BY
ANTHRAX LETHAL TOXIN, AND DOMAIN.
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).
[4]
INHIBITION OF INFLAMMASOME RESPONSE.
PubMed=19494813; DOI=10.1038/nature08100;
Guarda G., Dostert C., Staehli F., Cabalzar K., Castillo R.,
Tardivel A., Schneider P., Tschopp J.;
"T cells dampen innate immune responses through inhibition of NLRP1
and NLRP3 inflammasomes.";
Nature 460:269-273(2009).
[5]
FUNCTION, AND ACTIVATION BY ANTHRAX LETHAL TOXIN.
PubMed=19949100; DOI=10.4049/jimmunol.0903114;
Terra J.K., Cote C.K., France B., Jenkins A.L., Bozue J.A.,
Welkos S.L., LeVine S.M., Bradley K.A.;
"Resistance to Bacillus anthracis infection mediated by a lethal toxin
sensitive allele of Nalp1b/Nlrp1b.";
J. Immunol. 184:17-20(2010).
[6]
FUNCTION, ACTIVATION BY ANTHRAX LETHAL TOXIN, AND POLYMORPHISM.
PubMed=21170303; DOI=10.1371/journal.ppat.1001222;
Moayeri M., Crown D., Newman Z.L., Okugawa S., Eckhaus M.,
Cataisson C., Liu S., Sastalla I., Leppla S.H.;
"Inflammasome sensor Nlrp1b-dependent resistance to anthrax is
mediated by caspase-1, IL-1 signaling and neutrophil recruitment.";
PLoS Pathog. 6:E1001222-E1001222(2010).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22753929; DOI=10.4049/jimmunol.1201065;
Kovarova M., Hesker P.R., Jania L., Nguyen M., Snouwaert J.N.,
Xiang Z., Lommatzsch S.E., Huang M.T., Ting J.P., Koller B.H.;
"NLRP1-dependent pyroptosis leads to acute lung injury and morbidity
in mice.";
J. Immunol. 189:2006-2016(2012).
[8]
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).
[9]
HOMOMERIZATION, SUBUNIT, AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF
VAL-988; ALA-996; VAL-1012; GLN-1014; ASN-1026; 1100-GLU--LYS-1106 AND
LYS-1112.
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).
[10]
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).
[11]
ACTIVATION BY ANTHRAX LETHAL TOXIN AND METABOLIC INHIBITORS, AND
MUTAGENESIS OF 137-GLY--SER-139.
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).
[12]
FUNCTION, CLEAVAGE BY ANTHRAX LETHAL TOXIN, AUTOCATALYTIC CLEAVAGE,
AND MUTAGENESIS OF 34-LYS--ARG-36; 37-PRO--LEU-39; 38-LYS-LEU-39;
LEU-43; LYS-44; LEU-45; 626-ARG--LEU-719 AND SER-984.
PubMed=23818853; DOI=10.1371/journal.ppat.1003452;
Chavarria-Smith J., Vance R.E.;
"Direct proteolytic cleavage of NLRP1B is necessary and sufficient for
inflammasome activation by anthrax lethal factor.";
PLoS Pathog. 9:E1003452-E1003452(2013).
[13]
ACTIVATION BY TOXOPLASMA GONDII.
PubMed=24218483; DOI=10.1128/IAI.01170-13;
Ewald S.E., Chavarria-Smith J., Boothroyd J.C.;
"NLRP1 is an inflammasome sensor for Toxoplasma gondii.";
Infect. Immun. 82:460-468(2014).
[14]
ACTIVATION BY ANTHRAX LETHAL TOXIN AND METABOLIC INHIBITORS,
MUTAGENESIS OF 1-MET--GLU-40; 1-MET--LYS-44; 1-MET--VAL-50;
43-LEU--LEU-45; GLU-629; ASP-632; SER-634; GLN-644; ASN-648; ARG-651;
LYS-658; THR-659; TRP-661; VAL-663; LYS-664; ARG-670; SER-673;
THR-686; GLU-687; TYR-689; GLN-691; ASP-698; ARG-701; MET-702;
GLU-705; ASP-720; THR-734; LYS-738; ILE-744; SER-746; 749-MET--ARG-809
AND 810-MET--ARG-870, AND DOMAIN.
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).
[15]
FUNCTION, ACTIVATION BY ANTHRAX LETHAL TOXIN, INFLAMMASOME ASSEMBLY,
AND SUBCELLULAR LOCATION.
PubMed=24492532; DOI=10.1038/ncomms4209;
Van Opdenbosch N., Gurung P., Vande Walle L., Fossoul A.,
Kanneganti T.D., Lamkanfi M.;
"Activation of the NLRP1b inflammasome independently of ASC-mediated
caspase-1 autoproteolysis and speck formation.";
Nat. Commun. 5:3209-3209(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 (PubMed:19651869,
PubMed:21170303, PubMed:22753929, PubMed:22536155,
PubMed:23818853). Activated by cleavage by Bacillus anthracis
lethal toxin (LT) endopeptidase component (PubMed:19124602,
PubMed:19651869, PubMed:19949100, PubMed:22536155,
PubMed:23818853,PubMed:24935976, PubMed:24492532). Activated by
metabolic inhibitors, such as 2-deoxy-D-glucose and sodium azide,
by nutrient deprivation and hypoxia, possibly due to a decrease in
cytosolic ATP (PubMed:23230290, PubMed:24935976). Also activated
by Toxoplasma gondii (PubMed:24218483). Not activated by muramyl
dipeptide, nor by full-length bacterial peptidoglycan
(PubMed:22753929). 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 (PubMed:16429160,
PubMed:19949100, PubMed:21170303, PubMed:22753929,
PubMed:23818853). Binds ATP (By similarity).
{ECO:0000250|UniProtKB:Q9C000, ECO:0000269|PubMed:16429160,
ECO:0000269|PubMed:19124602, ECO:0000269|PubMed:19651869,
ECO:0000269|PubMed:19949100, ECO:0000269|PubMed:21170303,
ECO:0000269|PubMed:22536155, ECO:0000269|PubMed:22753929,
ECO:0000269|PubMed:23230290, ECO:0000269|PubMed:23818853,
ECO:0000269|PubMed:24218483, ECO:0000269|PubMed:24492532,
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 (PubMed:19124602,
PubMed:19651869, PubMed:24492532). Hence PYCARD may not be
necessary for NLRP1 and CASP1 interaction, but is required for
speck formation and full inflammasome activity (PubMed:19651869,
PubMed:24492532). Homomer (PubMed:19651869, PubMed:22536155).
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 increase 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 (PubMed:22801494). Interacts
with MEFV; this interaction targets NLRP1 to degradation by
autophagy, hence preventing excessive IL1B- and IL18-mediated
inflammation (By similarity). {ECO:0000250|UniProtKB:Q9C000,
ECO:0000269|PubMed:19124602, ECO:0000269|PubMed:19651869,
ECO:0000269|PubMed:22536155, ECO:0000269|PubMed:24492532}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19124602}.
Cytoplasm, cytosol {ECO:0000269|PubMed:19124602}. Inflammasome
{ECO:0000269|PubMed:24492532}. Membrane
{ECO:0000269|PubMed:19124602}.
-!- TISSUE SPECIFICITY: Widely expressed, including 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:0000269|PubMed:19651869, ECO:0000269|PubMed:23818853,
ECO:0000269|PubMed:24935976}.
-!- DOMAIN: The FIIND (domain with function to find) region is
involved in homomerization, but not in CASP1-binding
(PubMed:22536155). 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
(PubMed:22536155, PubMed:23818853). {ECO:0000269|PubMed:22536155,
ECO:0000269|PubMed:23818853}.
-!- 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, PubMed:19949100, PubMed:21170303). The
sequence shown in this entry is that of allele 1
(PubMed:16429160). {ECO:0000269|PubMed:16429160,
ECO:0000269|PubMed:19949100, ECO:0000269|PubMed:21170303,
ECO:0000303|PubMed:16429160}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under usual housing
conditions. When challenged with intratracheal instillation of
Bacillus anthracis lethal toxin (LT), mutant animals are protected
from lung damages caused by sustained inflammation. Macrophages
isolated from mutant animals are resistant LT.
{ECO:0000269|PubMed:22753929}.
-!- 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:0000269|PubMed:19494813}.
-!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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EMBL; DQ117583; AAZ40509.1; -; mRNA.
EMBL; DQ117584; AAZ40510.1; -; mRNA.
EMBL; DQ117585; AAZ40511.1; -; mRNA.
EMBL; DQ117586; AAZ40512.1; -; mRNA.
EMBL; DQ117587; AAZ40513.1; -; mRNA.
EMBL; DQ117588; AAZ40514.1; -; mRNA.
EMBL; DQ117589; AAZ40515.1; -; mRNA.
EMBL; DQ117590; AAZ40516.1; -; mRNA.
UniGene; Mm.390402; -.
IntAct; Q2LKW6; 1.
MGI; MGI:3582959; Nlrp1b.
HOVERGEN; HBG052573; -.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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.
InterPro; IPR001315; CARD.
InterPro; IPR033516; CARD8/ASC/NALP1_CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR025307; FIIND_dom.
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; PS51450; LRR; 2.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
ATP-binding; Cytoplasm; Immunity; Inflammasome; Inflammatory response;
Innate immunity; Leucine-rich repeat; Membrane; Nucleotide-binding;
Repeat.
CHAIN 1 1233 NACHT, LRR and PYD domains-containing
protein 1b allele 1.
/FTId=PRO_0000435103.
DOMAIN 126 435 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 627 647 LRR 1.
REPEAT 684 704 LRR 2.
DOMAIN 850 1133 FIIND. {ECO:0000255|PROSITE-
ProRule:PRU01174}.
DOMAIN 1143 1226 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 (LT) endopeptidase component.
{ECO:0000305|PubMed:23818853}.
SITE 983 984 Cleavage; by autocatalysis.
{ECO:0000250|UniProtKB:Q9C000,
ECO:0000255|PROSITE-ProRule:PRU01174}.
MUTAGEN 1 50 Missing: Low spontaneous IL1B release and
loss of activation by LT. Increased IL1B
release in response to metabolic
inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 1 44 Missing: Low spontaneous IL1B release and
loss of activation by LT. No effect on
activation by metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 1 40 Missing: No effect on IL1B release.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 34 36 KHR->AAA: No effect on cleavage by LT,
nor on IL1B processing. No effect on
cleavage by LT, nor on IL1B processing;
when associated with 38-A-A-39.
{ECO:0000269|PubMed:23818853}.
MUTAGEN 37 39 PKL->QAQ: No effect on cleavage by LT.
{ECO:0000269|PubMed:23818853}.
MUTAGEN 38 39 KL->AA: No effect on cleavage by LT, nor
on IL1B processing.
{ECO:0000269|PubMed:23818853}.
MUTAGEN 43 43 L->Q: Loss of cleavage by LT and of LT-
induced IL1B processing and suppression
of LT-induced pyroptosis in macrophages,
no effect on IL1B release in response to
metabolic inhibitors; when associated
with A-44 and Q-45.
{ECO:0000269|PubMed:23818853,
ECO:0000269|PubMed:24935976}.
MUTAGEN 44 44 K->A: Partial loss of cleavage by LT and
of LT-induced IL1B processing. Loss of
cleavage by LT and of LT-induced IL1B
processing; when associated with Q-43 and
Q-45. No effect on IL1B release in
response to metabolic inhibitors; when
associated with Q-43 and Q-45.
{ECO:0000269|PubMed:23818853,
ECO:0000269|PubMed:24935976}.
MUTAGEN 45 45 L->Q: Loss of cleavage by LT and of LT-
induced IL1B processing. Loss of cleavage
by LT and of LT-induced IL1B processing;
when associated with Q-43 and A-44. No
effect on IL1B release in response to
metabolic inhibitors; when associated
with Q-43 and A-44.
{ECO:0000269|PubMed:23818853,
ECO:0000269|PubMed:24935976}.
MUTAGEN 137 139 GKS->AAA: Constitutive IL1B release.
{ECO:0000269|PubMed:23230290}.
MUTAGEN 626 719 Missing: Constitutive IL1B processing.
{ECO:0000269|PubMed:23818853}.
MUTAGEN 629 629 E->A: Increased IL1B release under basal
conditions. No effect on IL1B release in
response to LT or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 632 632 D->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors and to LT; when
associated with A-634.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 634 634 S->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors and to LT; when
associated with A-632.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 644 644 Q->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 648 648 N->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 651 651 R->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 658 658 K->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors and to LT; when
associated with A-659.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 659 659 T->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors and to LT; when
associated with A-658.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 661 661 W->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 663 663 V->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors, no effect on the
response to LT; when associated with A-
664. {ECO:0000269|PubMed:24935976}.
MUTAGEN 664 664 K->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors, no effect on the
response to LT; when associated with A-
663. {ECO:0000269|PubMed:24935976}.
MUTAGEN 670 670 R->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 673 673 S->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 686 686 T->A: Spontaneous IL1B release under
basal conditions, no effect on the
response to metabolic inhibitors, partial
loss of response to LT; when associated
with A-687.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 687 687 E->A: Spontaneous IL1B release under
basal conditions, no effect on the
response to metabolic inhibitors, partial
loss of response to LT; when associated
with A-686.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 689 689 Y->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 691 691 Q->A: Low spontaneous IL1B release, no
effect on the response to metabolic
inhibitors, nor to LT.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 698 698 D->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors; when associated
with A-701 and A-702.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 701 701 R->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors; when associated
with A-698 and A-702.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 702 702 M->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors; when associated
with A-698 and A-701.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 705 705 E->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 720 720 D->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors and to LT.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 727 727 Q->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 731 731 E->A: Increased IL1B release under basal
conditions. No effect on IL1B release in
response to LT or metabolic inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 734 734 T->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors; when associated
with A-738.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 738 738 K->A: No effect on IL1B release under
basal conditions, nor in response to LT
or metabolic inhibitors; when associated
with A-734.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 744 744 I->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors and to LT; when
associated with A-746.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 746 746 S->A: Spontaneous IL1B release under
basal conditions, loss of response to
metabolic inhibitors and to LT; when
associated with A-744.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 749 809 Missing: No effect on response to LT,
attenuated response to metabolic
inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 810 870 Missing: No effect on response to LT,
attenuated response to metabolic
inhibitors.
{ECO:0000269|PubMed:24935976}.
MUTAGEN 984 984 S->A: Loss of autocatalytic cleavage
within the FIIND region. No effect on
cleavage by LT.
{ECO:0000269|PubMed:23818853}.
MUTAGEN 988 988 V->D: Loss of autocatalytic cleavage
within the FIIND region and of IL1B
release, decrease in CASP1-binding. No
effect on homomerization.
{ECO:0000269|PubMed:22536155}.
MUTAGEN 996 996 A->D: Strong decrease of IL1B release,
but no effect on autocatalytic cleavage
within the FIIND region.
{ECO:0000269|PubMed:22536155}.
MUTAGEN 1012 1012 V->L: No effect on autocatalytic cleavage
within the FIIND region.
{ECO:0000269|PubMed:22536155}.
MUTAGEN 1014 1014 Q->L: No effect on autocatalytic cleavage
within the FIIND region.
{ECO:0000269|PubMed:22536155}.
MUTAGEN 1026 1026 N->S: Decrease of IL1B release, but no
effect on autocatalytic cleavage within
the FIIND region.
{ECO:0000269|PubMed:22536155}.
MUTAGEN 1100 1106 EIKLQIK->AAAAAAA: Loss of homomerization,
of autocatalytic cleavage within the
FIIND region and of IL1B release. No
effect on CASP1-binding.
{ECO:0000269|PubMed:22536155}.
MUTAGEN 1112 1112 K->R: No effect on autocatalytic cleavage
within the FIIND region.
{ECO:0000269|PubMed:22536155}.
SEQUENCE 1233 AA; 140688 MW; ECB340C9A58BAFCD CRC64;
MEESPPKQKS NTKVAQHEGQ QDLNTTRHMN VELKHRPKLE RHLKLGMIPV VYMKQGEEIL
YPAQSLREEN LIQNFTSLLL LQKLCPKDPE NMIRKSWASC VPEEGGHMIN IQDLFGPNIG
TQKEPQLVII EGAAGIGKST LARLVKRAWK EGQLYRDHFQ HVFFFSCREL AQCKKLSLAE
LIAQGQEVPT APINQILSHP EKLLFILDGI DEPAWVLADQ NPELCLHWSQ RQPVHTLLGS
LLGKSILPEA 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
TIVPGPNDTA HTVLQTNVKH LVVQTDMELM VATFCIQFYC HVRTLQLNME KQQGYALISP
RMVLYRWTPI TNASWEILFY NLKFTRNLEG LDLSGNSLRY SVVQSLCNTL RYPGCQLKTL
WLVKCGLTSR YCSLLASVLS AHSSLTELYL QLNDLGDDGV RMLCEGLRNP VCNLSILWLD
LSSLSAQVIT ELRTLEEKNP KLYIRSIWMP HMMVPTENMD EEAILTTLKQ QRQESGDKPM
EILGTEEDFW GPTGPVATEL VDRVRNLYRM PQMMVPTENM DEEDILTSFK QQRQQSGANP
MEILGTEEDF WGPIGPVATE VVYRERNLYR VQLPMAGSYH CPSTRLHFVV TRAVTIEIEF
CAWSQFLDKT PLQQSHMVVG PLFDIKAEQG AVTAVYLPHF VSLKDTKAST FDFKVAHFQE
HGMVLETPDR VKPGYTVLKN PSFSPMGVVL RIIPAARHFI PITSITLIYY RVNQEEVTLH
LYLVPNDCTI QKAIDDEEMK FQFVRINKPP PVDNLFIGSR YIVSGSENLE ITPKELELCY
RSSKEFQLFS EIYVGNMGSE IKLQIKNKKH MKLIWEALLK PGDLRPALPR IAQALKDAPS
LLHFMDQHRE QLVARVTSVD PLLDKLHGLV LNEESYEAVR AENTNQDKMR KLFNLSRSWS
RACKDLFYQA LKETHPHLVM DLLEKSGGVS LGS


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