Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

NACHT, LRR and PYD domains-containing protein 3 (Angiotensin/vasopressin receptor AII/AVP-like) (Caterpiller protein 1.1) (CLR1.1) (Cold-induced autoinflammatory syndrome 1 protein) (Cryopyrin) (PYRIN-containing APAF1-like protein 1)

 NLRP3_HUMAN             Reviewed;        1036 AA.
Q96P20; A0A024R5Q0; B2RC97; B7ZKS9; B7ZKT2; B7ZKT3; O75434; Q17RS2;
Q59H68; Q5JQS8; Q5JQS9; Q6TG35; Q8TCW0; Q8TEU9; Q8WXH9;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
03-NOV-2009, sequence version 3.
27-SEP-2017, entry version 180.
RecName: Full=NACHT, LRR and PYD domains-containing protein 3;
AltName: Full=Angiotensin/vasopressin receptor AII/AVP-like;
AltName: Full=Caterpiller protein 1.1;
Short=CLR1.1;
AltName: Full=Cold-induced autoinflammatory syndrome 1 protein;
AltName: Full=Cryopyrin;
AltName: Full=PYRIN-containing APAF1-like protein 1;
Name=NLRP3; Synonyms=C1orf7, CIAS1, NALP3, PYPAF1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS
FCAS1 MET-200; VAL-441 AND GLY-629, AND VARIANT MWS VAL-354.
PubMed=11687797; DOI=10.1038/ng756;
Hoffman H.M., Mueller J.L., Broide D.H., Wanderer A.A., Kolodner R.D.;
"Mutation of a new gene encoding a putative pyrin-like protein causes
familial cold autoinflammatory syndrome and Muckle-Wells syndrome.";
Nat. Genet. 29:301-305(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT MWS MET-200,
AND VARIANTS FCAS1/MWS TRP-262 AND PRO-307.
PubMed=12355493; DOI=10.1002/art.10509;
Aganna E., Martinon F., Hawkins P.N., Ross J.B., Swan D.C.,
Booth D.R., Lachmann H.J., Gaudet R., Woo P., Feighery C.,
Cotter F.E., Thome M., Hitman G.A., Tschopp J., McDermott M.F.;
"Association of mutations in the NALP3/CIAS1/PYPAF1 gene with a broad
phenotype including recurrent fever, cold sensitivity, sensorineural
deafness, and AA amyloidosis.";
Arthritis Rheum. 46:2445-2452(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PYCARD,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND AUTOINHIBITION.
PubMed=11786556; DOI=10.1074/jbc.M112208200;
Manji G.A., Wang L., Geddes B.J., Brown M., Merriam S., Al-Garawi A.,
Mak S., Lora J.M., Briskin M., Jurman M., Cao J., DiStefano P.S.,
Bertin J.;
"PYPAF1: a PYRIN-containing APAF1-like protein that assembles with ASC
and activates NF-kB.";
J. Biol. Chem. 277:11570-11575(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 6).
TISSUE=Colon;
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 [MRNA] OF 2-1036 (ISOFORM 4), ALTERNATIVE SPLICING
(ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND INDUCTION BY LPS; LTA;
POLY(I:C) AND TNF.
PubMed=14662828; DOI=10.4049/jimmunol.171.12.6329;
O'Connor W. Jr., Harton J.A., Zhu X., Linhoff M.W., Ting J.-P.;
"CIAS1/cryopyrin/PYPAF1/NALP3/CATERPILLER 1.1 is an inducible
inflammatory mediator with NF-kappa B suppressive properties.";
J. Immunol. 171:6329-6333(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-1036 (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[11]
IDENTIFICATION OF NRLP3 INFLAMMASOME COMPLEX.
PubMed=15030775; DOI=10.1016/S1074-7613(04)00046-9;
Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N.,
Tschopp J.;
"NALP3 forms an IL-1beta-processing inflammasome with increased
activity in Muckle-Wells autoinflammatory disorder.";
Immunity 20:319-325(2004).
[12]
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).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[14]
TISSUE SPECIFICITY, AND INDUCTION BY SALMONELLA.
PubMed=17907925; DOI=10.1359/jbmr.071002;
McCall S.H., Sahraei M., Young A.B., Worley C.S., Duncan J.A.,
Ting J.P., Marriott I.;
"Osteoblasts express NLRP3, a nucleotide-binding domain and leucine-
rich repeat region containing receptor implicated in bacterially
induced cell death.";
J. Bone Miner. Res. 23:30-40(2008).
[15]
UBIQUITINATION.
PubMed=22948162; DOI=10.1074/jbc.M112.407130;
Juliana C., Fernandes-Alnemri T., Kang S., Farias A., Qin F.,
Alnemri E.S.;
"Non-transcriptional priming and deubiquitination regulate NLRP3
inflammasome activation.";
J. Biol. Chem. 287:36617-36622(2012).
[16]
FUNCTION, AND 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).
[17]
INTERACTION WITH GBP5, AND MUTAGENESIS OF 22-LEU-LYS-23.
PubMed=22461501; DOI=10.1126/science.1217141;
Shenoy A.R., Wellington D.A., Kumar P., Kassa H., Booth C.J.,
Cresswell P., MacMicking J.D.;
"GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals.";
Science 336:481-485(2012).
[18]
INTERACTION WITH PML.
PubMed=23430110; DOI=10.1182/blood-2012-05-432104;
Lo Y.H., Huang Y.W., Wu Y.H., Tsai C.S., Lin Y.C., Mo S.T., Kuo W.C.,
Chuang Y.T., Jiang S.T., Shih H.M., Lai M.Z.;
"Selective inhibition of the NLRP3 inflammasome by targeting to
promyelocytic leukemia protein in mouse and human.";
Blood 121:3185-3194(2013).
[19]
REVIEW.
PubMed=23305783; DOI=10.1016/j.coi.2012.12.004;
Haneklaus M., O'Neill L.A., Coll R.C.;
"Modulatory mechanisms controlling the NLRP3 inflammasome in
inflammation: recent developments.";
Curr. Opin. Immunol. 25:40-45(2013).
[20]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
PubMed=23955712; DOI=10.1038/nm.3265;
Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J.,
Tam J., Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M.,
Czech M.P., Kunos G.;
"Activation of the Nlrp3 inflammasome in infiltrating macrophages by
endocannabinoids mediates beta cell loss in type 2 diabetes.";
Nat. Med. 19:1132-1140(2013).
[21]
MECHANISM OF INFLAMMASOME ASSEMBLY, AND MUTAGENESIS OF GLU-15; LYS-23;
LYS-24; MET-27; ARG-43; GLU-64 AND ASP-82.
PubMed=24630722; DOI=10.1016/j.cell.2014.02.008;
Lu A., Magupalli V.G., Ruan J., Yin Q., Atianand M.K., Vos M.R.,
Schroder G.F., Fitzgerald K.A., Wu H., Egelman E.H.;
"Unified polymerization mechanism for the assembly of ASC-dependent
inflammasomes.";
Cell 156:1193-1206(2014).
[22]
SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT FCAS1/MWS TRP-262,
CHARACTERIZATION OF VARIANT CINCA ASN-305, AND CHARACTERIZATION OF
VARIANT CINCA/MWS MET-350.
PubMed=24952504; DOI=10.1038/ni.2919;
Baroja-Mazo A., Martin-Sanchez F., Gomez A.I., Martinez C.M.,
Amores-Iniesta J., Compan V., Barbera-Cremades M., Yaguee J.,
Ruiz-Ortiz E., Anton J., Bujan S., Couillin I., Brough D.,
Arostegui J.I., Pelegrin P.;
"The NLRP3 inflammasome is released as a particulate danger signal
that amplifies the inflammatory response.";
Nat. Immunol. 15:738-748(2014).
[23]
REVIEW ON INFLAMMASOME ASSEMBLY.
PubMed=25354325; DOI=10.1111/febs.13133;
Lu A., Wu H.;
"Structural mechanisms of inflammasome assembly.";
FEBS J. 282:435-444(2015).
[24]
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).
[25]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 3-112, SUBUNIT, AND DISULFIDE
BOND.
PubMed=21880711; DOI=10.1074/jbc.M111.278812;
Bae J.Y., Park H.H.;
"Crystal structure of NALP3 protein pyrin domain (PYD) and its
implications in inflammasome assembly.";
J. Biol. Chem. 286:39528-39536(2011).
[26]
VARIANT FCAS1 MET-200, VARIANTS MWS ASN-305; MET-350; THR-441 AND
ARG-571, AND VARIANT FCAS1/MWS TRP-262.
PubMed=11992256; DOI=10.1086/340786;
Dode C., Le Du N., Cuisset L., Letourneur F., Berthelot J.-M.,
Vaudour G., Meyrier A., Watts R.A., Scott D.G.I., Nicholls A.,
Granel B., Frances C., Garcier F., Edery P., Boulinguez S.,
Domergues J.-P., Delpech M., Grateau G.;
"New mutations of CIAS1 that are responsible for Muckle-Wells syndrome
and familial cold urticaria: a novel mutation underlies both
syndromes.";
Am. J. Hum. Genet. 70:1498-1506(2002).
[27]
VARIANTS CINCA ASN-305; LYS-308; SER-311; ARG-360; ASN-438; SER-575
AND THR-664, AND TISSUE SPECIFICITY.
PubMed=12032915; DOI=10.1086/341357;
Feldmann J., Prieur A.-M., Quartier P., Berquin P., Certain S.,
Cortis E., Teillac-Hamel D., Fischer A., de Saint Basile G.;
"Chronic infantile neurological cutaneous and articular syndrome is
caused by mutations in CIAS1, a gene highly expressed in
polymorphonuclear cells and chondrocytes.";
Am. J. Hum. Genet. 71:198-203(2002).
[28]
ERRATUM.
Feldmann J., Prieur A.-M., Quartier P., Berquin P., Certain S.,
Cortis E., Teillac-Hamel D., Fischer A., de Saint Basile G.;
Am. J. Hum. Genet. 71:1258-1258(2002).
[29]
VARIANTS CINCA HIS-266; ASN-305; LEU-525 AND CYS-572.
PubMed=12483741; DOI=10.1002/art.10688;
Aksentijevich I., Nowak M., Mallah M., Chae J.J., Watford W.T.,
Hofmann S.R., Stein L., Russo R., Goldsmith D., Dent P.,
Rosenberg H.F., Austin F., Remmers E.F., Balow J.E. Jr.,
Rosenzweig S., Komarow H., Shoham N.G., Wood G., Jones J., Mangra N.,
Carrero H., Adams B.S., Moore T.L., Schikler K., Hoffman H.,
Lovell D.J., Lipnick R., Barron K., O'Shea J.J., Kastner D.L.,
Goldbach-Mansky R.;
"De novo CIAS1 mutations, cytokine activation, and evidence for
genetic heterogeneity in patients with neonatal-onset multisystem
inflammatory disease (NOMID): a new member of the expanding family of
pyrin-associated autoinflammatory diseases.";
Arthritis Rheum. 46:3340-3348(2002).
[30]
VARIANT FCAS1 PRO-355, AND VARIANT LYS-705.
PubMed=12522564; DOI=10.1007/s00439-002-0860-x;
Hoffman H.M., Gregory S.G., Mueller J.L., Tresierras M., Broide D.H.,
Wanderer A.A., Kolodner R.D.;
"Fine structure mapping of CIAS1: identification of an ancestral
haplotype and a common FCAS mutation, L353P.";
Hum. Genet. 112:209-216(2003).
[31]
VARIANT CINCA CYS-861.
PubMed=15334500; DOI=10.1002/art.20295;
Frenkel J., van Kempen M.J., Kuis W., van Amstel H.K.;
"Variant chronic infantile neurologic, cutaneous, articular syndrome
due to a mutation within the leucine-rich repeat domain of CIAS1.";
Arthritis Rheum. 50:2719-2720(2004).
[32]
VARIANTS FCAS1 MET-200; PRO-307 AND LYS-490, VARIANT CINCA ASN-305,
AND VARIANT MWS MET-350.
PubMed=15593220; DOI=10.1002/art.20633;
Arostegui J.I., Aldea A., Modesto C., Rua M.J., Argueelles F.,
Gonzalez-Ensenat M.A., Ramos E., Rius J., Plaza S., Vives J.,
Yaguee J.;
"Clinical and genetic heterogeneity among Spanish patients with
recurrent autoinflammatory syndromes associated with the
CIAS1/PYPAF1/NALP3 gene.";
Arthritis Rheum. 50:4045-4050(2004).
[33]
VARIANTS CINCA LEU-262; PRO-262; ASN-305; GLY-305; SER-311; MET-350;
ASP-356; PRO-407; ILE-438; CYS-572 AND PHE-634.
PubMed=14630794; DOI=10.1182/blood-2003-07-2531;
Neven B., Callebaut I., Prieur A.-M., Feldmann J., Bodemer C.,
Lepore L., Derfalvi B., Benjaponpitak S., Vesely R., Sauvain M.J.,
Oertle S., Allen R., Morgan G., Borkhardt A., Hill C.,
Gardner-Medwin J., Fischer A., de Saint Basile G.;
"Molecular basis of the spectral expression of CIAS1 mutations
associated with phagocytic cell-mediated autoinflammatory disorders
CINCA/NOMID, MWS, and FCU.";
Blood 103:2809-2815(2004).
[34]
VARIANT CINCA THR-174.
PubMed=15231984; DOI=10.1542/peds.114.1.e124;
Stojanov S., Weiss M., Lohse P., Belohradsky B.H.;
"A novel CIAS1 mutation and plasma/cerebrospinal fluid cytokine
profile in a German patient with neonatal-onset multisystem
inflammatory disease responsive to methotrexate therapy.";
Pediatrics 114:E124-E127(2004).
[35]
VARIANT FCAS1 CYS-525.
PubMed=17284928; DOI=10.1159/000099311;
Shalev S.A., Sprecher E., Indelman M., Hujirat Y., Bergman R.,
Rottem M.;
"A novel missense mutation in CIAS1 encoding the pyrin-like protein,
cryopyrin, causes familial cold autoinflammatory syndrome in a family
of Ethiopian origin.";
Int. Arch. Allergy Immunol. 143:190-193(2007).
-!- FUNCTION: As the sensor component of the NLRP3 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 NLRP3,
PYCARD and CASP1 (and possibly CASP4 and CASP5). Recruitment of
proCASP1 to the inflammasome promotes its activation and CASP1-
catalyzed IL1B and IL18 maturation and secretion in the
extracellular milieu. Activation of NLRP3 inflammasome is also
required for HMGB1 secretion (PubMed:22801494). The active
cytokines and HMGB1 stimulate inflammatory responses.
Inflammasomes can also induce pyroptosis, an inflammatory form of
programmed cell death. Under resting conditions, NLRP3 is
autoinhibited. NLRP3 activation stimuli include extracellular ATP,
reactive oxygen species, K(+) efflux, crystals of monosodium urate
or cholesterol, amyloid-beta fibers, environmental or industrial
particles and nanoparticles, etc. However, it is unclear what
constitutes the direct NLRP3 activator. Independently of
inflammasome activation, regulates the differentiation of T helper
2 (Th2) cells and has a role in Th2 cell-dependent asthma and
tumor growth (By similarity). During Th2 differentiation, required
for optimal IRF4 binding to IL4 promoter and for IRF4-dependent
IL4 transcription. Binds to the consensus DNA sequence 5'-
GRRGGNRGAG-3'. May also participate in the transcription of IL5,
IL13, GATA3, CCR3, CCR4 and MAF (By similarity).
{ECO:0000250|UniProtKB:Q8R4B8, ECO:0000269|PubMed:22801494,
ECO:0000305|PubMed:23305783}.
-!- SUBUNIT: Sensor component of NLRP3 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. The core of
NLRP3 inflammasomes consists of a signal sensor component (NLRP3),
an adapter (ASC/PYCARD), which recruits an effector
proinflammatory caspase (CASP1 and, possibly, CASP4 and CASP5).
Within the complex, NLRP3 and PYCARD interact via their respective
DAPIN/pyrin domains. This interaction initiates speck formation
(nucleation) which greatly enhances further addition of soluble
PYCARD molecules to the speck in a prion-like polymerization
process (PubMed:24630722). NLRP3 localizes at the end of each
PYCARD filament (PubMed:24630722). Clustered PYCARD nucleates the
formation of CASP1 filaments through the interaction of their
respective CARD domains, acting as a platform for CASP1
polymerization (PubMed:24630722). 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. Reconstituted
ternary inflammasomes show star-shaped structures, in which
multiple filaments, containing CASP1, protrude radially from a
single central hub, containing the sensor protein and PYCARD
(PubMed:24630722). In this complex, the sensor protein is sub-
stoichiometric to PYCARD, and PYCARD is further substoichiometric
to CASP1, suggesting amplifications of signal transduction from
the sensor, via the adapter, to the effector (PubMed:24630722).
Interacts with MEFV; this interaction targets NLRP3 to degradation
by autophagy, hence preventing excessive IL1B- and IL18-mediated
inflammation (PubMed:17431422) (PubMed:26347139). Interacts with
GBP5 (via DAPIN domain); this interaction promotes inflammasome
assembly in response to microbial and soluble, but not
crystalline, agents (PubMed:22461501). Interacts with EIF2AK2/PKR;
this interaction requires EIF2AK2 activity, is accompanied by
EIF2AK2 autophosphorylation and promotes inflammasome assembly in
response to specific stimuli (PubMed:22801494). Interacts with PML
(isoform PML-1) (via the leucine-rich repeat (LRR) domain); PML-
mediated increase in NLRP3 inflammasome activation does not depend
upon this interaction (PubMed:23430110). Directly interacts with
IRF4 (via the LRR domain); this interaction is required for
optimal IRF4 binding to IL4 promoter and efficient IL4
transactivation during differentiation of Th2 helper T-cells (By
similarity). {ECO:0000250|UniProtKB:Q8R4B8,
ECO:0000269|PubMed:11786556, ECO:0000269|PubMed:15030775,
ECO:0000269|PubMed:17431422, ECO:0000269|PubMed:21880711,
ECO:0000269|PubMed:22461501, ECO:0000269|PubMed:22801494,
ECO:0000269|PubMed:23430110, ECO:0000269|PubMed:24630722,
ECO:0000269|PubMed:26347139, ECO:0000305|PubMed:23305783,
ECO:0000305|PubMed:25354325}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-6253230, EBI-6253230;
Q7Z434:MAVS; NbExp=4; IntAct=EBI-6253230, EBI-995373;
Q9ULZ3:PYCARD; NbExp=8; IntAct=EBI-6253230, EBI-751215;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:11786556, ECO:0000269|PubMed:14662828,
ECO:0000269|PubMed:17164409}. Inflammasome
{ECO:0000269|PubMed:11786556, ECO:0000269|PubMed:14662828,
ECO:0000269|PubMed:17164409}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:Q8R4B8}. Secreted
{ECO:0000269|PubMed:24952504}. Nucleus
{ECO:0000250|UniProtKB:Q8R4B8}. Note=In macrophages, under resting
conditions, mainly located in the cytosol, on the endoplasmic
reticulum. After stimulation with inducers of the NLRP3
inflammasome, mitochondria redistribute in the vicinity of the
endoplasmic reticulum in the perinuclear region, which results in
colocalization of NLRP3 on the endoplasmic reticulum and PYCARD on
mitochondria, allowing the activation of inflammasome assembly.
After the induction of pyroptosis, inflammasome specks are
released into the extracellular space where they can further
promote IL1B processing and where they can be engulfed by
macrophages. Phagocytosis induces lysosomal damage and
inflammasome activation in the recipient cells (PubMed:24952504).
In the Th2 subset of CD4(+) helper T-cells, mainly located in the
nucleus. Nuclear localization depends upon KPNA2. In the Th1
subset of CD4(+) helper T-cells, mainly cytoplasmic (By
similarity). {ECO:0000250|UniProtKB:Q8R4B8,
ECO:0000269|PubMed:24952504}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=2;
IsoId=Q96P20-1; Sequence=Displayed;
Name=1;
IsoId=Q96P20-2; Sequence=VSP_005520, VSP_005521;
Name=3;
IsoId=Q96P20-3; Sequence=VSP_005519;
Name=4;
IsoId=Q96P20-4; Sequence=VSP_005520;
Name=5;
IsoId=Q96P20-5; Sequence=VSP_005521;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q96P20-6; Sequence=VSP_053714;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in macrophages. Also
expressed in dendritic cells, B- and T-cells (at protein level)
(PubMed:11786556) (PubMed:17164409). Expressed in LPS-treated
granulocytes, but not in resting cells (at protein level)
(PubMed:17164409). Expression in monocytes is very weak (at
protein level) (PubMed:17164409). Expressed in stratified non-
keratinizing squamous epithelium, including oral, esophageal and
ectocervical mucosa and in the Hassall's corpuscles in the thymus.
Also, detected in the stratified epithelium covering the bladder
and ureter (transitional mucosa) (at protein level)
(PubMed:17164409). Expressed in chondrocytes (PubMed:12032915).
Expressed at low levels in resting osteoblasts (PubMed:17907925).
{ECO:0000269|PubMed:11786556, ECO:0000269|PubMed:12032915,
ECO:0000269|PubMed:17164409, ECO:0000269|PubMed:17907925}.
-!- INDUCTION: By activators of Toll-like receptors, such as
lipoteichoic acid (LTA) (TLR2), polyinosine-polycytidylic acid
(poly(I:C), a synthetic analog of dsRNA) (TLR3) and bacterial
lipopolysaccharides (LPS) (TLR4), and by TNF (PubMed:14662828).
Up-regulated in osteoblasts after exposure to invasive, but not
invasion-defective, strains of Salmonella typhimurium (at protein
level) (PubMed:17907925). In macrophages, up-regulated by
endocannabinoid anandamide/AEA (PubMed:23955712).
{ECO:0000269|PubMed:14662828, ECO:0000269|PubMed:17907925,
ECO:0000269|PubMed:23955712}.
-!- DOMAIN: The pyrin domain (also called DAPIN domain or PYD) is
involved in PYCARD-binding. {ECO:0000269|PubMed:24630722}.
-!- DOMAIN: The LRR domain mediates the interaction with IRF4 and PML.
{ECO:0000250|UniProtKB:Q8R4B8, ECO:0000269|PubMed:23430110}.
-!- DOMAIN: Intramolecular interactions between NACHT and leucine-rich
repeat (LRR) domains may be important for autoinhibition in the
absence of activating signal. {ECO:0000250|UniProtKB:Q9EPB4,
ECO:0000305|PubMed:11786556}.
-!- PTM: The disulfide bond in the pyrin domain might play a role in
reactive oxygen species-mediated activation.
{ECO:0000305|PubMed:21880711}.
-!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
polyubiquitination. Ubiquitination does not lead to degradation,
but inhibits inflammasome activation (By similarity).
Deubiquitination is catalyzed by BRCC3 and associated with NLRP3
activation and inflammasome assembly. This process can be induced
by the activation of Toll-like receptors (by LPS), through a non-
transcriptional pathway dependent on the mitochondrial production
of reactive oxygen species, and by ATP.
{ECO:0000250|UniProtKB:Q8R4B8, ECO:0000269|PubMed:22948162}.
-!- DISEASE: Familial cold autoinflammatory syndrome 1 (FCAS1)
[MIM:120100]: A rare autosomal dominant systemic inflammatory
disease characterized by recurrent episodes of maculopapular rash
associated with arthralgias, myalgias, fever and chills, swelling
of the extremities, and conjunctivitis after generalized exposure
to cold. Rarely, some patients may also develop late-onset renal
amyloidosis. {ECO:0000269|PubMed:11687797,
ECO:0000269|PubMed:11992256, ECO:0000269|PubMed:12355493,
ECO:0000269|PubMed:12522564, ECO:0000269|PubMed:15593220,
ECO:0000269|PubMed:17284928, ECO:0000269|PubMed:24952504}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Muckle-Wells syndrome (MWS) [MIM:191900]: A hereditary
periodic fever syndrome characterized by fever, chronic recurrent
urticaria, arthralgias, progressive sensorineural deafness, and
reactive renal amyloidosis. The disease may be severe if
generalized reactive amyloidosis occurs.
{ECO:0000269|PubMed:11687797, ECO:0000269|PubMed:11992256,
ECO:0000269|PubMed:12355493, ECO:0000269|PubMed:15593220,
ECO:0000269|PubMed:24952504}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Chronic infantile neurologic cutaneous and articular
syndrome (CINCA) [MIM:607115]: Rare congenital inflammatory
disorder characterized by a triad of neonatal onset of cutaneous
symptoms, chronic meningitis, and joint manifestations with
recurrent fever and inflammation. {ECO:0000269|PubMed:12032915,
ECO:0000269|PubMed:12483741, ECO:0000269|PubMed:14630794,
ECO:0000269|PubMed:15231984, ECO:0000269|PubMed:15334500,
ECO:0000269|PubMed:15593220, ECO:0000269|PubMed:24952504}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC39910.1; Type=Frameshift; Positions=893, 918, 926; Evidence={ECO:0000305};
Sequence=AAL12497.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL12498.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL33908.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAL65136.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD92128.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG37494.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=INFEVERS; Note=Repertory of FMF and hereditary
autoinflammatory disorders mutations;
URL="http://fmf.igh.cnrs.fr/ISSAID/infevers/search.php?n=4";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF410477; AAL33908.1; ALT_INIT; mRNA.
EMBL; AF427617; AAL33911.1; -; mRNA.
EMBL; AY051117; AAL12497.1; ALT_INIT; Genomic_DNA.
EMBL; AY051112; AAL12497.1; JOINED; Genomic_DNA.
EMBL; AY051113; AAL12497.1; JOINED; Genomic_DNA.
EMBL; AY051114; AAL12497.1; JOINED; Genomic_DNA.
EMBL; AY051115; AAL12497.1; JOINED; Genomic_DNA.
EMBL; AY051116; AAL12497.1; JOINED; Genomic_DNA.
EMBL; AY056059; AAL12497.1; JOINED; Genomic_DNA.
EMBL; AY056060; AAL12497.1; JOINED; Genomic_DNA.
EMBL; AY051117; AAL12498.1; ALT_INIT; Genomic_DNA.
EMBL; AY051112; AAL12498.1; JOINED; Genomic_DNA.
EMBL; AY051113; AAL12498.1; JOINED; Genomic_DNA.
EMBL; AY051114; AAL12498.1; JOINED; Genomic_DNA.
EMBL; AY051115; AAL12498.1; JOINED; Genomic_DNA.
EMBL; AY051116; AAL12498.1; JOINED; Genomic_DNA.
EMBL; AF468522; AAL78632.1; -; mRNA.
EMBL; AF420469; AAL65136.1; ALT_INIT; mRNA.
EMBL; AY092033; AAM14669.1; -; mRNA.
EMBL; AF418985; AAL14640.2; -; mRNA.
EMBL; AK314998; BAG37494.1; ALT_INIT; mRNA.
EMBL; AB208891; BAD92128.1; ALT_INIT; mRNA.
EMBL; AC104335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL606804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471148; EAW77184.1; -; Genomic_DNA.
EMBL; CH471148; EAW77186.1; -; Genomic_DNA.
EMBL; BC117211; AAI17212.1; -; mRNA.
EMBL; BC143359; AAI43360.1; -; mRNA.
EMBL; BC143362; AAI43363.1; -; mRNA.
EMBL; BC143363; AAI43364.1; -; mRNA.
EMBL; AY422168; AAQ98889.1; -; mRNA.
EMBL; AF054176; AAC39910.1; ALT_FRAME; mRNA.
CCDS; CCDS1632.1; -. [Q96P20-1]
CCDS; CCDS1633.1; -. [Q96P20-2]
CCDS; CCDS44346.1; -. [Q96P20-5]
CCDS; CCDS44347.1; -. [Q96P20-4]
RefSeq; NP_001073289.1; NM_001079821.2. [Q96P20-1]
RefSeq; NP_001120933.1; NM_001127461.2. [Q96P20-5]
RefSeq; NP_001120934.1; NM_001127462.2. [Q96P20-4]
RefSeq; NP_001230062.1; NM_001243133.1.
RefSeq; NP_004886.3; NM_004895.4. [Q96P20-1]
RefSeq; NP_899632.1; NM_183395.2. [Q96P20-2]
RefSeq; XP_011542350.1; XM_011544048.2. [Q96P20-1]
RefSeq; XP_016855670.1; XM_017000181.1. [Q96P20-1]
RefSeq; XP_016855671.1; XM_017000182.1. [Q96P20-1]
RefSeq; XP_016855672.1; XM_017000183.1. [Q96P20-4]
RefSeq; XP_016855673.1; XM_017000184.1. [Q96P20-2]
UniGene; Hs.159483; -.
PDB; 2NAQ; NMR; -; A=3-93.
PDB; 3QF2; X-ray; 1.70 A; A/B=3-112.
PDBsum; 2NAQ; -.
PDBsum; 3QF2; -.
ProteinModelPortal; Q96P20; -.
SMR; Q96P20; -.
BioGrid; 125319; 49.
CORUM; Q96P20; -.
DIP; DIP-41153N; -.
IntAct; Q96P20; 38.
MINT; MINT-230535; -.
STRING; 9606.ENSP00000337383; -.
BindingDB; Q96P20; -.
ChEMBL; CHEMBL1741208; -.
GuidetoPHARMACOLOGY; 1770; -.
iPTMnet; Q96P20; -.
PhosphoSitePlus; Q96P20; -.
BioMuta; NLRP3; -.
DMDM; 262527566; -.
EPD; Q96P20; -.
PaxDb; Q96P20; -.
PeptideAtlas; Q96P20; -.
PRIDE; Q96P20; -.
Ensembl; ENST00000336119; ENSP00000337383; ENSG00000162711. [Q96P20-1]
Ensembl; ENST00000348069; ENSP00000294752; ENSG00000162711. [Q96P20-2]
Ensembl; ENST00000366496; ENSP00000355452; ENSG00000162711. [Q96P20-5]
Ensembl; ENST00000366497; ENSP00000355453; ENSG00000162711. [Q96P20-5]
Ensembl; ENST00000391827; ENSP00000375703; ENSG00000162711. [Q96P20-4]
Ensembl; ENST00000391828; ENSP00000375704; ENSG00000162711. [Q96P20-1]
GeneID; 114548; -.
KEGG; hsa:114548; -.
UCSC; uc001icr.4; human. [Q96P20-1]
CTD; 114548; -.
DisGeNET; 114548; -.
EuPathDB; HostDB:ENSG00000162711.16; -.
GeneCards; NLRP3; -.
HGNC; HGNC:16400; NLRP3.
HPA; HPA012878; -.
MalaCards; NLRP3; -.
MIM; 120100; phenotype.
MIM; 191900; phenotype.
MIM; 606416; gene.
MIM; 607115; phenotype.
neXtProt; NX_Q96P20; -.
OpenTargets; ENSG00000162711; -.
Orphanet; 93365; CINCA syndrome with NLRP3 mutations.
Orphanet; 47045; Familial cold urticaria.
Orphanet; 575; Muckle-Wells syndrome.
PharmGKB; PA26512; -.
eggNOG; ENOG410IE5X; Eukaryota.
eggNOG; ENOG4111H3D; LUCA.
GeneTree; ENSGT00860000133669; -.
HOVERGEN; HBG063656; -.
InParanoid; Q96P20; -.
KO; K12800; -.
OMA; PVHTVVF; -.
OrthoDB; EOG091G01CG; -.
PhylomeDB; Q96P20; -.
TreeFam; TF340267; -.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-844456; The NLRP3 inflammasome.
GeneWiki; NALP3; -.
GenomeRNAi; 114548; -.
PRO; PR:Q96P20; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162711; -.
Genevisible; Q96P20; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0072559; C:NLRP3 inflammasome complex; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042834; F:peptidoglycan binding; TAS:HGNC.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
GO; GO:0006952; P:defense response; TAS:HGNC.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0009595; P:detection of biotic stimulus; TAS:HGNC.
GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0032611; P:interleukin-1 beta production; IEA:Ensembl.
GO; GO:0050701; P:interleukin-1 secretion; IEA:Ensembl.
GO; GO:0032621; P:interleukin-18 production; IEA:Ensembl.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IMP:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:BHF-UCL.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IMP:BHF-UCL.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IDA:HGNC.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:HGNC.
GO; GO:0044546; P:NLRP3 inflammasome complex assembly; IEA:Ensembl.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:HGNC.
GO; GO:0032736; P:positive regulation of interleukin-13 production; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:0032754; P:positive regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:2000321; P:positive regulation of T-helper 17 cell differentiation; IEA:Ensembl.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; ISS:UniProtKB.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0002830; P:positive regulation of type 2 immune response; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051259; P:protein oligomerization; TAS:HGNC.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR004020; DAPIN.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR029495; NACHT-assoc.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF14484; FISNA; 1.
Pfam; PF13516; LRR_6; 4.
Pfam; PF02758; PYRIN; 1.
SMART; SM01288; FISNA; 1.
SMART; SM01289; PYRIN; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS50824; DAPIN; 1.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Amyloidosis;
ATP-binding; Complete proteome; Cytoplasm; Deafness; Disease mutation;
Disulfide bond; Endoplasmic reticulum; Immunity; Inflammasome;
Inflammatory response; Innate immunity; Leucine-rich repeat;
Nucleotide-binding; Nucleus; Reference proteome; Repeat; Secreted;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 1036 NACHT, LRR and PYD domains-containing
protein 3.
/FTId=PRO_0000080886.
DOMAIN 1 93 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 220 536 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 742 762 LRR 1.
REPEAT 771 792 LRR 2.
REPEAT 799 819 LRR 3.
REPEAT 828 849 LRR 4.
REPEAT 856 876 LRR 5.
REPEAT 885 906 LRR 6.
REPEAT 913 933 LRR 7.
REPEAT 942 963 LRR 8.
REPEAT 970 991 LRR 9.
NP_BIND 226 233 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
COMPBIAS 690 697 Poly-Glu.
DISULFID 8 108 Redox-active.
{ECO:0000269|PubMed:21880711}.
VAR_SEQ 720 1036 Missing (in isoform 3).
{ECO:0000303|PubMed:12355493}.
/FTId=VSP_005519.
VAR_SEQ 721 777 Missing (in isoform 1 and isoform 4).
{ECO:0000303|PubMed:11042152,
ECO:0000303|PubMed:11687797,
ECO:0000303|PubMed:12355493,
ECO:0000303|PubMed:14662828,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005520.
VAR_SEQ 776 796 WLGRCGLSHECCFDISLVLSS -> C (in isoform
6). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_053714.
VAR_SEQ 836 892 Missing (in isoform 1 and isoform 5).
{ECO:0000303|PubMed:11042152,
ECO:0000303|PubMed:11687797,
ECO:0000303|PubMed:12355493,
ECO:0000303|PubMed:14662828,
ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.5}.
/FTId=VSP_005521.
VARIANT 174 174 I -> T (in CINCA; dbSNP:rs180177449).
{ECO:0000269|PubMed:15231984}.
/FTId=VAR_043679.
VARIANT 200 200 V -> M (in FCAS1 and MWS;
dbSNP:rs121908147).
{ECO:0000269|PubMed:11687797,
ECO:0000269|PubMed:11992256,
ECO:0000269|PubMed:12355493,
ECO:0000269|PubMed:15593220}.
/FTId=VAR_013227.
VARIANT 262 262 R -> L (in CINCA; dbSNP:rs180177442).
{ECO:0000269|PubMed:14630794}.
/FTId=VAR_043680.
VARIANT 262 262 R -> P (in CINCA; dbSNP:rs180177442).
{ECO:0000269|PubMed:14630794}.
/FTId=VAR_043681.
VARIANT 262 262 R -> W (in FCAS1 and MWS; spontaneous
polymerization into inflammasome speck).
{ECO:0000269|PubMed:11992256,
ECO:0000269|PubMed:12355493,
ECO:0000269|PubMed:24952504}.
/FTId=VAR_014104.
VARIANT 266 266 L -> H (in CINCA; dbSNP:rs180177436).
{ECO:0000269|PubMed:12483741}.
/FTId=VAR_043682.
VARIANT 305 305 D -> G (in CINCA; dbSNP:rs180177447).
{ECO:0000269|PubMed:14630794}.
/FTId=VAR_043683.
VARIANT 305 305 D -> N (in CINCA and MWS; spontaneous
polymerization into inflammasome speck;
dbSNP:rs121908153).
{ECO:0000269|PubMed:11992256,
ECO:0000269|PubMed:12032915,
ECO:0000269|PubMed:12483741,
ECO:0000269|PubMed:14630794,
ECO:0000269|PubMed:15593220,
ECO:0000269|PubMed:24952504}.
/FTId=VAR_014105.
VARIANT 307 307 L -> P (in FCAS1 and MWS;
dbSNP:rs180177431).
{ECO:0000269|PubMed:12355493,
ECO:0000269|PubMed:15593220}.
/FTId=VAR_014124.
VARIANT 308 308 Q -> K (in CINCA; dbSNP:rs180177432).
{ECO:0000269|PubMed:12032915}.
/FTId=VAR_043684.
VARIANT 311 311 F -> S (in CINCA; dbSNP:rs121908154).
{ECO:0000269|PubMed:12032915,
ECO:0000269|PubMed:14630794}.
/FTId=VAR_014106.
VARIANT 350 350 T -> M (in MWS and CINCA; spontaneous
polymerization into inflammasome speck;
dbSNP:rs151344629).
{ECO:0000269|PubMed:11992256,
ECO:0000269|PubMed:14630794,
ECO:0000269|PubMed:15593220,
ECO:0000269|PubMed:24952504}.
/FTId=VAR_014366.
VARIANT 354 354 A -> V (in MWS; dbSNP:rs121908149).
{ECO:0000269|PubMed:11687797}.
/FTId=VAR_013228.
VARIANT 355 355 L -> P (in FCAS1; dbSNP:rs28937896).
{ECO:0000269|PubMed:12522564}.
/FTId=VAR_043685.
VARIANT 356 356 E -> D (in CINCA; dbSNP:rs180177444).
{ECO:0000269|PubMed:14630794}.
/FTId=VAR_043686.
VARIANT 360 360 H -> R (in CINCA; dbSNP:rs180177434).
{ECO:0000269|PubMed:12032915}.
/FTId=VAR_014367.
VARIANT 407 407 T -> P (in CINCA; dbSNP:rs180177445).
{ECO:0000269|PubMed:14630794}.
/FTId=VAR_043687.
VARIANT 438 438 T -> I (in CINCA; dbSNP:rs180177433).
{ECO:0000269|PubMed:14630794}.
/FTId=VAR_043688.
VARIANT 438 438 T -> N (in CINCA; dbSNP:rs180177433).
{ECO:0000269|PubMed:12032915}.
/FTId=VAR_014368.
VARIANT 441 441 A -> T (in MWS; dbSNP:rs180177430).
{ECO:0000269|PubMed:11992256}.
/FTId=VAR_014369.
VARIANT 441 441 A -> V (in FCAS1; dbSNP:rs121908146).
{ECO:0000269|PubMed:11687797}.
/FTId=VAR_013229.
VARIANT 490 490 R -> K (in FCAS1; dbSNP:rs145268073).
{ECO:0000269|PubMed:15593220}.
/FTId=VAR_043689.
VARIANT 525 525 F -> C (in FCAS1; dbSNP:rs180177478).
{ECO:0000269|PubMed:17284928}.
/FTId=VAR_031853.
VARIANT 525 525 F -> L (in CINCA; dbSNP:rs180177439).
{ECO:0000269|PubMed:12483741}.
/FTId=VAR_043690.
VARIANT 571 571 G -> R (in MWS; dbSNP:rs121908151).
{ECO:0000269|PubMed:11992256}.
/FTId=VAR_014107.
VARIANT 572 572 Y -> C (in CINCA; dbSNP:rs180177438).
{ECO:0000269|PubMed:12483741,
ECO:0000269|PubMed:14630794}.
/FTId=VAR_043691.
VARIANT 575 575 F -> S (in CINCA; dbSNP:rs121908152).
{ECO:0000269|PubMed:12032915}.
/FTId=VAR_014108.
VARIANT 629 629 E -> G (in FCAS1; dbSNP:rs121908148).
{ECO:0000269|PubMed:11687797}.
/FTId=VAR_013230.
VARIANT 634 634 L -> F (in CINCA; dbSNP:rs180177446).
{ECO:0000269|PubMed:14630794}.
/FTId=VAR_043692.
VARIANT 664 664 M -> T (in CINCA; dbSNP:rs180177435).
{ECO:0000269|PubMed:12032915}.
/FTId=VAR_014370.
VARIANT 705 705 Q -> K (in dbSNP:rs35829419).
{ECO:0000269|PubMed:12522564}.
/FTId=VAR_043693.
VARIANT 861 861 Y -> C (in CINCA; dbSNP:rs180177452).
{ECO:0000269|PubMed:15334500}.
/FTId=VAR_023551.
MUTAGEN 15 15 E->R: Complete loss of PYCARD filament
nucleation.
{ECO:0000269|PubMed:24630722}.
MUTAGEN 22 23 LK->PA: Loss of PYCARD-binding. No effect
on GBP5-binding.
{ECO:0000269|PubMed:22461501}.
MUTAGEN 23 23 K->E: Complete loss of PYCARD filament
nucleation; when associated with E-24.
{ECO:0000269|PubMed:24630722}.
MUTAGEN 24 24 K->E: Complete loss of PYCARD filament
nucleation; when associated with E-23.
{ECO:0000269|PubMed:24630722}.
MUTAGEN 27 27 M->E: Complete loss of PYCARD filament
nucleation.
{ECO:0000269|PubMed:24630722}.
MUTAGEN 43 43 R->W: Complete loss of PYCARD filament
nucleation.
{ECO:0000269|PubMed:24630722}.
MUTAGEN 64 64 E->R: Complete loss of PYCARD filament
nucleation.
{ECO:0000269|PubMed:24630722}.
MUTAGEN 82 82 D->R: Complete loss of PYCARD filament
nucleation.
{ECO:0000269|PubMed:24630722}.
CONFLICT 167 167 R -> L (in Ref. 2; AAL78632/AAM14669/
AAL14640). {ECO:0000305}.
CONFLICT 323 323 Q -> H (in Ref. 2; AAL78632/AAM14669/
AAL14640). {ECO:0000305}.
CONFLICT 439 439 T -> S (in Ref. 10; AAC39910).
{ECO:0000305}.
CONFLICT 523 523 M -> V (in Ref. 5; BAG37494).
{ECO:0000305}.
CONFLICT 599 599 K -> M (in Ref. 10; AAC39910).
{ECO:0000305}.
CONFLICT 617 617 K -> N (in Ref. 2; AAL78632/AAM14669/
AAL14640). {ECO:0000305}.
CONFLICT 622 623 QI -> HD (in Ref. 10; AAC39910).
{ECO:0000305}.
HELIX 6 15 {ECO:0000244|PDB:3QF2}.
HELIX 19 30 {ECO:0000244|PDB:3QF2}.
STRAND 34 37 {ECO:0000244|PDB:3QF2}.
HELIX 43 48 {ECO:0000244|PDB:3QF2}.
HELIX 51 62 {ECO:0000244|PDB:3QF2}.
HELIX 64 77 {ECO:0000244|PDB:3QF2}.
HELIX 81 89 {ECO:0000244|PDB:3QF2}.
SEQUENCE 1036 AA; 118173 MW; 4C1DFB2B5B283CE8 CRC64;
MKMASTRCKL ARYLEDLEDV DLKKFKMHLE DYPPQKGCIP LPRGQTEKAD HVDLATLMID
FNGEEKAWAM AVWIFAAINR RDLYEKAKRD EPKWGSDNAR VSNPTVICQE DSIEEEWMGL
LEYLSRISIC KMKKDYRKKY RKYVRSRFQC IEDRNARLGE SVSLNKRYTR LRLIKEHRSQ
QEREQELLAI GKTKTCESPV SPIKMELLFD PDDEHSEPVH TVVFQGAAGI GKTILARKMM
LDWASGTLYQ DRFDYLFYIH CREVSLVTQR SLGDLIMSCC PDPNPPIHKI VRKPSRILFL
MDGFDELQGA FDEHIGPLCT DWQKAERGDI LLSSLIRKKL LPEASLLITT RPVALEKLQH
LLDHPRHVEI LGFSEAKRKE YFFKYFSDEA QARAAFSLIQ ENEVLFTMCF IPLVCWIVCT
GLKQQMESGK SLAQTSKTTT AVYVFFLSSL LQPRGGSQEH GLCAHLWGLC SLAADGIWNQ
KILFEESDLR NHGLQKADVS AFLRMNLFQK EVDCEKFYSF IHMTFQEFFA AMYYLLEEEK
EGRTNVPGSR LKLPSRDVTV LLENYGKFEK GYLIFVVRFL FGLVNQERTS YLEKKLSCKI
SQQIRLELLK WIEVKAKAKK LQIQPSQLEL FYCLYEMQEE DFVQRAMDYF PKIEINLSTR
MDHMVSSFCI ENCHRVESLS LGFLHNMPKE EEEEEKEGRH LDMVQCVLPS SSHAACSHGL
VNSHLTSSFC RGLFSVLSTS QSLTELDLSD NSLGDPGMRV LCETLQHPGC NIRRLWLGRC
GLSHECCFDI SLVLSSNQKL VELDLSDNAL GDFGIRLLCV GLKHLLCNLK KLWLVSCCLT
SACCQDLASV LSTSHSLTRL YVGENALGDS GVAILCEKAK NPQCNLQKLG LVNSGLTSVC
CSALSSVLST NQNLTHLYLR GNTLGDKGIK LLCEGLLHPD CKLQVLELDN CNLTSHCCWD
LSTLLTSSQS LRKLSLGNND LGDLGVMMFC EVLKQQSCLL QNLGLSEMYF NYETKSALET
LQEEKPELTV VFEPSW


Related products :

Catalog number Product name Quantity
EIAAB26333 Angiotensin_vasopressin receptor AII_AVP-like,C1orf7,Caterpiller protein 1.1,CIAS1,CLR1.1,Cold autoinflammatory syndrome 1 protein,Cryopyrin,Homo sapiens,Human,NACHT, LRR and PYD domains-containing pr
EIAAB26332 Cias1,Cold autoinflammatory syndrome 1 protein homolog,Cryopyrin,Mast cell maturation-associated-inducible protein 1,Mmig1,Mouse,Mus musculus,NACHT, LRR and PYD domains-containing protein 3,Nalp3,Nlrp
20-272-191261 NALP3 - Mouse monoclonal [Nalpy3 - a] to NALP3; Cold autoinflammatory syndrome 1 protein; Cryopyrin; PYRIN-containing APAF1-like protein 1; Angiotensin_vasopressin receptor AII_AVP-like Monoclonal 0.05 mg
20-272-191451 NALP3 - Mouse monoclonal [nalpy3-b] to NALP3; Cold autoinflammatory syndrome 1 protein; Cryopyrin; PYRIN-containing APAF1-like protein 1; Angiotensin_vasopressin receptor AII_AVP-like Monoclonal 0.05 mg
EIAAB26341 Angiotensin II_vasopressin receptor,Avr,NACHT, LRR and PYD domains-containing protein 6,Nalp6,Nlrp6,Pypaf5,PYRIN-containing APAF1-like protein 5-like,Rat,Rattus norvegicus
EIAAB26335 Cancer_testis antigen 58,CT58,Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 4,NALP4,NLRP4,PAAD and NACHT-containing protein 2,PAN2,PYPAF4,PYRIN and NACHT-containing protein 2,PYRIN-
EIAAB26342 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 7,NALP7,NLRP7,NOD12,Nucleotide-binding oligomerization domain protein 12,PYPAF3,PYRIN-containing APAF1-like protein 3
EIAAB26340 Mouse,Mus musculus,NACHT, LRR and PYD domains-containing protein 6,Nalp6,Nlrp6,Pypaf5,PYRIN-containing APAF1-like protein 5-like
EIAAB26339 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 6,NALP6,NLRP6,PYPAF5,PYRIN-containing APAF1-like protein 5
EIAAB26331 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 2,NALP2,NBS1,NLRP2,Nucleotide-binding site protein 1,PAN1,PYPAF2,PYRIN domain and NACHT domain-containing protein 1,PYRIN-containing AP
EIAAB26310 Homo sapiens,Human,Monarch-1,NACHT, LRR and PYD domains-containing protein 12,NALP12,NLRP12,PYPAF7,PYRIN-containing APAF1-like protein 7,Regulated by nitric oxide,RNO
EIAAB26343 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 8,NALP8,NLRP8,NOD16,Nucleotide-binding oligomerization domain protein 16,PAN4,PYRIN and NACHT-containing protein 4
EIAAB26344 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 9,NALP9,NLRP9,NOD6,Nucleotide-binding oligomerization domain protein 6,PAN12,PYRIN and NACHT-containing protein 12
EIAAB26309 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 11,NALP11,NLRP11,NOD17,Nucleotide-binding oligomerization domain protein 17,PAAD-and NACHT domain-containing protein 10,PAN10,PYPAF6,PY
EIAAB26330 CARD7,Caspase recruitment domain-containing protein 7,Death effector filament-forming ced-4-like apoptosis protein,DEFCAP,Homo sapiens,Human,KIAA0926,NAC,NACHT, LRR and PYD domains-containing protein
EIAAB26336 Mater,Mater protein,Maternal antigen that embryos require,Mouse,Mus musculus,NACHT, LRR and PYD domains-containing protein 5,Nalp5,Nlrp5,Ooplasm-specific protein 1,OP1
P3463Rb Rabbit anti_ cold autoinflammatory syndrome 1 pol 40ug/0.2ml
EIAAB33260 ASC2,ASCI,Homo sapiens,Human,PAAD-only protein 1,POP1,PYC1,PYDC1,Pyrin domain-containing protein 1,Pyrin-only protein 1
EIAAB26311 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 13,NALP13,NLRP13,NOD14,Nucleotide-binding oligomerization domain protein 14
EIAAB26313 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 14,NALP14,NLRP14,NOD5,Nucleotide-binding oligomerization domain protein 5
EIAAB26307 Homo sapiens,Human,NACHT, LRR and PYD domains-containing protein 10,NALP10,NLRP10,NOD8,Nucleotide-binding oligomerization domain protein 8,PYNOD
18-461-10751 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10472 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-003-44260 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein-coupling receptor PEIG-1 Polyclonal 0.05 mg Aff Pur
18-461-10473 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur