NLRX1

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

NLRX1 or NLR family member X1, short for nucleotide-binding oligomerization domain, leucine rich repeat containing X1 is a protein that in humans is encoded by the NLRX1 gene.[5][6] It is also known as NOD-like receptor X1, NLR family, X1, NOD5, NOD9, and CLR11.3, and is a member of the NOD-like receptor family of pattern recognition receptors.

PDBOrtholog search: PDBe RCSB
AliasesNLRX1, CLR11.3, DLNB26, NOD26, NOD5, NOD9, NLR family member X1
Quick facts Available structures, PDB ...
NLRX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesNLRX1, CLR11.3, DLNB26, NOD26, NOD5, NOD9, NLR family member X1
External IDsOMIM: 611947; MGI: 2429611; HomoloGene: 11623; GeneCards: NLRX1; OMA:NLRX1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001282143
NM_001282144
NM_001282358
NM_024618
NM_170722

NM_001163742
NM_001163743
NM_178420

RefSeq (protein)

NP_001269072
NP_001269073
NP_001269287
NP_078894

NP_001157214
NP_001157215
NP_848507

Location (UCSC)Chr 11: 119.17 – 119.18 MbChr 9: 44.16 – 44.18 Mb
PubMed search[3][4]
Wikidata
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Function

NLRX1 is an intracellular protein that plays a role in the immune system. NLRX1 has been proposed to affect innate immunity to viruses by interfering with the mitochondrial antiviral signaling protein (MAVS)/retinoic-acid-inducible gene I (RIG-I) mitochondrial antiviral pathway.,[7] although this was recently questioned.[8][9]

NLRX1 also plays a role in host immunity during bacterial infections, such as Chlamydia trachomatis and Helicobacter pylori, by regulating bacterial burden and inflammation in mononuclear phagocytes. Mechanisms underlying the modulation of NLRX1 are not well characterized, however computational modeling predictions suggest that levels of NLRX1 may be controlled by negative feedback circuits induced early after infection.[10][11][12]

Structure

NLRX1 has a unique protein structure composed of 3 protein domains: an N-terminal effector domain containing a mitochondrion localization signal; a central NACHT domain; a C-terminal leucine-rich repeat (LRR) domain.[13]

References

Further reading

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