NLRX1_RAT
ID NLRX1_RAT Reviewed; 973 AA.
AC Q5FVQ8;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=NLR family member X1;
DE Flags: Precursor;
GN Name=Nlrx1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
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; BC089834; AAH89834.1; -; mRNA.
DR RefSeq; NP_001020181.1; NM_001025010.1.
DR AlphaFoldDB; Q5FVQ8; -.
DR SMR; Q5FVQ8; -.
DR STRING; 10116.ENSRNOP00000011620; -.
DR iPTMnet; Q5FVQ8; -.
DR PhosphoSitePlus; Q5FVQ8; -.
DR jPOST; Q5FVQ8; -.
DR PaxDb; Q5FVQ8; -.
DR PRIDE; Q5FVQ8; -.
DR Ensembl; ENSRNOT00000077958; ENSRNOP00000071934; ENSRNOG00000052386.
DR GeneID; 315599; -.
DR KEGG; rno:315599; -.
DR UCSC; RGD:1311293; rat.
DR CTD; 79671; -.
DR RGD; 1311293; Nlrx1.
DR eggNOG; KOG4308; Eukaryota.
DR GeneTree; ENSGT00940000159493; -.
DR InParanoid; Q5FVQ8; -.
DR OrthoDB; 114368at2759; -.
DR Reactome; R-RNO-936440; Negative regulators of DDX58/IFIH1 signaling.
DR PRO; PR:Q5FVQ8; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; ISO:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:RGD.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; ISO:RGD.
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 2: Evidence at transcript 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..84
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 85..973
FT /note="NLR family member X1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000296192"
FT DOMAIN 158..481
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT DOMAIN 665..692
FT /note="LRRNT"
FT REPEAT 693..716
FT /note="LRR 1"
FT REPEAT 722..745
FT /note="LRR 2"
FT REPEAT 747..775
FT /note="LRR 3"
FT REPEAT 776..799
FT /note="LRR 4"
FT REPEAT 809..832
FT /note="LRR 5"
FT REPEAT 833..855
FT /note="LRR 6"
FT REPEAT 856..875
FT /note="LRR 7"
FT REPEAT 876..897
FT /note="LRR 8"
FT DOMAIN 904..968
FT /note="LRRCT"
FT REGION 73..554
FT /note="Required for interaction with MAVS"
FT /evidence="ECO:0000250"
FT REGION 554..972
FT /note="Required for the repression of MAVS-induced
FT interferon signaling"
FT /evidence="ECO:0000250"
FT BINDING 164..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
SQ SEQUENCE 973 AA; 107590 MW; 73B87B5A1B70DE9F CRC64;
MRWGCHLPRT SWGSGLGRTV PLPDELRIQS SWPFKGVHHP LRPPRAFIRH HGNSADSAPP
PGRHGQLFRS ISATEAIQRH RRNLTEWFSR LPREERQFGP TFALDTVHVD PVIRESTPDD
LLRPSTELAT GHQRTQAELP PLALSQLFDP DACGRRVQTV VLYGTVGTGK STLVRKMVLD
WCYGRLPAFE LLIPFSCEDL SSLGSTPASL CQLVTQRYTP LKEVLPLMNA AGSRLLFVLH
GLERLNLDFR LAGTGLCSDP EEPGAPAAIM VNLLRKYMLP EASILVTTRP SAIGRIPSKY
VGRYGEICGF SDTNLQKLYF QLRLNQPDCG YGAGGTGVSV TPAQRDNLIQ MLSRNLEGHH
QIAAACFLPS YCWLVCATLH FLHAPTSAGQ TLTSIYTSFL RLNFNGETLD STDPSNLSLM
SYAARTMGKL AYEGVSSRKT YFSEEDVRGC LEAGIKTEEE FQLLQIFRRD ALRFFLAPCV
EPGHLGTFVF TVPAMQEYLA ALYIVLGLRK TALQRVGKEV FEFVGRVGED VSLVLGIVAK
LLPLRILPLL FNLLKVVPRV FGRMVSKSRE AVAQAMVLEM FREEDYYNDD VLDQMGASIL
GVEGPRRHPD EPPEDEVFEL FPMFMSGLLS AHNRAVLAQL GCPIKNLDAL ENAQAIKKKL
GKMGRQVLPP SELLDHLFFH YEFQNQRFSA EVLGSLRQLN LAGVRMTPLK CTVVASVLGS
GRHPLDEVNL ASCQLDPAGL HTLMPVLLRA RKLGLQLNNL GPEACRDLRD LLLHDQCQIT
TLRLSNNPLT AAGVGVLMDG LAGNTSVTHL SLLHTDLGDE GLELLAAQLD RNKQLQELNV
AYNGAGDTVA LALAKAARKH PSLELLHLYF NELSSEGRQV LRDLGGSGEG GARVVASLTE
GTAVSEYWSV ILSEVQRNLN SWDPVRVQRH LKLLLRDLED SRGATLNPWR KAQLLRVESE
VKTLLEQLGG SGH
