ID   NLRX1_HUMAN             Reviewed;         975 AA.
AC   Q86UT6; A8K6Q1; B3KPK2; B3KTA2; Q7RTR3; Q96D51; Q9H724;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   10-JUN-2026, entry version 179.
DE   RecName: Full=NLR family member X1;
DE   AltName: Full=Caterpiller protein 11.3;
DE            Short=CLR11.3;
DE   AltName: Full=Nucleotide-binding oligomerization domain protein 5 {ECO:0000312|EMBL:ABO40480.1};
DE   AltName: Full=Nucleotide-binding oligomerization domain protein 9 {ECO:0000303|PubMed:12766759};
DE   Flags: Precursor;
GN   Name=NLRX1;
GN   Synonyms=NOD5 {ECO:0000312|EMBL:ABO40480.1}, NOD9
GN   {ECO:0000303|PubMed:12766759};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-63 AND GLU-793.
RX   PubMed=12766759; DOI=10.1038/nri1086;
RA   Inohara N., Nunez G.;
RT   "NODs: intracellular proteins involved in inflammation and apoptosis.";
RL   Nat. Rev. Immunol. 3:371-382(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Kronos K.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kubo T., Arai Y., Ohira M., Gamou T., Maeno G., Sakiyama T., Toyoda A.,
RA   Hattori M., Sakaki Y., Nakagawara A., Ohki M.;
RT   "Identification of a 500-kb region of common allelic loss in chromosome
RT   11q23 in non-MYCN amplified type of neuroblastoma.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS SER-63 AND
RP   GLU-793.
RC   TISSUE=Colon, Placenta, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 214-975 (ISOFORM 2), AND VARIANT GLU-793.
RC   TISSUE=Bone, and Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=15952891; DOI=10.1146/annurev.biochem.74.082803.133347;
RA   Inohara N., Chamaillard M., McDonald C., Nunez G.;
RT   "NOD-LRR proteins: role in host-microbial interactions and inflammatory
RT   disease.";
RL   Annu. Rev. Biochem. 74:355-383(2005).
RN   [7]
RP   REVIEW.
RX   PubMed=15771576; DOI=10.1146/annurev.immunol.23.021704.115616;
RA   Ting J.P.-Y., Davis B.K.;
RT   "CATERPILLER: a novel gene family important in immunity, cell death, and
RT   diseases.";
RL   Annu. Rev. Immunol. 23:387-414(2005).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18219313; DOI=10.1038/sj.embor.7401161;
RA   Tattoli I., Carneiro L.A., Jehanno M., Magalhaes J.G., Shu Y.,
RA   Philpott D.J., Arnoult D., Girardin S.E.;
RT   "NLRX1 is a mitochondrial NOD-like receptor that amplifies NF-kappaB and
RT   JNK pathways by inducing reactive oxygen species production.";
RL   EMBO Rep. 9:293-300(2008).
RN   [9]
RP   FUNCTION, INTERACTION WITH MAVS, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18200010; DOI=10.1038/nature06501;
RA   Moore C.B., Bergstralh D.T., Duncan J.A., Lei Y., Morrison T.E.,
RA   Zimmermann A.G., Accavitti-Loper M.A., Madden V.J., Sun L., Ye Z.,
RA   Lich J.D., Heise M.T., Chen Z., Ting J.P.-Y.;
RT   "NLRX1 is a regulator of mitochondrial antiviral immunity.";
RL   Nature 451:573-577(2008).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TUFM.
RX   PubMed=22749352; DOI=10.1016/j.immuni.2012.03.025;
RA   Lei Y., Wen H., Yu Y., Taxman D.J., Zhang L., Widman D.G., Swanson K.V.,
RA   Wen K.W., Damania B., Moore C.B., Giguere P.M., Siderovski D.P.,
RA   Hiscott J., Razani B., Semenkovich C.F., Chen X., Ting J.P.;
RT   "The mitochondrial proteins NLRX1 and TUFM form a complex that regulates
RT   type I interferon and autophagy.";
RL   Immunity 36:933-946(2012).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=27393910; DOI=10.1016/j.molimm.2016.06.013;
RA   Li H., Zhang S., Li F., Qin L.;
RT   "NLRX1 attenuates apoptosis and inflammatory responses in myocardial
RT   ischemia by inhibiting MAVS-dependent NLRP3 inflammasome activation.";
RL   Mol. Immunol. 76:90-97(2016).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 629-975, LRR REPEATS, AND
RP   SUBUNIT.
RX   PubMed=22386589; DOI=10.1016/j.immuni.2011.12.018;
RA   Hong M., Yoon S.I., Wilson I.A.;
RT   "Structure and functional characterization of the RNA-binding element of
RT   the NLRX1 innate immune modulator.";
RL   Immunity 36:337-347(2012).
RN   [13]
RP   INTERACTION WITH INFLUENZA A VIRUS PROTEIN PB1-F2 (MICROBIAL INFECTION).
RX   PubMed=24799673; DOI=10.1073/pnas.1322118111;
RA   Jaworska J., Coulombe F., Downey J., Tzelepis F., Shalaby K., Tattoli I.,
RA   Berube J., Rousseau S., Martin J.G., Girardin S.E., McCullers J.A.,
RA   Divangahi M.;
RT   "NLRX1 prevents mitochondrial induced apoptosis and enhances macrophage
RT   antiviral immunity by interacting with influenza virus PB1-F2 protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:E2110-E2119(2014).
CC   -!- FUNCTION: Participates in antiviral signaling. Acts as a negative
CC       regulator of MAVS-mediated antiviral responses, through the inhibition
CC       of the virus-induced RLH (RIG-like helicase)-MAVS interaction
CC       (PubMed:18200010). Instead, promotes autophagy by interacting with TUFM
CC       and subsequently recruiting the autophagy-related proteins ATG5 and
CC       ATG12 (PubMed:22749352). Also regulates MAVS-dependent NLRP3
CC       inflammasome activation to attenuate apoptosis (PubMed:27393910). Has
CC       no inhibitory function on NF-kappa-B signaling pathway, but enhances
CC       NF-kappa-B and JUN N-terminal kinase dependent signaling through the
CC       production of reactive oxygen species (PubMed:18219313). Regulates
CC       viral mediated-inflammation and energy metabolism in a sex-dependent
CC       manner (By similarity). In females, prevents uncontrolled inflammation
CC       and energy metabolism and thus, may contribute to the sex differences
CC       observed in infectious and inflammatory diseases (By similarity).
CC       {ECO:0000250|UniProtKB:Q3TL44, ECO:0000269|PubMed:18200010,
CC       ECO:0000269|PubMed:18219313, ECO:0000269|PubMed:22749352,
CC       ECO:0000269|PubMed:27393910}.
CC   -!- SUBUNIT: Homohexamer (PubMed:22386589). Interacts with MAVS
CC       (PubMed:18200010). Interacts with TUFM (PubMed:22749352).
CC       {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:22386589,
CC       ECO:0000269|PubMed:22749352}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus protein
CC       PB1-F2. {ECO:0000269|PubMed:24799673}.
CC   -!- INTERACTION:
CC       Q86UT6; P49411: TUFM; NbExp=2; IntAct=EBI-3893071, EBI-359097;
CC       Q86UT6; Q6PDS3: Sarm1; Xeno; NbExp=2; IntAct=EBI-3893071, EBI-6117196;
CC       Q86UT6-1; Q7Z434-1: MAVS; NbExp=3; IntAct=EBI-15680006, EBI-15577799;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:18200010, ECO:0000269|PubMed:18219313,
CC       ECO:0000269|PubMed:27393910}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86UT6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86UT6-2; Sequence=VSP_027158, VSP_027159;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Strongest expression in
CC       mammary gland, heart and muscle. Detected in HeLa, HEK293T, THP-1, HL-
CC       60, Raji and Jurkat cell lines (at protein level).
CC       {ECO:0000269|PubMed:15952891, ECO:0000269|PubMed:18200010,
CC       ECO:0000269|PubMed:18219313}.
CC   -!- DOMAIN: The LRRCT domain mediates homodimerization and LRRNT mediates
CC       trimerization of the dimers. {ECO:0000269|PubMed:22386589}.
CC   -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15075.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAG51714.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAG51714.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY245437; AAP31240.1; -; mRNA.
DR   EMBL; BK001111; DAA01244.1; -; mRNA.
DR   EMBL; EF452237; ABO40480.1; -; mRNA.
DR   EMBL; AB094095; BAC76049.1; -; mRNA.
DR   EMBL; AK025131; BAB15075.1; ALT_INIT; mRNA.
DR   EMBL; AK056454; BAG51714.1; ALT_SEQ; mRNA.
DR   EMBL; AK095247; BAG53014.1; -; mRNA.
DR   EMBL; AK291716; BAF84405.1; -; mRNA.
DR   EMBL; BC013199; AAH13199.3; -; mRNA.
DR   EMBL; BC110890; AAI10891.1; -; mRNA.
DR   CCDS; CCDS44752.1; -. [Q86UT6-2]
DR   CCDS; CCDS8416.1; -. [Q86UT6-1]
DR   RefSeq; NP_001269072.1; NM_001282143.2. [Q86UT6-1]
DR   RefSeq; NP_001269073.1; NM_001282144.2. [Q86UT6-1]
DR   RefSeq; NP_001269287.1; NM_001282358.2. [Q86UT6-1]
DR   RefSeq; NP_078894.2; NM_024618.3. [Q86UT6-1]
DR   RefSeq; NP_733840.1; NM_170722.2. [Q86UT6-2]
DR   RefSeq; XP_005271726.1; XM_005271669.2. [Q86UT6-1]
DR   RefSeq; XP_006718967.1; XM_006718904.2. [Q86UT6-2]
DR   RefSeq; XP_011541282.1; XM_011542980.2. [Q86UT6-1]
DR   RefSeq; XP_047283542.1; XM_047427586.1. [Q86UT6-2]
DR   RefSeq; XP_047283543.1; XM_047427587.1. [Q86UT6-2]
DR   RefSeq; XP_054225919.1; XM_054369944.1. [Q86UT6-1]
DR   RefSeq; XP_054225920.1; XM_054369945.1. [Q86UT6-1]
DR   RefSeq; XP_054225921.1; XM_054369946.1. [Q86UT6-2]
DR   RefSeq; XP_054225922.1; XM_054369947.1. [Q86UT6-2]
DR   RefSeq; XP_054225923.1; XM_054369948.1. [Q86UT6-2]
DR   PDB; 3UN9; X-ray; 2.65 A; A/B/C=629-975.
DR   PDBsum; 3UN9; -.
DR   AlphaFoldDB; Q86UT6; -.
DR   SMR; Q86UT6; -.
DR   BioGRID; 122796; 103.
DR   DIP; DIP-60637N; -.
DR   FunCoup; Q86UT6; 1019.
DR   IntAct; Q86UT6; 72.
DR   NDEx; IQUERY-CP-NLRX1; 6 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000387334; -.
DR   DrugBank; DB21563; Amelenodor.
DR   GuidetoPHARMACOLOGY; 1766; -.
DR   GlyGen; Q86UT6; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q86UT6; -.
DR   PhosphoSitePlus; Q86UT6; -.
DR   SwissPalm; Q86UT6; -.
DR   BioMuta; NLRX1; -.
DR   DMDM; 74759406; -.
DR   jPOST; Q86UT6; -.
DR   MassIVE; Q86UT6; -.
DR   PaxDb; 9606-ENSP00000387334; -.
DR   PeptideAtlas; Q86UT6; -.
DR   ProteomicsDB; 69887; -. [Q86UT6-1]
DR   ProteomicsDB; 69888; -. [Q86UT6-2]
DR   Pumba; Q86UT6; -.
DR   Antibodypedia; 45879; 230 antibodies from 35 providers.
DR   DNASU; 79671; -.
DR   Ensembl; ENST00000292199.6; ENSP00000292199.2; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000409109.6; ENSP00000387334.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000409991.5; ENSP00000386851.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000525863.1; ENSP00000433442.1; ENSG00000160703.18. [Q86UT6-2]
DR   Ensembl; ENST00000706729.1; ENSP00000516519.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000886077.1; ENSP00000556136.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000886078.1; ENSP00000556137.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000886079.1; ENSP00000556138.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000886080.1; ENSP00000556139.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000920615.1; ENSP00000590674.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000964948.1; ENSP00000635007.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000964949.1; ENSP00000635008.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000964950.1; ENSP00000635009.1; ENSG00000160703.18. [Q86UT6-1]
DR   Ensembl; ENST00000964951.1; ENSP00000635010.1; ENSG00000160703.18. [Q86UT6-1]
DR   GeneID; 79671; -.
DR   KEGG; hsa:79671; -.
DR   MANE-Select; ENST00000409109.6; ENSP00000387334.1; NM_001282144.2; NP_001269073.1.
DR   UCSC; uc001pvu.5; human. [Q86UT6-1]
DR   AGR; HGNC:29890; -.
DR   ClinPGx; PA162398052; -.
DR   CTD; 79671; -.
DR   DisGeNET; 79671; -.
DR   GeneCards; NLRX1; -.
DR   HGNC; HGNC:29890; NLRX1.
DR   HPA; ENSG00000160703; Tissue enhanced (esophagus).
DR   MalaCards; NLRX1; -.
DR   MIM; 611947; gene.
DR   OpenTargets; ENSG00000160703; -.
DR   VEuPathDB; HostDB:ENSG00000160703; -.
DR   eggNOG; KOG4308; Eukaryota.
DR   GeneTree; ENSGT00940000159493; -.
DR   HOGENOM; CLU_016769_0_0_1; -.
DR   InParanoid; Q86UT6; -.
DR   OMA; CVEPGHR; -.
DR   OrthoDB; 120976at2759; -.
DR   PAN-GO; Q86UT6; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q86UT6; -.
DR   PathwayCommons; Q86UT6; -.
DR   Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR   Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR   Reactome; R-HSA-9758274; Regulation of NF-kappa B signaling.
DR   SignaLink; Q86UT6; -.
DR   SIGNOR; Q86UT6; -.
DR   Agora; ENSG00000160703; -.
DR   BioGRID-ORCS; 79671; 12 hits in 1157 CRISPR screens.
DR   ChiTaRS; NLRX1; human.
DR   EvolutionaryTrace; Q86UT6; -.
DR   GeneWiki; NLRX1; -.
DR   GenomeRNAi; 79671; -.
DR   Pharos; Q86UT6; Tbio.
DR   PRO; PR:Q86UT6; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q86UT6; protein.
DR   Bgee; ENSG00000160703; Expressed in lower esophagus mucosa and 188 other cell types or tissues.
DR   ExpressionAtlas; Q86UT6; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IBA:GO_Central.
DR   GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IBA:GO_Central.
DR   FunFam; 3.40.50.300:FF:001029; NLR family member X1; 1.
DR   FunFam; 3.80.10.10:FF:000149; NLR family member X1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR007111; NACHT_NTPase.
DR   InterPro; IPR051261; NLR.
DR   InterPro; IPR048900; NLRX1_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24106; NACHT, LRR AND CARD DOMAINS-CONTAINING; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF05729; NACHT; 1.
DR   Pfam; PF21402; NLRX1_C; 1.
DR   SMART; SM00368; LRR_RI; 7.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS50837; NACHT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Host-virus interaction;
KW   Immunity; Innate immunity; Leucine-rich repeat; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding;
KW   Proteomics identification; Reference proteome; Repeat; Transit peptide.
FT   TRANSIT         1..86
FT                   /note="Mitochondrion"
FT   CHAIN           87..975
FT                   /note="NLR family member X1"
FT                   /id="PRO_0000296190"
FT   DOMAIN          160..483
FT                   /note="NACHT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT   DOMAIN          667..694
FT                   /note="LRRNT"
FT                   /evidence="ECO:0000305|PubMed:22386589"
FT   REPEAT          695..718
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   REPEAT          724..747
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   REPEAT          749..777
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   REPEAT          778..801
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   REPEAT          811..834
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   REPEAT          835..857
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   REPEAT          858..877
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   REPEAT          878..899
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000269|PubMed:22386589"
FT   DOMAIN          906..970
FT                   /note="LRRCT"
FT                   /evidence="ECO:0000305|PubMed:22386589"
FT   REGION          75..556
FT                   /note="Required for interaction with MAVS"
FT                   /evidence="ECO:0000269|PubMed:18200010"
FT   REGION          556..974
FT                   /note="Required for the repression of MAVS-induced
FT                   interferon signaling"
FT                   /evidence="ECO:0000269|PubMed:18200010"
FT   BINDING         166..173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT   VAR_SEQ         869..921
FT                   /note="HLYFNELSSEGRQVLRDLGGAAEGGARVVVSLTEGTAVSEYWSVILSEVQRN
FT                   L -> QGVAIQMCWKLPLLPYAHLWTPRMPSHWCFLLILMPPLPQWYDGLVAPRGRCT
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027158"
FT   VAR_SEQ         922..975
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027159"
FT   VARIANT         63
FT                   /note="P -> S (in dbSNP:rs643423)"
FT                   /evidence="ECO:0000269|PubMed:12766759,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_034614"
FT   VARIANT         125
FT                   /note="R -> L (in dbSNP:rs3809045)"
FT                   /id="VAR_034615"
FT   VARIANT         793
FT                   /note="A -> E (in dbSNP:rs4245191)"
FT                   /evidence="ECO:0000269|PubMed:12766759,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_034616"
FT   VARIANT         843
FT                   /note="A -> S (in dbSNP:rs35500631)"
FT                   /id="VAR_034617"
FT   CONFLICT        325
FT                   /note="R -> C (in Ref. 4; BAG53014)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        575
FT                   /note="A -> T (in Ref. 4; BAG51714)"
FT                   /evidence="ECO:0000305"
FT   HELIX           672..686
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           688..695
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          700..702
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           710..720
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          727..731
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           739..744
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           746..750
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          752..756
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           764..775
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          783..785
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           792..804
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          811..813
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           820..830
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           831..833
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          839..841
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           849..861
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          867..869
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           877..885
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   STRAND          895..897
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           907..920
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           926..945
FT                   /evidence="ECO:0007829|PDB:3UN9"
FT   HELIX           950..969
FT                   /evidence="ECO:0007829|PDB:3UN9"
SQ   SEQUENCE   975 AA;  107616 MW;  25B6624FC13217FF CRC64;
     MRWGHHLPRA SWGSGFRRAL QRPDDRIPFL IHWSWPLQGE RPFGPPRAFI RHHGSSVDSA
     PPPGRHGRLF PSASATEAIQ RHRRNLAEWF SRLPREERQF GPTFALDTVH VDPVIRESTP
     DELLRPPAEL ALEHQPPQAG LPPLALSQLF NPDACGRRVQ TVVLYGTVGT GKSTLVRKMV
     LDWCYGRLPA FELLIPFSCE DLSSLGPAPA SLCQLVAQRY TPLKEVLPLM AAAGSHLLFV
     LHGLEHLNLD FRLAGTGLCS DPEEPQEPAA IIVNLLRKYM LPQASILVTT RPSAIGRIPS
     KYVGRYGEIC GFSDTNLQKL YFQLRLNQPY CGYAVGGSGV SATPAQRDHL VQMLSRNLEG
     HHQIAAACFL PSYCWLVCAT LHFLHAPTPA GQTLTSIYTS FLRLNFSGET LDSTDPSNLS
     LMAYAARTMG KLAYEGVSSR KTYFSEEDVC GCLEAGIRTE EEFQLLHIFR RDALRFFLAP
     CVEPGRAGTF VFTVPAMQEY LAALYIVLGL RKTTLQKVGK EVAELVGRVG EDVSLVLGIM
     AKLLPLRALP LLFNLIKVVP RVFGRMVGKS REAVAQAMVL EMFREEDYYN DDVLDQMGAS
     ILGVEGPRRH PDEPPEDEVF ELFPMFMGGL LSAHNRAVLA QLGCPIKNLD ALENAQAIKK
     KLGKLGRQVL PPSELLDHLF FHYEFQNQRF SAEVLSSLRQ LNLAGVRMTP VKCTVVAAVL
     GSGRHALDEV NLASCQLDPA GLRTLLPVFL RARKLGLQLN SLGPEACKDL RDLLLHDQCQ
     ITTLRLSNNP LTAAGVAVLM EGLAGNTSVT HLSLLHTGLG DEGLELLAAQ LDRNRQLQEL
     NVAYNGAGDT AALALARAAR EHPSLELLHL YFNELSSEGR QVLRDLGGAA EGGARVVVSL
     TEGTAVSEYW SVILSEVQRN LNSWDRARVQ RHLELLLRDL EDSRGATLNP WRKAQLLRVE
     GEVRALLEQL GSSGS
//