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NACHT, LRR and PYD domains-containing protein 12 (Monarch-1) (PYRIN-containing APAF1-like protein 7) (Regulated by nitric oxide)

 NAL12_HUMAN             Reviewed;        1061 AA.
P59046; A8MTQ2; B3KTE7; Q8NEU4; Q9BY26;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
22-AUG-2003, sequence version 2.
05-JUN-2019, entry version 164.
RecName: Full=NACHT, LRR and PYD domains-containing protein 12;
AltName: Full=Monarch-1;
AltName: Full=PYRIN-containing APAF1-like protein 7;
AltName: Full=Regulated by nitric oxide;
Name=NLRP12; Synonyms=NALP12, PYPAF7, RNO;
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 1).
PubMed=12019269; DOI=10.1074/jbc.M203915200;
Wang L., Manji G.A., Grenier J.M., Al-Garawi A., Merriam S.,
Lora J.M., Geddes B.J., Briskin M., DiStefano P.S., Bertin J.;
"PYPAF7, a novel PYRIN-containing Apaf1-like protein that regulates
activation of NF-kappa B and caspase-1-dependent cytokine
processing.";
J. Biol. Chem. 277:29874-29880(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=12563287; DOI=10.1038/nrm1019;
Tschopp J., Martinon F., Burns K.;
"NALPs: a novel protein family involved in inflammation.";
Nat. Rev. Mol. Cell Biol. 4:95-104(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 7).
TISSUE=Lymphoma;
Williams K.L., Linhoff M.W., Harton J.A., Ting J.P.Y.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY,
ALTERNATIVE SPLICING, AND INDUCTION.
TISSUE=Peripheral blood leukocyte;
PubMed=11167794; DOI=10.1046/j.1365-2141.2001.02491.x;
Shami P.J., Kanai N., Wang L.Y., Vreeke T.M., Parker C.J.;
"Identification and characterization of a novel gene that is
upregulated in leukaemia cells by nitric oxide.";
Br. J. Haematol. 112:138-147(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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] (ISOFORM 1).
TISSUE=Leukocyte;
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]
FUNCTION, AND INTERACTION WITH MAP3K14.
PubMed=17237370;
Lich J.D., Williams K.L., Moore C.B., Arthur J.C., Davis B.K.,
Taxman D.J., Ting J.P.;
"Monarch-1 suppresses non-canonical NF-kappaB activation and p52-
dependent chemokine expression in monocytes.";
J. Immunol. 178:1256-1260(2007).
[10]
FUNCTION, AND INTERACTION WITH HSPA8; HSPA1A AND HSP90AA1.
PubMed=17947705;
Arthur J.C., Lich J.D., Aziz R.K., Kotb M., Ting J.P.;
"Heat shock protein 90 associates with monarch-1 and regulates its
ability to promote degradation of NF-kappaB-inducing kinase.";
J. Immunol. 179:6291-6296(2007).
[11]
ATP-BINDING.
PubMed=18160710; DOI=10.1128/MCB.01468-07;
Ye Z., Lich J.D., Moore C.B., Duncan J.A., Williams K.L., Ting J.P.;
"ATP binding by monarch-1/NLRP12 is critical for its inhibitory
function.";
Mol. Cell. Biol. 28:1841-1850(2008).
[12]
INVOLVEMENT IN FCAS2.
PubMed=18230725; DOI=10.1073/pnas.0708616105;
Jeru I., Duquesnoy P., Fernandes-Alnemri T., Cochet E., Yu J.W.,
Lackmy-Port-Lis M., Grimprel E., Landman-Parker J., Hentgen V.,
Marlin S., McElreavey K., Sarkisian T., Grateau G., Alnemri E.S.,
Amselem S.;
"Mutations in NALP12 cause hereditary periodic fever syndromes.";
Proc. Natl. Acad. Sci. U.S.A. 105:1614-1619(2008).
[13]
FUNCTION, AND INTERACTION WITH NOD2 AND HSP90AA1.
PubMed=30559449; DOI=10.1038/s41467-018-07750-5;
Normand S., Waldschmitt N., Neerincx A., Martinez-Torres R.J.,
Chauvin C., Couturier-Maillard A., Boulard O., Cobret L., Awad F.,
Huot L., Ribeiro-Ribeiro A., Lautz K., Ruez R., Delacre M., Bondu C.,
Guilliams M., Scott C., Segal A., Amselem S., Hot D., Karabina S.,
Bohn E., Ryffel B., Poulin L.F., Kufer T.A., Chamaillard M.;
"Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes
bacterial tolerance and colonization by enteropathogens.";
Nat. Commun. 9:5338-5338(2018).
[14]
FUNCTION, INTERACTION WITH TRIM25, AND SUBCELLULAR LOCATION.
PubMed=30902577; DOI=10.1016/j.chom.2019.02.013;
Chen S.T., Chen L., Lin D.S., Chen S.Y., Tsao Y.P., Guo H., Li F.J.,
Tseng W.T., Tam J.W., Chao C.W., Brickey W.J., Dzhagalov I.,
Song M.J., Kang H.R., Jung J.U., Ting J.P.;
"NLRP12 Regulates Anti-viral RIG-I Activation via Interaction with
TRIM25.";
Cell Host Microbe 0:0-0(2019).
[15]
STRUCTURE BY NMR OF 1-98, AND INTERACTION WITH FAF1.
PubMed=21978668; DOI=10.1016/j.jmb.2011.09.024;
Pinheiro A.S., Eibl C., Ekman-Vural Z., Schwarzenbacher R., Peti W.;
"The NLRP12 pyrin domain: structure, dynamics, and functional
insights.";
J. Mol. Biol. 413:790-803(2011).
[16]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 9-106.
PubMed=28112203; DOI=10.1038/srep40991;
Jin T., Chuenchor W., Jiang J., Cheng J., Li Y., Fang K., Huang M.,
Smith P., Xiao T.S.;
"Design of an expression system to enhance MBP-mediated
crystallization.";
Sci. Rep. 7:40991-40991(2017).
-!- FUNCTION: Plays an essential role as an potent mitigator of
inflammation (PubMed:30559449). Primarily expressed in dendritic
cells and macrophages, inhibits both canonical and non-canonical
NF-kappa-B and ERK activation pathways (PubMed:15489334,
PubMed:17947705). Functions as a negative regulator of NOD2 by
targeting it to degradation via the proteasome pathway
(PubMed:30559449). In turn, promotes bacterial tolerance
(PubMed:30559449). Inhibits also the DDX58-mediated immune
signaling against RNA viruses by reducing the E3 ubiquitin ligase
TRIM25-mediated 'Lys-63'-linked DDX58 activation but enhancing the
E3 ubiquitin ligase RNF125-mediated 'Lys-48'-linked DDX58
degradation (PubMed:30902577). Acts also as a negative regulator
of inflammatory response to mitigate obesity and obesity-
associated diseases in adipose tissue (By similarity).
{ECO:0000250|UniProtKB:E9Q5R7, ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17947705, ECO:0000269|PubMed:30559449,
ECO:0000269|PubMed:30902577}.
-!- SUBUNIT: Interacts (via pyrin domain) with ASC. Interacts (via
pyrin domain) with FAF1 (via UBA domain) (PubMed:21978668).
Interacts with MAP3K14; this interaction promotes proteasomal
degradation of MAP3K14 (PubMed:17237370). Interacts with NOD2;
this interaction promotes degradation of NOD2 through the
ubiquitin-proteasome pathway (PubMed:30559449). Interacts with
HSPA1A and HSPA8 (PubMed:17947705). Interacts with HSP90AA1
(PubMed:17947705, PubMed:30559449). Interacts with TRIM25; this
interaction inhibits DDX58-mediated signaling pathway
(PubMed:30902577). {ECO:0000269|PubMed:17237370,
ECO:0000269|PubMed:17947705, ECO:0000269|PubMed:21978668,
ECO:0000269|PubMed:30559449, ECO:0000269|PubMed:30902577}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30902577}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=1; Synonyms=I;
IsoId=P59046-1; Sequence=Displayed;
Name=2; Synonyms=II;
IsoId=P59046-2; Sequence=VSP_005524;
Name=3; Synonyms=III;
IsoId=P59046-3; Sequence=VSP_005523;
Name=4; Synonyms=IV;
IsoId=P59046-4; Sequence=VSP_009879;
Name=5; Synonyms=rno-2;
IsoId=P59046-5; Sequence=VSP_016908, VSP_016909, VSP_016910;
Name=6;
IsoId=P59046-6; Sequence=VSP_054622;
Note=No experimental confirmation available.;
Name=7;
IsoId=P59046-7; Sequence=VSP_055193;
Note=No experimental confirmation.;
-!- TISSUE SPECIFICITY: Detected only in peripheral blood leukocytes,
predominantly in eosinophils and granulocytes, and at lower levels
in monocytes. {ECO:0000269|PubMed:11167794}.
-!- INDUCTION: By nitric oxide and DMSO in HL-60 cells, an acute
myeloid leukemia cell line. {ECO:0000269|PubMed:11167794}.
-!- DISEASE: Familial cold autoinflammatory syndrome 2 (FCAS2)
[MIM:611762]: 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. {ECO:0000269|PubMed:18230725}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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EMBL; AY095146; AAM18227.1; -; mRNA.
EMBL; AY154467; AAO18163.1; -; mRNA.
EMBL; AY116204; AAM75142.1; -; mRNA.
EMBL; AY116205; AAM75143.1; -; mRNA.
EMBL; AY116206; AAM75144.1; -; mRNA.
EMBL; AY116207; AAM75145.1; -; mRNA.
EMBL; AF231021; AAK14942.1; -; mRNA.
EMBL; AK095460; BAG53059.1; -; mRNA.
EMBL; AC008753; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW72152.1; -; Genomic_DNA.
EMBL; BC028069; AAH28069.1; -; mRNA.
CCDS; CCDS12864.1; -. [P59046-1]
CCDS; CCDS62784.1; -. [P59046-6]
CCDS; CCDS62785.1; -. [P59046-7]
RefSeq; NP_001264055.1; NM_001277126.1. [P59046-7]
RefSeq; NP_001264058.1; NM_001277129.1. [P59046-6]
RefSeq; NP_653288.1; NM_144687.3. [P59046-1]
PDB; 2L6A; NMR; -; A=1-98.
PDB; 4XHS; X-ray; 1.70 A; A/B=10-106.
PDB; 5H7N; X-ray; 1.85 A; A/B=9-106.
PDBsum; 2L6A; -.
PDBsum; 4XHS; -.
PDBsum; 5H7N; -.
SMR; P59046; -.
BioGrid; 124861; 5.
IntAct; P59046; 26.
MINT; P59046; -.
STRING; 9606.ENSP00000375653; -.
iPTMnet; P59046; -.
PhosphoSitePlus; P59046; -.
BioMuta; NLRP12; -.
DMDM; 34223733; -.
jPOST; P59046; -.
PaxDb; P59046; -.
PeptideAtlas; P59046; -.
PRIDE; P59046; -.
ProteomicsDB; 57117; -.
ProteomicsDB; 57118; -. [P59046-2]
ProteomicsDB; 57119; -. [P59046-3]
ProteomicsDB; 57120; -. [P59046-4]
ProteomicsDB; 57121; -. [P59046-5]
DNASU; 91662; -.
Ensembl; ENST00000324134; ENSP00000319377; ENSG00000142405. [P59046-1]
Ensembl; ENST00000391773; ENSP00000375653; ENSG00000142405. [P59046-7]
Ensembl; ENST00000391775; ENSP00000375655; ENSG00000142405. [P59046-6]
GeneID; 91662; -.
KEGG; hsa:91662; -.
UCSC; uc002qch.6; human. [P59046-1]
CTD; 91662; -.
DisGeNET; 91662; -.
GeneCards; NLRP12; -.
HGNC; HGNC:22938; NLRP12.
HPA; HPA042981; -.
MalaCards; NLRP12; -.
MIM; 609648; gene.
MIM; 611762; phenotype.
neXtProt; NX_P59046; -.
OpenTargets; ENSG00000142405; -.
Orphanet; 247868; NLRP12-associated hereditary periodic fever syndrome.
PharmGKB; PA162397866; -.
eggNOG; ENOG410IE5X; Eukaryota.
eggNOG; ENOG4111H3D; LUCA.
GeneTree; ENSGT00940000160873; -.
HOGENOM; HOG000294064; -.
InParanoid; P59046; -.
KO; K20865; -.
OMA; LCRLSAY; -.
OrthoDB; 114368at2759; -.
PhylomeDB; P59046; -.
TreeFam; TF340267; -.
EvolutionaryTrace; P59046; -.
GeneWiki; NLRP12; -.
GenomeRNAi; 91662; -.
PRO; PR:P59046; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000142405; Expressed in 61 organ(s), highest expression level in blood.
ExpressionAtlas; P59046; baseline and differential.
Genevisible; P59046; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; NAS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; NAS:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; IBA:GO_Central.
GO; GO:0036336; P:dendritic cell migration; IEA:Ensembl.
GO; GO:0050710; P:negative regulation of cytokine secretion; IDA:HGNC.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:HGNC.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:BHF-UCL.
GO; GO:0050711; P:negative regulation of interleukin-1 secretion; IDA:HGNC.
GO; GO:0045409; P:negative regulation of interleukin-6 biosynthetic process; IDA:HGNC.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:HGNC.
GO; GO:0009968; P:negative regulation of signal transduction; IDA:HGNC.
GO; GO:0045751; P:negative regulation of Toll signaling pathway; IDA:HGNC.
GO; GO:0050729; P:positive regulation of inflammatory response; NAS:UniProtKB.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; NAS:UniProtKB.
GO; GO:0045345; P:positive regulation of MHC class I biosynthetic process; IDA:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
GO; GO:0045381; P:regulation of interleukin-18 biosynthetic process; NAS:UniProtKB.
GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR004020; DAPIN.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR029495; NACHT-assoc.
InterPro; IPR007111; NACHT_NTPase.
InterPro; IPR041267; NLRC_HD2.
InterPro; IPR041075; NOD2_WH.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF14484; FISNA; 1.
Pfam; PF13516; LRR_6; 5.
Pfam; PF05729; NACHT; 1.
Pfam; PF17776; NLRC4_HD2; 1.
Pfam; PF17779; NOD2_WH; 1.
Pfam; PF02758; PYRIN; 1.
SMART; SM01288; FISNA; 1.
SMART; SM01289; PYRIN; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50824; DAPIN; 1.
PROSITE; PS51450; LRR; 5.
PROSITE; PS50837; NACHT; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Leucine-rich repeat; Nucleotide-binding; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 1061 NACHT, LRR and PYD domains-containing
protein 12.
/FTId=PRO_0000080899.
DOMAIN 1 95 Pyrin. {ECO:0000255|PROSITE-
ProRule:PRU00061}.
DOMAIN 211 528 NACHT. {ECO:0000255|PROSITE-
ProRule:PRU00136}.
REPEAT 828 848 LRR 1.
REPEAT 857 878 LRR 2.
REPEAT 885 906 LRR 3.
REPEAT 914 935 LRR 4.
REPEAT 942 962 LRR 5.
REPEAT 971 992 LRR 6.
REPEAT 999 1020 LRR 7.
REPEAT 1028 1049 LRR 8.
NP_BIND 217 224 ATP.
VAR_SEQ 1 717 Missing (in isoform 5).
{ECO:0000303|PubMed:11167794}.
/FTId=VSP_016908.
VAR_SEQ 691 691 L -> LR (in isoform 7).
{ECO:0000303|Ref.3}.
/FTId=VSP_055193.
VAR_SEQ 718 748 LSLYRNALGSRGVKLLCQGLRHPNCKLQNLR -> MSQAWW
HTSVSPATQEAKAGGLLQPRRQRLW (in isoform 5).
{ECO:0000303|PubMed:11167794}.
/FTId=VSP_016909.
VAR_SEQ 862 1031 Missing (in isoform 4).
{ECO:0000303|Ref.3}.
/FTId=VSP_009879.
VAR_SEQ 862 973 Missing (in isoform 3).
{ECO:0000303|Ref.3}.
/FTId=VSP_005523.
VAR_SEQ 920 976 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054622.
VAR_SEQ 921 977 Missing (in isoform 5).
{ECO:0000303|PubMed:11167794}.
/FTId=VSP_016910.
VAR_SEQ 976 1031 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_005524.
VARIANT 39 39 G -> V (in dbSNP:rs34436714).
/FTId=VAR_053620.
VARIANT 402 402 F -> L (in dbSNP:rs34971363).
/FTId=VAR_053621.
CONFLICT 648 648 M -> T (in Ref. 5; BAG53059).
{ECO:0000305}.
HELIX 10 17 {ECO:0000244|PDB:4XHS}.
HELIX 22 35 {ECO:0000244|PDB:4XHS}.
TURN 37 40 {ECO:0000244|PDB:2L6A}.
HELIX 45 48 {ECO:0000244|PDB:4XHS}.
HELIX 53 64 {ECO:0000244|PDB:4XHS}.
HELIX 66 77 {ECO:0000244|PDB:4XHS}.
TURN 78 81 {ECO:0000244|PDB:4XHS}.
HELIX 83 90 {ECO:0000244|PDB:4XHS}.
STRAND 95 98 {ECO:0000244|PDB:2L6A}.
SEQUENCE 1061 AA; 120173 MW; 8C10AFE4907C131B CRC64;
MLRTAGRDGL CRLSTYLEEL EAVELKKFKL YLGTATELGE GKIPWGSMEK AGPLEMAQLL
ITHFGPEEAW RLALSTFERI NRKDLWERGQ REDLVRDTPP GGPSSLGNQS TCLLEVSLVT
PRKDPQETYR DYVRRKFRLM EDRNARLGEC VNLSHRYTRL LLVKEHSNPM QVQQQLLDTG
RGHARTVGHQ ASPIKIETLF EPDEERPEPP RTVVMQGAAG IGKSMLAHKV MLDWADGKLF
QGRFDYLFYI NCREMNQSAT ECSMQDLIFS CWPEPSAPLQ ELIRVPERLL FIIDGFDELK
PSFHDPQGPW CLCWEEKRPT ELLLNSLIRK KLLPELSLLI TTRPTALEKL HRLLEHPRHV
EILGFSEAER KEYFYKYFHN AEQAGQVFNY VRDNEPLFTM CFVPLVCWVV CTCLQQQLEG
GGLLRQTSRT TTAVYMLYLL SLMQPKPGAP RLQPPPNQRG LCSLAADGLW NQKILFEEQD
LRKHGLDGED VSAFLNMNIF QKDINCERYY SFIHLSFQEF FAAMYYILDE GEGGAGPDQD
VTRLLTEYAF SERSFLALTS RFLFGLLNEE TRSHLEKSLC WKVSPHIKMD LLQWIQSKAQ
SDGSTLQQGS LEFFSCLYEI QEEEFIQQAL SHFQVIVVSN IASKMEHMVS SFCLKRCRSA
QVLHLYGATY SADGEDRARC SAGAHTLLVQ LPERTVLLDA YSEHLAAALC TNPNLIELSL
YRNALGSRGV KLLCQGLRHP NCKLQNLRLK RCRISSSACE DLSAALIANK NLTRMDLSGN
GVGFPGMMLL CEGLRHPQCR LQMIQLRKCQ LESGACQEMA SVLGTNPHLV ELDLTGNALE
DLGLRLLCQG LRHPVCRLRT LWLKICRLTA AACDELASTL SVNQSLRELD LSLNELGDLG
VLLLCEGLRH PTCKLQTLRL GICRLGSAAC EGLSVVLQAN HNLRELDLSF NDLGDWGLWL
LAEGLQHPAC RLQKLWLDSC GLTAKACENL YFTLGINQTL TDLYLTNNAL GDTGVRLLCK
RLSHPGCKLR VLWLFGMDLN KMTHSRLAAL RVTKPYLDIG C


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Bibliography :