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NACHT, LRR and PYD domains-containing protein 1 (Caspase recruitment domain-containing protein 7) (Death effector filament-forming ced-4-like apoptosis protein) (Nucleotide-binding domain and caspase recruitment domain)

 NLRP1_HUMAN             Reviewed;        1473 AA.
Q9C000; E9PE50; I6L9D9; Q9BZZ8; Q9BZZ9; Q9H5Z7; Q9H5Z8; Q9HAV8;
Q9UFT4; Q9Y2E0;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
27-SEP-2017, entry version 186.
RecName: Full=NACHT, LRR and PYD domains-containing protein 1;
AltName: Full=Caspase recruitment domain-containing protein 7;
AltName: Full=Death effector filament-forming ced-4-like apoptosis protein;
AltName: Full=Nucleotide-binding domain and caspase recruitment domain;
Name=NLRP1;
Synonyms=CARD7, DEFCAP, KIAA0926, NAC {ECO:0000303|PubMed:11113115},
NALP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS HIS-155; SER-246;
MET-878; VAL-1119; VAL-1184; LEU-1241 AND CYS-1366.
PubMed=11270363; DOI=10.1038/sj.cdd.4400774;
Bertin J., DiStefano P.S.;
"The PYRIN domain: a novel motif found in apoptosis and inflammation
proteins.";
Cell Death Differ. 7:1273-1274(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=11250163; DOI=10.1016/S0960-9822(01)00056-2;
Martinon F., Hofmann K., Tschopp J.;
"The pyrin domain: a possible member of the death domain-fold family
implicated in apoptosis and inflammation.";
Curr. Biol. 11:R118-R120(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND MUTAGENESIS OF
LYS-340.
TISSUE=Erythroleukemia;
PubMed=11076957; DOI=10.1074/jbc.M009853200;
Hlaing T., Guo R.-F., Dilley K.A., Loussia J.M., Morrish T.A.,
Shi M.M., Vincenz C., Ward P.A.;
"Molecular cloning and characterization of DEFCAP-L and -S, two
isoforms of a novel member of the mammalian Ced-4 family of apoptosis
proteins.";
J. Biol. Chem. 276:9230-9238(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
TISSUE=T-cell;
PubMed=11113115; DOI=10.1074/jbc.M006309200;
Chu Z.-L., Pio F., Xie Z., Welsh K., Krajewska M., Krajewski S.,
Godzik A., Reed J.C.;
"A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-
dependent caspase activation and apoptosis.";
J. Biol. Chem. 276:9239-9245(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10231032; DOI=10.1093/dnares/6.1.63;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:63-70(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-1473 (ISOFORM 1), AND
VARIANT VAL-1184.
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[10]
PROTEIN SEQUENCE OF 1213-1224, FUNCTION, INTERACTION WITH PYCARD,
INVOLVEMENT IN INFLAMMASOME COMPLEX, AUTOCATALYTIC CLEAVAGE,
SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS VAL-1119 AND
VAL-1184, AND MUTAGENESIS OF SER-1211; PHE-1212; SER-1213 AND
PRO-1214.
PubMed=22665479; DOI=10.1074/jbc.M112.378323;
Finger J.N., Lich J.D., Dare L.C., Cook M.N., Brown K.K.,
Duraiswami C., Bertin J.J., Bertin J., Gough P.J.;
"Autolytic proteolysis within the function to find domain (FIIND) is
required for NLRP1 inflammasome activity.";
J. Biol. Chem. 287:25030-25037(2012).
[11]
ERRATUM.
Finger J.N., Lich J.D., Dare L.C., Cook M.N., Brown K.K.,
Duraiswami C., Bertin J.J., Bertin J., Gough P.J.;
J. Biol. Chem. 287:31456-31456(2012).
[12]
FUNCTION, INTERACTION WITH CASP1; CASP5 AND PYCARD, AUTOINHIBITION,
AND IDENTIFICATION IN INFLAMMASOME COMPLEX.
PubMed=12191486; DOI=10.1016/S1097-2765(02)00599-3;
Martinon F., Burns K., Tschopp J.;
"The inflammasome: a molecular platform triggering activation of
inflammatory caspases and processing of proIL-beta.";
Mol. Cell 10:417-426(2002).
[13]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15285719; DOI=10.1042/BJ20040867;
Sanz C., Calasanz M.J., Andreu E., Richard C., Prosper F.,
Fernandez-Luna J.L.;
"NALP1 is a transcriptional target for cAMP-response-element-binding
protein (CREB) in myeloid leukaemia cells.";
Biochem. J. 384:281-286(2004).
[14]
FUNCTION, AND MUTAGENESIS OF 339-GLY-LYS-340.
PubMed=15212762; DOI=10.1016/j.cellsig.2004.02.006;
Liu F., Lo C.F., Ning X., Kajkowski E.M., Jin M., Chiriac C.,
Gonzales C., Naureckiene S., Lock Y.-W., Pong K., Zaleska M.M.,
Jacobsen J.S., Silverman S., Ozenberger B.A.;
"Expression of NALP1 in cerebellar granule neurons stimulates
apoptosis.";
Cell. Signal. 16:1013-1021(2004).
[15]
FUNCTION, INTERACTION WITH BCL2; BCL2L1; CASP5 AND PYCARD, SUBCELLULAR
LOCATION, AND ACTIVATION BY MDP.
PubMed=17418785; DOI=10.1016/j.cell.2007.01.045;
Bruey J.M., Bruey-Sedano N., Luciano F., Zhai D., Balpai R., Xu C.,
Kress C.L., Bailly-Maitre B., Li X., Osterman A., Matsuzawa S.,
Terskikh A.V., Faustin B., Reed J.C.;
"Bcl-2 and Bcl-XL regulate proinflammatory caspase-1 activation by
interaction with NALP1.";
Cell 129:45-56(2007).
[16]
INTERACTION WITH MEFV.
PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
Grutter C., Grutter M., Tschopp J.;
"The SPRY domain of Pyrin, mutated in familial Mediterranean fever
patients, interacts with inflammasome components and inhibits proIL-
1beta processing.";
Cell Death Differ. 14:1457-1466(2007).
[17]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17164409; DOI=10.1369/jhc.6A7101.2006;
Kummer J.A., Broekhuizen R., Everett H., Agostini L., Kuijk L.,
Martinon F., van Bruggen R., Tschopp J.;
"Inflammasome components NALP 1 and 3 Show distinct but separate
expression profiles in human tissues suggesting a site-specific role
in the inflammatory response.";
J. Histochem. Cytochem. 55:443-452(2007).
[18]
FUNCTION, INTERACTION WITH CASP1, AUTOINHIBITION, HOMOMERIZATION, AND
ACTIVATION BY MDP.
PubMed=17349957; DOI=10.1016/j.molcel.2007.01.032;
Faustin B., Lartigue L., Bruey J.-M., Luciano F., Sergienko E.,
Bailly-Maitre B., Volkmann N., Hanein D., Rouiller I., Reed J.C.;
"Reconstituted NALP1 inflammasome reveals two-step mechanism of
caspase-1 activation.";
Mol. Cell 25:713-724(2007).
[19]
FUNCTION, INTERACTION WITH NOD2, AND ACTIVATION BY MDP.
PubMed=18511561; DOI=10.1073/pnas.0802726105;
Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S.,
Humke E.W., Eckmann L., Powell J.J., Nizet V., Dixit V.M., Karin M.;
"A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion
in response to Bacillus anthracis infection and muramyl dipeptide.";
Proc. Natl. Acad. Sci. U.S.A. 105:7803-7808(2008).
[20]
LACK OF ACTIVATION BY ANTHRAX 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).
[21]
AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF SER-1213.
PubMed=22087307; DOI=10.1371/journal.pone.0027396;
D'Osualdo A., Weichenberger C.X., Wagner R.N., Godzik A., Wooley J.,
Reed J.C.;
"CARD8 and NLRP1 undergo autoproteolytic processing through a ZU5-like
domain.";
PLoS ONE 6:E27396-E27396(2011).
[22]
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).
[23]
TISSUE SPECIFICITY, AND VARIANT MSPC THR-77.
PubMed=23349227; DOI=10.1136/jmedgenet-2012-101325;
Soler V.J., Tran-Viet K.N., Galiacy S.D., Limviphuvadh V., Klemm T.P.,
St Germain E., Fournie P.R., Guillaud C., Maurer-Stroh S.,
Hawthorne F., Suarez C., Kantelip B., Afshari N.A., Creveaux I.,
Luo X., Meng W., Calvas P., Cassagne M., Arne J.L., Rozen S.G.,
Malecaze F., Young T.L.;
"Whole exome sequencing identifies a mutation for a novel form of
corneal intraepithelial dyskeratosis.";
J. Med. Genet. 50:246-254(2013).
[24]
INTERACTION WITH VACCINIA VIRUS PROTEIN F1.
PubMed=16439990; DOI=10.1038/sj.cdd.4401853;
Postigo A., Cross J.R., Downward J., Way M.;
"Interaction of F1L with the BH3 domain of Bak is responsible for
inhibiting vaccinia-induced apoptosis.";
Cell Death Differ. 13:1651-1662(2006).
[25]
INDUCTION.
PubMed=24439873; DOI=10.1016/j.ijcard.2013.12.201;
Bleda S., de Haro J., Varela C., Esparza L., Ferruelo A., Acin F.;
"NLRP1 inflammasome, and not NLRP3, is the key in the shift to
proinflammatory state on endothelial cells in peripheral arterial
disease.";
Int. J. Cardiol. 172:E282-E284(2014).
[26]
INTERACTION WITH MEFV.
PubMed=26347139; DOI=10.1083/jcb.201503023;
Kimura T., Jain A., Choi S.W., Mandell M.A., Schroder K., Johansen T.,
Deretic V.;
"TRIM-mediated precision autophagy targets cytoplasmic regulators of
innate immunity.";
J. Cell Biol. 210:973-989(2015).
[27]
INDUCTION BY ATF4.
PubMed=26086088; DOI=10.1371/journal.pone.0130635;
D'Osualdo A., Anania V.G., Yu K., Lill J.R., Kaufman R.J.,
Matsuzawa S., Reed J.C.;
"Transcription factor ATF4 induces NLRP1 inflammasome expression
during endoplasmic reticulum stress.";
PLoS ONE 10:E0130635-E0130635(2015).
[28]
INVOLVEMENT IN AIADK, AND VARIANTS AIADK TRP-726 AND ARG-1214.
PubMed=27965258; DOI=10.1136/annrheumdis-2016-210021;
Grandemange S., Sanchez E., Louis-Plence P., Tran Mau-Them F.,
Bessis D., Coubes C., Frouin E., Seyger M., Girard M., Puechberty J.,
Costes V., Rodiere M., Carbasse A., Jeziorski E., Portales P.,
Sarrabay G., Mondain M., Jorgensen C., Apparailly F., Hoppenreijs E.,
Touitou I., Genevieve D.;
"A new autoinflammatory and autoimmune syndrome associated with NLRP1
mutations: NAIAD (NLRP1-associated autoinflammation with arthritis and
dyskeratosis).";
Ann. Rheum. Dis. 76:1191-1198(2017).
[29]
FUNCTION, TISSUE SPECIFICITY, VARIANTS MSPC THR-54; VAL-66 AND
787-PHE--ARG-843 DEL, AND CHARACTERIZATION OF VARIANTS MSPC THR-54;
VAL-66 AND 787-PHE--ARG-843 DEL.
PubMed=27662089; DOI=10.1016/j.cell.2016.09.001;
Zhong F.L., Mamai O., Sborgi L., Boussofara L., Hopkins R.,
Robinson K., Szeverenyi I., Takeichi T., Balaji R., Lau A., Tye H.,
Roy K., Bonnard C., Ahl P.J., Jones L.A., Baker P., Lacina L.,
Otsuka A., Fournie P.R., Malecaze F., Lane E.B., Akiyama M.,
Kabashima K., Connolly J.E., Masters S.L., Soler V.J., Omar S.S.,
McGrath J.A., Nedelcu R., Gribaa M., Denguezli M., Saad A., Hiller S.,
Reversade B.;
"Germline NLRP1 mutations cause skin inflammatory and cancer
susceptibility syndromes via inflammasome activation.";
Cell 167:187-202(2016).
[30]
STRUCTURE BY NMR OF 1-93.
PubMed=14527388; DOI=10.1016/j.str.2003.08.009;
Hiller S., Kohl A., Fiorito F., Herrmann T., Wider G., Tschopp J.,
Gruetter M.G., Wuethrich K.;
"NMR structure of the apoptosis- and inflammation-related NALP1 pyrin
domain.";
Structure 11:1199-1205(2003).
[31]
INVOLVEMENT IN VAMAS1, AND VARIANT VAMAS1 HIS-155.
PubMed=17377159; DOI=10.1056/NEJMoa061592;
Jin Y., Mailloux C.M., Gowan K., Riccardi S.L., LaBerge G.,
Bennett D.C., Fain P.R., Spritz R.A.;
"NALP1 in vitiligo-associated multiple autoimmune disease.";
N. Engl. J. Med. 356:1216-1225(2007).
[32]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1371-1467.
Northeast structural genomics consortium (NESG);
"Northeast structural genomics consortium target HR3486E.";
Submitted (OCT-2009) to the PDB data bank.
-!- 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 NLRP1,
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:22665479,
PubMed:17418785). May be activated by muramyl dipeptide (MDP), a
fragment of bacterial peptidoglycan, in a NOD2-dependent manner
(PubMed:18511561). Contrary to its mouse ortholog, not activated
by Bacillus anthracis lethal toxin (PubMed:19651869). It is
unclear whether isoform 2 is involved in inflammasome formation.
It is not cleaved within the FIIND domain, does not assemble into
specks, nor promote IL1B release (PubMed:22665479). However, in an
vitro cell-free system, it has been shown to be activated by MDP
(PubMed:17349957). Binds ATP (PubMed:11113115, PubMed:15212762).
{ECO:0000250|UniProtKB:A1Z198, ECO:0000269|PubMed:11113115,
ECO:0000269|PubMed:15212762, ECO:0000269|PubMed:17349957,
ECO:0000269|PubMed:17418785, ECO:0000269|PubMed:18511561,
ECO:0000269|PubMed:19651869, ECO:0000269|PubMed:22665479,
ECO:0000269|PubMed:27662089}.
-!- 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 CASP5). This interaction initiates speck formation
(nucleation) which greatly enhances further addition of soluble
PYCARD molecules to the speck in a prion-like polymerization
process. 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, NLRP1 can directly interact
with CASP1 (possibly through CARD domain) to form a functional
inflammasome, although the presence of PYCARD increases CASP1
activity (PubMed:17418785, PubMed:17349957). In a different
experimental system, neither CASP1-binding, NLRP1 inflammasome
speck formation, nor IL1B release were observed in the absence of
PYCARD (PubMed:22665479, PubMed:12191486). Hence PYCARD may not be
necessary for NLRP1 and CASP1 interaction, but is required for
speck formation and full inflammasome activity (By similarity).
Homomer (PubMed:17349957). 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 (PubMed:17418785). Interacts with NOD2; this interaction is
enhanced in the presence of muramyl dipeptide (MDP) and increases
IL1B release (PubMed:18511561). Interacts with EIF2AK2/PKR; this
interaction requires EIF2AK2 activity, is accompanied by EIF2AK2
autophosphorylation and promotes inflammasome assembly in response
to danger-associated signals (By similarity). Interacts with MEFV;
this interaction targets NLRP1 to degradation by autophagy, hence
preventing excessive IL1B- and IL18-mediated inflammation
(PubMed:17431422, PubMed:26347139). {ECO:0000250|UniProtKB:A1Z198,
ECO:0000250|UniProtKB:Q2LKW6, ECO:0000269|PubMed:12191486,
ECO:0000269|PubMed:17349957, ECO:0000269|PubMed:17418785,
ECO:0000269|PubMed:17431422, ECO:0000269|PubMed:18511561,
ECO:0000269|PubMed:22665479, ECO:0000269|PubMed:26347139}.
-!- SUBUNIT: (Microbial infection) Interacts with vaccinia virus
protein F1 (PubMed:16439990). {ECO:0000269|PubMed:16439990}.
-!- INTERACTION:
P10415:BCL2; NbExp=12; IntAct=EBI-1220518, EBI-77694;
Q07817:BCL2L1; NbExp=9; IntAct=EBI-1220518, EBI-78035;
Q9ULZ3:PYCARD; NbExp=5; IntAct=EBI-1220518, EBI-751215;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17418785}. Cytoplasm
{ECO:0000269|PubMed:17164409}. Inflammasome
{ECO:0000269|PubMed:12191486, ECO:0000269|PubMed:22665479}.
Nucleus {ECO:0000269|PubMed:17164409}. Note=Nucleocytoplasmic
distribution in lymphoid organs (probably in T-cells) and in
neurons. In epithelial cells, predominantly cytoplasmic.
{ECO:0000269|PubMed:17164409}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=NAC beta, DEFCAP-L, NALP1-L
{ECO:0000303|PubMed:15285719};
IsoId=Q9C000-1; Sequence=Displayed;
Name=2; Synonyms=NAC alpha, DEFCAP-S, NALP1-S
{ECO:0000303|PubMed:15285719}, NLRP1deltaEx14;
IsoId=Q9C000-2; Sequence=VSP_004327;
Name=3; Synonyms=NAC gamma;
IsoId=Q9C000-3; Sequence=VSP_004326, VSP_004327;
Name=4; Synonyms=NAC delta;
IsoId=Q9C000-4; Sequence=VSP_004326;
Name=5;
IsoId=Q9C000-5; Sequence=VSP_053803, VSP_053804, VSP_053805;
Name=6;
IsoId=Q9C000-6; Sequence=VSP_053802;
Name=7;
IsoId=Q9C000-7; Sequence=VSP_053801, VSP_053803, VSP_053804,
VSP_053805;
-!- TISSUE SPECIFICITY: Widely expressed (PubMed:11113115,
PubMed:17164409). Abundantly expressed in primary immune cells
(isoform 1 and isoform 2), including in neutrophils,
monocytes/macrophages, dendritic cells (mostly Langerhans cells),
and B- and T-lymphocytes (at protein level) (PubMed:15285719,
PubMed:17164409). Strongly expressed in epithelial cells lining
the glandular epithelium, such as that of the gastrointestinal
tract (stomach, small intestine, colon), the respiratory tract
(trachea and bronchi), and the endometrial and endocervical
glands, gallbladder, prostate, and breast (at protein level). In
testis, expressed in spermatogonia and primary spermatocytes, but
not in Sertoli cells (at protein level). In the brain, expressed
in neurons, in particular in pyramidal ones and in
oligodendrocytes, but not detected in microglia (at protein level)
(PubMed:17164409). Expressed in adult and fetal ocular tissues,
including in adult and 24-week old fetal choroid, sclera, cornea,
and optic nerve, as well as in adult retina and fetal
retina/retinal pigment epithelium (PubMed:23349227). Highly
expressed in the skin throughout the epidermis and in dermal
fibroblasts, in both glabrous skin and plantar skin. It is
detected in keratinocytes, but not in melanocytes. Expressed in
epidermal appendages such as hair follicles (PubMed:27662089).
{ECO:0000269|PubMed:11113115, ECO:0000269|PubMed:15285719,
ECO:0000269|PubMed:17164409, ECO:0000269|PubMed:23349227,
ECO:0000269|PubMed:27662089}.
-!- DEVELOPMENTAL STAGE: Associated with differentiation in stratified
epithelia of the skin, esophagus, intestine, and cervix, as well
as in the prostate gland. Undetectable in undifferentiated basal
cells, but expressed in differentiated luminal secretory cells
(PubMed:11113115). Expressed in differentiated macrophages and
granulocytes, but not their precursors (at protein level)
(PubMed:11113115, PubMed:15285719). In testis, also associated
with cell differentiation, with conflicting results. Expressed in
spermatogonia and primary spermatocytes, but not in cells from
later differentiation stages, including secondary spermatocytes,
spermatids, and spermatozoa (at protein level) (PubMed:17164409).
Not detected in spermatocytes, nor spermatids, and strongly
expressed in spermatozoa (at protein level) (PubMed:11113115).
{ECO:0000269|PubMed:11113115, ECO:0000269|PubMed:15285719,
ECO:0000269|PubMed:17164409}.
-!- INDUCTION: Up-regulated by ATF4 during endoplasmic reticulum (ER)
stress response (PubMed:26086088). Up-regulated in arterial
endothelial cells exposed to plasma from patients with peripheral
arterial disease, but not to plasma from healthy controls
(PubMed:24439873). {ECO:0000269|PubMed:24439873,
ECO:0000269|PubMed:26086088}.
-!- DOMAIN: The CARD domain, rather than the pyrin domain, is involved
in the interaction with PYCARD, CASP1 and CASP5.
{ECO:0000269|PubMed:12191486, ECO:0000269|PubMed:17349957,
ECO:0000269|PubMed:22665479}.
-!- 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:Q9EPB4, ECO:0000269|PubMed:12191486,
ECO:0000269|PubMed:17349957}.
-!- DOMAIN: The FIIND (domain with function to find) region is
involved in homomerization, but not in CASP1-binding (By
similarity). 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:22665479, PubMed:22087307). {ECO:0000250|UniProtKB:Q2LKW6,
ECO:0000269|PubMed:22087307, ECO:0000269|PubMed:22665479}.
-!- DISEASE: Vitiligo-associated multiple autoimmune disease 1
(VAMAS1) [MIM:606579]: A disorder characterized by the association
of vitiligo with several autoimmune and autoinflammatory diseases
including autoimmune thyroid disease, rheumatoid arthritis and
systemic lupus erythematosus. {ECO:0000269|PubMed:17377159}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Palmoplantar carcinoma, multiple self-healing (MSPC)
[MIM:615225]: An autosomal dominant disease characterized by
keratopathy with neovascularization, bilateral corneal
opacification, palmoplantar hyperkeratosis, dyshidrosis,
dystrophic nails, and recurrent keratoacanthomas in palmoplantar
skin as well as in conjunctival and corneal epithelia. In
addition, patients experience a high susceptibility to malignant
squamous cell carcinoma. {ECO:0000269|PubMed:23349227,
ECO:0000269|PubMed:27662089}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Autoinflammation with arthritis and dyskeratosis (AIADK)
[MIM:617388]: A disorder characterized by recurrent fever, diffuse
skin dyskeratosis, autoinflammation, autoimmunity, arthritis and
high transitional B-cell level. Inheritance can be autosomal
dominant or autosomal recessive. {ECO:0000269|PubMed:27965258}.
Note=The disease may be caused by mutations affecting the gene
represented in this entry.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=BAA76770.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB15469.1; Type=Frameshift; Positions=1241; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF298548; AAG15254.1; -; mRNA.
EMBL; AF310105; AAG30288.1; -; mRNA.
EMBL; AF229059; AAK00748.1; -; mRNA.
EMBL; AF229060; AAK00749.1; -; mRNA.
EMBL; AF229061; AAK00750.1; -; mRNA.
EMBL; AF229062; AAK00751.1; -; mRNA.
EMBL; AB023143; BAA76770.2; ALT_INIT; mRNA.
EMBL; AK026393; BAB15469.1; ALT_FRAME; mRNA.
EMBL; AK026398; BAB15470.1; -; mRNA.
EMBL; AC055839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC051787; AAH51787.1; -; mRNA.
EMBL; AL117470; CAB55945.1; -; mRNA.
CCDS; CCDS32537.1; -. [Q9C000-5]
CCDS; CCDS42244.1; -. [Q9C000-4]
CCDS; CCDS42245.1; -. [Q9C000-2]
CCDS; CCDS42246.1; -. [Q9C000-1]
CCDS; CCDS58508.1; -. [Q9C000-3]
PIR; T17255; T17255.
RefSeq; NP_001028225.1; NM_001033053.2. [Q9C000-5]
RefSeq; NP_055737.1; NM_014922.4. [Q9C000-2]
RefSeq; NP_127497.1; NM_033004.3. [Q9C000-1]
RefSeq; NP_127499.1; NM_033006.3. [Q9C000-4]
RefSeq; NP_127500.1; NM_033007.3. [Q9C000-3]
UniGene; Hs.652273; -.
PDB; 1PN5; NMR; -; A=1-93.
PDB; 3KAT; X-ray; 3.10 A; A=1371-1467.
PDB; 4IFP; X-ray; 1.99 A; A/B/C=1379-1462.
PDB; 4IM6; X-ray; 1.65 A; A=791-990.
PDBsum; 1PN5; -.
PDBsum; 3KAT; -.
PDBsum; 4IFP; -.
PDBsum; 4IM6; -.
DisProt; DP00554; -.
ProteinModelPortal; Q9C000; -.
SMR; Q9C000; -.
BioGrid; 116529; 12.
CORUM; Q9C000; -.
DIP; DIP-38407N; -.
IntAct; Q9C000; 9.
MINT; MINT-150191; -.
STRING; 9606.ENSP00000460475; -.
BindingDB; Q9C000; -.
ChEMBL; CHEMBL1741214; -.
iPTMnet; Q9C000; -.
PhosphoSitePlus; Q9C000; -.
BioMuta; NLRP1; -.
DMDM; 17380146; -.
EPD; Q9C000; -.
PaxDb; Q9C000; -.
PeptideAtlas; Q9C000; -.
PRIDE; Q9C000; -.
DNASU; 22861; -.
Ensembl; ENST00000262467; ENSP00000262467; ENSG00000091592. [Q9C000-5]
Ensembl; ENST00000269280; ENSP00000269280; ENSG00000091592. [Q9C000-2]
Ensembl; ENST00000345221; ENSP00000324366; ENSG00000091592. [Q9C000-2]
Ensembl; ENST00000354411; ENSP00000346390; ENSG00000091592. [Q9C000-4]
Ensembl; ENST00000544378; ENSP00000442029; ENSG00000091592. [Q9C000-5]
Ensembl; ENST00000571451; ENSP00000459661; ENSG00000091592. [Q9C000-2]
Ensembl; ENST00000572272; ENSP00000460475; ENSG00000091592. [Q9C000-1]
Ensembl; ENST00000577119; ENSP00000460216; ENSG00000091592. [Q9C000-3]
Ensembl; ENST00000613500; ENSP00000483359; ENSG00000091592. [Q9C000-5]
Ensembl; ENST00000617618; ENSP00000478516; ENSG00000091592. [Q9C000-1]
Ensembl; ENST00000619223; ENSP00000484692; ENSG00000091592. [Q9C000-4]
GeneID; 22861; -.
KEGG; hsa:22861; -.
UCSC; uc002gcg.2; human. [Q9C000-1]
CTD; 22861; -.
DisGeNET; 22861; -.
EuPathDB; HostDB:ENSG00000091592.15; -.
GeneCards; NLRP1; -.
HGNC; HGNC:14374; NLRP1.
HPA; CAB009189; -.
HPA; HPA064431; -.
MalaCards; NLRP1; -.
MIM; 606579; phenotype.
MIM; 606636; gene.
MIM; 615225; phenotype.
MIM; 617388; phenotype.
neXtProt; NX_Q9C000; -.
OpenTargets; ENSG00000091592; -.
Orphanet; 352662; Corneal intraepithelial dyskeratosis with palmoplantar hyperkeratosis and laryngeal dyskeratosis.
Orphanet; 3435; Vitiligo.
Orphanet; 247871; Vitiligo-associated autoimmune disease.
PharmGKB; PA162397797; -.
eggNOG; ENOG410JAIN; Eukaryota.
eggNOG; ENOG410YGKV; LUCA.
GeneTree; ENSGT00860000133669; -.
HOGENOM; HOG000230509; -.
HOVERGEN; HBG052573; -.
InParanoid; Q9C000; -.
KO; K12798; -.
OMA; LIMELWE; -.
OrthoDB; EOG091G01QH; -.
PhylomeDB; Q9C000; -.
TreeFam; TF340267; -.
Reactome; R-HSA-844455; The NLRP1 inflammasome.
EvolutionaryTrace; Q9C000; -.
GeneWiki; NLRP1; -.
GenomeRNAi; 22861; -.
PRO; PR:Q9C000; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000091592; -.
CleanEx; HS_NLRP1; -.
ExpressionAtlas; Q9C000; baseline and differential.
Genevisible; Q9C000; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005622; C:intracellular; IC:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0072558; C:NLRP1 inflammasome complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:HGNC.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; NAS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; ISS:BHF-UCL.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0051402; P:neuron apoptotic process; IDA:HGNC.
GO; GO:1904784; P:NLRP1 inflammasome complex assembly; IMP:UniProtKB.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; ISS:BHF-UCL.
GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032495; P:response to muramyl dipeptide; ISS:BHF-UCL.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd08330; CARD_ASC_NALP1; 1.
InterPro; IPR001315; CARD.
InterPro; IPR033516; CARD8/ASC/NALP1_CARD.
InterPro; IPR004020; DAPIN.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR025307; FIIND_dom.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00619; CARD; 1.
Pfam; PF13553; FIIND; 1.
Pfam; PF13516; LRR_6; 3.
Pfam; PF02758; PYRIN; 1.
SMART; SM01289; PYRIN; 1.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS50209; CARD; 1.
PROSITE; PS50824; DAPIN; 1.
PROSITE; PS51830; FIIND; 1.
PROSITE; PS51450; LRR; 3.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation;
Ectodermal dysplasia; Host-virus interaction; Immunity; Inflammasome;
Inflammatory response; Innate immunity; Leucine-rich repeat;
Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Repeat.
CHAIN 1 1473 NACHT, LRR and PYD domains-containing
protein 1.
/FTId=PRO_0000096710.
DOMAIN 1 92 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 328 637 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 809 830 LRR 1.
REPEAT 838 858 LRR 2.
REPEAT 866 887 LRR 3.
REPEAT 895 915 LRR 4.
REPEAT 923 944 LRR 5.
REPEAT 950 973 LRR 6.
DOMAIN 1079 1364 FIIND. {ECO:0000255|PROSITE-
ProRule:PRU01174}.
DOMAIN 1374 1463 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
NP_BIND 334 341 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
SITE 1186 1186 Trigger for autolytic processing.
{ECO:0000269|PubMed:22665479}.
SITE 1212 1213 Cleavage; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU01174,
ECO:0000269|PubMed:22665479}.
VAR_SEQ 1 966 Missing (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053801.
VAR_SEQ 1 734 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053802.
VAR_SEQ 958 987 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:11113115}.
/FTId=VSP_004326.
VAR_SEQ 1044 1044 A -> AGKSH (in isoform 5 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_053803.
VAR_SEQ 1262 1305 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:10231032,
ECO:0000303|PubMed:11076957,
ECO:0000303|PubMed:11113115,
ECO:0000303|PubMed:11250163,
ECO:0000303|PubMed:11270363}.
/FTId=VSP_004327.
VAR_SEQ 1354 1371 DLMPATTLIPPARIAVPS -> RNTSQPWNLRCNRDARRY
(in isoform 5 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_053804.
VAR_SEQ 1372 1473 Missing (in isoform 5 and isoform 7).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_053805.
VARIANT 54 54 A -> T (in MSPC; increased NLRP1-
inflammasome complex assembly; altered
protein folding).
{ECO:0000269|PubMed:27662089}.
/FTId=VAR_078798.
VARIANT 66 66 A -> V (in MSPC; increased NLRP1-
inflammasome complex assembly; altered
protein folding).
{ECO:0000269|PubMed:27662089}.
/FTId=VAR_078799.
VARIANT 77 77 M -> T (in MSPC; dbSNP:rs397514692).
{ECO:0000269|PubMed:23349227}.
/FTId=VAR_069901.
VARIANT 155 155 L -> H (in VAMAS1; associated with
disease susceptibility;
dbSNP:rs12150220).
{ECO:0000269|PubMed:11270363,
ECO:0000269|PubMed:17377159}.
/FTId=VAR_033239.
VARIANT 246 246 T -> S (in dbSNP:rs11651595).
{ECO:0000269|PubMed:11270363}.
/FTId=VAR_024238.
VARIANT 404 404 R -> Q (in dbSNP:rs3744718).
/FTId=VAR_021886.
VARIANT 726 726 R -> W (in AIADK; unknown pathological
significance; dbSNP:rs776245016).
{ECO:0000269|PubMed:27965258}.
/FTId=VAR_078800.
VARIANT 787 843 Missing (in MSPC; increased NLRP1-
inflammasome complex assembly).
{ECO:0000269|PubMed:27662089}.
/FTId=VAR_078801.
VARIANT 878 878 T -> M (in dbSNP:rs11657747).
{ECO:0000269|PubMed:11270363}.
/FTId=VAR_033240.
VARIANT 1059 1059 V -> M (in dbSNP:rs2301582).
/FTId=VAR_024239.
VARIANT 1069 1069 H -> Y (in dbSNP:rs9907167).
/FTId=VAR_033241.
VARIANT 1119 1119 M -> V (no effect on autocatalytic
processing, nor on IL1B release;
dbSNP:rs35596958).
{ECO:0000269|PubMed:11270363,
ECO:0000269|PubMed:22665479}.
/FTId=VAR_033242.
VARIANT 1184 1184 M -> V (increased autocatalytic
processing and IL1B release;
dbSNP:rs11651270).
{ECO:0000269|PubMed:11270363,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:22665479}.
/FTId=VAR_033243.
VARIANT 1214 1214 P -> R (in AIADK; unknown pathological
significance).
{ECO:0000269|PubMed:27965258}.
/FTId=VAR_078802.
VARIANT 1241 1241 V -> L (in dbSNP:rs11653832).
{ECO:0000269|PubMed:11270363}.
/FTId=VAR_033244.
VARIANT 1366 1366 R -> C (in dbSNP:rs2137722).
{ECO:0000269|PubMed:11270363}.
/FTId=VAR_020437.
MUTAGEN 339 340 GK->EA: Loss of ATP binding.
{ECO:0000269|PubMed:15212762}.
MUTAGEN 340 340 K->L,S: No effect.
{ECO:0000269|PubMed:11076957}.
MUTAGEN 1168 1168 H->A: Complete loss of autocatalytic
processing and of IL1B release.
Autocatalytic processing cannot be
restored by treatment with hydroxylamine.
{ECO:0000269|PubMed:22665479}.
MUTAGEN 1186 1186 H->A: Complete loss of autocatalytic
processing and of IL1B release.
Autocatalytic processing can be restored
by treatment with hydroxylamine.
{ECO:0000269|PubMed:22665479}.
MUTAGEN 1211 1211 S->A: Partial loss of autocatalytic
processing and of IL1B release.
{ECO:0000269|PubMed:22665479}.
MUTAGEN 1212 1212 F->A: Complete loss of autocatalytic
processing and of IL1B release.
{ECO:0000269|PubMed:22665479}.
MUTAGEN 1213 1213 S->A: Complete loss of autocatalytic
processing and of IL1B release.
Autocatalytic processing cannot be
restored by treatment with hydroxylamine.
{ECO:0000269|PubMed:22087307,
ECO:0000269|PubMed:22665479}.
MUTAGEN 1213 1213 S->C: Complete loss of autocatalytic
processing, which can be restored by
treatment with hydroxylamine.
{ECO:0000269|PubMed:22665479}.
MUTAGEN 1214 1214 P->A: Partial loss of autocatalytic
processing (50%) and of IL1B release
(50%). {ECO:0000269|PubMed:22665479}.
MUTAGEN 1249 1249 H->A: Complete loss of autocatalytic
processing and IL1B release.
Autocatalytic processing cannot be
restored by treatment with hydroxylamine.
{ECO:0000269|PubMed:22665479}.
CONFLICT 287 287 P -> S (in Ref. 8; AAH51787).
{ECO:0000305}.
CONFLICT 782 782 T -> S (in Ref. 1; AAG15254).
{ECO:0000305}.
CONFLICT 995 995 T -> I (in Ref. 1; AAG15254).
{ECO:0000305}.
HELIX 9 15 {ECO:0000244|PDB:1PN5}.
HELIX 18 31 {ECO:0000244|PDB:1PN5}.
HELIX 50 60 {ECO:0000244|PDB:1PN5}.
HELIX 63 77 {ECO:0000244|PDB:1PN5}.
HELIX 80 85 {ECO:0000244|PDB:1PN5}.
STRAND 88 91 {ECO:0000244|PDB:1PN5}.
HELIX 794 804 {ECO:0000244|PDB:4IM6}.
STRAND 812 814 {ECO:0000244|PDB:4IM6}.
HELIX 822 833 {ECO:0000244|PDB:4IM6}.
STRAND 840 843 {ECO:0000244|PDB:4IM6}.
HELIX 851 862 {ECO:0000244|PDB:4IM6}.
STRAND 869 871 {ECO:0000244|PDB:4IM6}.
HELIX 878 889 {ECO:0000244|PDB:4IM6}.
STRAND 898 900 {ECO:0000244|PDB:4IM6}.
HELIX 908 910 {ECO:0000244|PDB:4IM6}.
HELIX 911 920 {ECO:0000244|PDB:4IM6}.
STRAND 926 928 {ECO:0000244|PDB:4IM6}.
STRAND 931 933 {ECO:0000244|PDB:4IM6}.
HELIX 935 946 {ECO:0000244|PDB:4IM6}.
STRAND 955 957 {ECO:0000244|PDB:4IM6}.
HELIX 965 977 {ECO:0000244|PDB:4IM6}.
STRAND 982 984 {ECO:0000244|PDB:4IM6}.
HELIX 1381 1384 {ECO:0000244|PDB:4IFP}.
HELIX 1386 1392 {ECO:0000244|PDB:4IFP}.
HELIX 1396 1403 {ECO:0000244|PDB:4IFP}.
TURN 1405 1407 {ECO:0000244|PDB:4IFP}.
HELIX 1410 1417 {ECO:0000244|PDB:4IFP}.
STRAND 1419 1421 {ECO:0000244|PDB:4IFP}.
HELIX 1422 1433 {ECO:0000244|PDB:4IFP}.
HELIX 1438 1451 {ECO:0000244|PDB:4IFP}.
HELIX 1453 1462 {ECO:0000244|PDB:4IFP}.
SEQUENCE 1473 AA; 165866 MW; 438F0DCE45C2562D CRC64;
MAGGAWGRLA CYLEFLKKEE LKEFQLLLAN KAHSRSSSGE TPAQPEKTSG MEVASYLVAQ
YGEQRAWDLA LHTWEQMGLR SLCAQAQEGA GHSPSFPYSP SEPHLGSPSQ PTSTAVLMPW
IHELPAGCTQ GSERRVLRQL PDTSGRRWRE ISASLLYQAL PSSPDHESPS QESPNAPTST
AVLGSWGSPP QPSLAPREQE APGTQWPLDE TSGIYYTEIR EREREKSEKG RPPWAAVVGT
PPQAHTSLQP HHHPWEPSVR ESLCSTWPWK NEDFNQKFTQ LLLLQRPHPR SQDPLVKRSW
PDYVEENRGH LIEIRDLFGP GLDTQEPRIV ILQGAAGIGK STLARQVKEA WGRGQLYGDR
FQHVFYFSCR ELAQSKVVSL AELIGKDGTA TPAPIRQILS RPERLLFILD GVDEPGWVLQ
EPSSELCLHW SQPQPADALL GSLLGKTILP EASFLITART TALQNLIPSL EQARWVEVLG
FSESSRKEYF YRYFTDERQA IRAFRLVKSN KELWALCLVP WVSWLACTCL MQQMKRKEKL
TLTSKTTTTL CLHYLAQALQ AQPLGPQLRD LCSLAAEGIW QKKTLFSPDD LRKHGLDGAI
ISTFLKMGIL QEHPIPLSYS FIHLCFQEFF AAMSYVLEDE KGRGKHSNCI IDLEKTLEAY
GIHGLFGAST TRFLLGLLSD EGEREMENIF HCRLSQGRNL MQWVPSLQLL LQPHSLESLH
CLYETRNKTF LTQVMAHFEE MGMCVETDME LLVCTFCIKF SRHVKKLQLI EGRQHRSTWS
PTMVVLFRWV PVTDAYWQIL FSVLKVTRNL KELDLSGNSL SHSAVKSLCK TLRRPRCLLE
TLRLAGCGLT AEDCKDLAFG LRANQTLTEL DLSFNVLTDA GAKHLCQRLR QPSCKLQRLQ
LVSCGLTSDC CQDLASVLSA SPSLKELDLQ QNNLDDVGVR LLCEGLRHPA CKLIRLGLDQ
TTLSDEMRQE LRALEQEKPQ LLIFSRRKPS VMTPTEGLDT GEMSNSTSSL KRQRLGSERA
ASHVAQANLK LLDVSKIFPI AEIAEESSPE VVPVELLCVP SPASQGDLHT KPLGTDDDFW
GPTGPVATEV VDKEKNLYRV HFPVAGSYRW PNTGLCFVMR EAVTVEIEFC VWDQFLGEIN
PQHSWMVAGP LLDIKAEPGA VEAVHLPHFV ALQGGHVDTS LFQMAHFKEE GMLLEKPARV
ELHHIVLENP SFSPLGVLLK MIHNALRFIP VTSVVLLYHR VHPEEVTFHL YLIPSDCSIR
KAIDDLEMKF QFVRIHKPPP LTPLYMGCRY TVSGSGSGML EILPKELELC YRSPGEDQLF
SEFYVGHLGS GIRLQVKDKK DETLVWEALV KPGDLMPATT LIPPARIAVP SPLDAPQLLH
FVDQYREQLI ARVTSVEVVL DKLHGQVLSQ EQYERVLAEN TRPSQMRKLF SLSQSWDRKC
KDGLYQALKE THPHLIMELW EKGSKKGLLP LSS


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