NLRX1_MOUSE
ID NLRX1_MOUSE Reviewed; 975 AA.
AC Q3TL44; Q3UKJ1; Q80W30; Q8C249;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=NLR family member X1;
DE Flags: Precursor;
GN Name=Nlrx1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Participates in antiviral signaling. {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Interacts with MAVS (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}.
CC -!- DOMAIN: The LRRCT domain mediates homodimerization and LRRNT mediates
CC trimerization of the dimers. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NLRP family. {ECO:0000305}.
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DR EMBL; AK089260; BAC40818.1; -; mRNA.
DR EMBL; AK145988; BAE26810.1; -; mRNA.
DR EMBL; AK166689; BAE38948.1; -; mRNA.
DR EMBL; BC050054; AAH50054.1; -; mRNA.
DR CCDS; CCDS23100.1; -.
DR RefSeq; NP_001157214.1; NM_001163742.1.
DR RefSeq; NP_001157215.1; NM_001163743.1.
DR RefSeq; NP_848507.2; NM_178420.3.
DR AlphaFoldDB; Q3TL44; -.
DR SMR; Q3TL44; -.
DR BioGRID; 234769; 5.
DR IntAct; Q3TL44; 1.
DR STRING; 10090.ENSMUSP00000126555; -.
DR iPTMnet; Q3TL44; -.
DR PhosphoSitePlus; Q3TL44; -.
DR SwissPalm; Q3TL44; -.
DR EPD; Q3TL44; -.
DR MaxQB; Q3TL44; -.
DR PaxDb; Q3TL44; -.
DR PeptideAtlas; Q3TL44; -.
DR PRIDE; Q3TL44; -.
DR ProteomicsDB; 252911; -.
DR Antibodypedia; 45879; 239 antibodies from 36 providers.
DR Ensembl; ENSMUST00000034621; ENSMUSP00000034621; ENSMUSG00000032109.
DR Ensembl; ENSMUST00000168499; ENSMUSP00000127531; ENSMUSG00000032109.
DR Ensembl; ENSMUST00000169651; ENSMUSP00000126555; ENSMUSG00000032109.
DR GeneID; 270151; -.
DR KEGG; mmu:270151; -.
DR UCSC; uc009pci.2; mouse.
DR CTD; 79671; -.
DR MGI; MGI:2429611; Nlrx1.
DR VEuPathDB; HostDB:ENSMUSG00000032109; -.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000159493; -.
DR HOGENOM; CLU_016769_0_0_1; -.
DR InParanoid; Q3TL44; -.
DR OMA; NQPDCGC; -.
DR OrthoDB; 114368at2759; -.
DR PhylomeDB; Q3TL44; -.
DR TreeFam; TF331068; -.
DR Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
DR BioGRID-ORCS; 270151; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Nlrx1; mouse.
DR PRO; PR:Q3TL44; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q3TL44; protein.
DR Bgee; ENSMUSG00000032109; Expressed in granulocyte and 188 other tissues.
DR ExpressionAtlas; Q3TL44; baseline and differential.
DR Genevisible; Q3TL44; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:MGI.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:MGI.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IMP:MGI.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IMP:MGI.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF05729; NACHT; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Host-virus interaction; Immunity; Innate immunity;
KW Leucine-rich repeat; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..86
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 87..975
FT /note="NLR family member X1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000296191"
FT DOMAIN 160..483
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT DOMAIN 667..694
FT /note="LRRNT"
FT REPEAT 695..718
FT /note="LRR 1"
FT REPEAT 724..747
FT /note="LRR 2"
FT REPEAT 749..777
FT /note="LRR 3"
FT REPEAT 778..801
FT /note="LRR 4"
FT REPEAT 811..834
FT /note="LRR 5"
FT REPEAT 835..857
FT /note="LRR 6"
FT REPEAT 858..877
FT /note="LRR 7"
FT REPEAT 878..899
FT /note="LRR 8"
FT DOMAIN 906..970
FT /note="LRRCT"
FT REGION 75..556
FT /note="Required for interaction with MAVS"
FT /evidence="ECO:0000250"
FT REGION 556..974
FT /note="Required for the repression of MAVS-induced
FT interferon signaling"
FT /evidence="ECO:0000250"
FT BINDING 166..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT CONFLICT 438
FT /note="S -> P (in Ref. 2; AAH50054)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="I -> S (in Ref. 2; AAH50054)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="D -> V (in Ref. 1; BAE26810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 975 AA; 107831 MW; B677729514B1A34F CRC64;
MRWGCHLPRT SWGSGLGRTP QLPDEHISFL IQWSWPFKGV HPLRPPRAFI RYHGNSADSA
PPPGRHGQLF RSISATEAIQ RHRRNLTEWF SRLPREERQF GPTFALDTVH VDPVIRESTP
DELLRPSTEL ATGHQQTQAG LPPLALSQLF DPDSCGRRVQ TVVLYGTVGT GKSTLVRKMV
LDWCYGRLPA FELLIPFSCE DLSSLGSTPA SLCQLVTQRY TPLKEVLPLM TAAGSRLLFV
LHGLERLNLD FRLAGTGLCS DPEEPGPPAA IIVNLLRKYM LPEASILVTT RPSTISRIPS
KYVGRYGEIC GFSDTNLQKL YFQLRLNQPD CGYGAGGASV SVTPAQRDNL IQMLSRNLEG
HHQIAAACFL PSYCWLVCAT LHFLHAPTPA GQTLTSIYTS FLRLNFSGET LDSTHTSNLS
LMSYAARTMG KLAYEGVSSR KTYFSEEDVR GCLEAGIKTE EEFQLLQIFR RDALRFFLAP
CVEPGHLGTF VFTVPAMQEY LAALYIVLGL RKTALQRVGK EVVEFVGRVG EDVSLVLGIV
AKLLPLRILP LLFNLLKVVP RVFGRMVSKS REAVAQAMVL EMFREEDYYN DDVLDQMGAS
ILGVEGPRRH PDEPSEDEVF ELFPMFMGGL LSAHNRAVLA QLGCPIKNLD ALENAQAIKK
KLGKLGRQVL PPSELLDHLF FHYEFQNQRF SAEVLGSLRQ LNLAGVRMTP LKCTVVASVL
GSGRHPLDEV NLASCQLDPA GLHTLMPVLL RARKLGLQLN NLGPEACRDL RDLLLHDQCQ
ITTLRLSNNP LTAAGVGLLM DGLAGNTSVT HLSLLHTDLG DEGLELLAAQ LDRNKQLQEL
NVAYNGAGDT VALALAKAAR EHPSLELLHL YFNELSSEGR QVLRDLGGSG EGGARVVASL
TEGTAVSEYW SVILSEVQRN VHSWDPLRVQ RHLKLLLRDL EDSRGATLNP WRKAQLLRVE
GEVKTLLEQL GGSGH
