Nod1 nucleotide-binding oligomerization domain containing 1 [Rattus norvegicus (Norway rat)] - Gene

Summary

Official Symbol: Nod1provided by RGD
Official Full Name: nucleotide-binding oligomerization domain containing 1provided by RGD
Primary source: RGD:1562269
See related: EnsemblRapid:ENSRNOG00000010629 AllianceGenome:RGD:1562269
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Rattus norvegicus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
Also known as: RGD1562269
Summary: Predicted to enable several functions, including CARD domain binding activity; peptidoglycan binding activity; and protein homodimerization activity. Involved in positive regulation of apoptotic process; positive regulation of cytokine production; and positive regulation of nitric-oxide synthase activity. Predicted to be located in basolateral plasma membrane; cytosol; and phagocytic vesicle. Predicted to be part of canonical inflammasome complex. Predicted to be active in plasma membrane. Human ortholog(s) of this gene implicated in asthma. Orthologous to human NOD1 (nucleotide binding oligomerization domain containing 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Biased expression in Lung (RPKM 116.8), Spleen (RPKM 113.4) and 9 other tissues See more
Orthologs: human mouse all
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Genomic context

Location:: 4q24

Exon count:: 12

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCr8 (GCF_036323735.1)	4	NC_086022.1 (85391142..85442281, complement)
RS_2023_06	previous assembly	mRatBN7.2 (GCF_015227675.2)	4	NC_051339.1 (84060871..84111668, complement)
106	previous assembly	Rnor_6.0 (GCF_000001895.5)	4	NC_005103.4 (85123965..85175206, complement)

Chromosome 4 - NC_086022.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
BioProject: PRJNA238328
Publication: PMID 24510058
Analysis date: Mon Jun 6 17:44:12 2016

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

MiR-702-3p inhibits the inflammatory injury in septic H9c2 cells by regulating NOD1.
Title: MiR-702-3p inhibits the inflammatory injury in septic H9c2 cells by regulating NOD1.
Nucleotide-binding oligomerization domain protein 1 enhances oxygen-glucose deprivation and reperfusion injury in cortical neurons via activation of endoplasmic reticulum stress-mediated autophagy.
Title: Nucleotide-binding oligomerization domain protein 1 enhances oxygen-glucose deprivation and reperfusion injury in cortical neurons via activation of endoplasmic reticulum stress-mediated autophagy.
Data show that mRNA expression and protein levels of nucleotide-binding oligomerization domain-containing proteins (NOD1, NOD2) and NLR family, pyrin domain containing 3 protein (NLRP3) were significantly increased in the severe acute pancreatitis (SAP) models.
Title: Involvement of Nucleotide-Binding and Oligomerization Domain-Like Receptors in the Intestinal Injury of Severe Acute Pancreatitis in Rats.
combined results support the hypothesis that high glucose and LPS can activate the NOD1-RICK-NF-kappaB inflammatory signaling pathway via the NOD1 receptor, and may participate in the development of diabetic nephropathy.
Title: High Glucose and Lipopolysaccharide Activate NOD1- RICK-NF-κB Inflammatory Signaling in Mesangial Cells.
These findings indicated that NOD1 expressed in odontoblasts functions to upregulate the chemokines expression via p38-AP-1 signaling pathway and suggested that NOD1 may play important roles in the initiation and progression of pulpitis.
Title: Functional Roles of NOD1 in Odontoblasts on Dental Pulp Innate Immunity.
in rat peritoneal mast cells the ingested cargo can, through interruptions of the phagosome membrane, interact directly with NOD1 and NOD2 proteins, which act as switches in the process of cytokine production.
Title: NOD1 and NOD2 Interact with the Phagosome Cargo in Mast Cells: A Detailed Morphological Evidence.
A key role for the endothelium in NOD1 mediated vascular inflammation: comparison to TLR4 responses.
Title: A key role for the endothelium in NOD1 mediated vascular inflammation: comparison to TLR4 responses.
Experiments performed with the synthetic Nod1 ligand L-Ala-D-gamma-Glu-meso-diaminopimelic acid confirmed that IKKalpha is involved in NF-kappaB activation triggered downstream of Nod1-mediated peptidoglycan recognition
Title: IKKα contributes to canonical NF-κB activation downstream of Nod1-mediated peptidoglycan recognition.
Vascular smooth muscle cells express NOD1 receptors and respond to agonists by expressing increased NOS2.
Title: Nucleotide oligomerization domain 1 is a dominant pathway for NOS2 induction in vascular smooth muscle cells: comparison with Toll-like receptor 4 responses in macrophages.

Submit: New GeneRIF Correction

General gene information

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Gene Ontology Provided by RGD

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables CARD domain binding	ISO Inferred from Sequence Orthology more info
enables hydrolase activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables pattern recognition receptor activity	ISO Inferred from Sequence Orthology more info
enables peptidoglycan binding	ISO Inferred from Sequence Orthology more info
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables scaffold protein binding	IEA Inferred from Electronic Annotation more info
enables ubiquitin binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
acts_upstream_of ERK1 and ERK2 cascade	ISO Inferred from Sequence Orthology more info
acts_upstream_of JNK cascade	ISO Inferred from Sequence Orthology more info
involved_in cellular response to muramyl dipeptide	ISO Inferred from Sequence Orthology more info
involved_in defense response to Gram-negative bacterium	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within defense response to Gram-positive bacterium	ISO Inferred from Sequence Orthology more info
involved_in defense response to bacterium	ISO Inferred from Sequence Orthology more info
involved_in detection of bacterium	ISO Inferred from Sequence Orthology more info
involved_in inflammatory response	IEA Inferred from Electronic Annotation more info
involved_in innate immune response	IEA Inferred from Electronic Annotation more info
involved_in intracellular signal transduction	IBA Inferred from Biological aspect of Ancestor more info
involved_in intracellular signal transduction	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of cellular defense response	IEA Inferred from Electronic Annotation more info
involved_in nucleotide-binding oligomerization domain containing 1 signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in pattern recognition receptor signaling pathway	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of ERK1 and ERK2 cascade	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of JNK cascade	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of NF-kappaB transcription factor activity	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of autophagy	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of canonical NF-kappaB signal transduction	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of canonical NF-kappaB signal transduction	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of cysteine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of dendritic cell antigen processing and presentation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interleukin-1 beta production	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within positive regulation of interleukin-6 production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interleukin-8 production	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of macrophage cytokine production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of nitric-oxide synthase activity	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of non-canonical NF-kappaB signal transduction	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of pyroptotic inflammatory response	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within positive regulation of stress-activated MAPK cascade	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of tumor necrosis factor production	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within positive regulation of tumor necrosis factor production	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of xenophagy	ISO Inferred from Sequence Orthology more info
involved_in response to endoplasmic reticulum stress	ISO Inferred from Sequence Orthology more info
acts_upstream_of stress-activated MAPK cascade	ISO Inferred from Sequence Orthology more info
acts_upstream_of xenophagy	ISO Inferred from Sequence Orthology more info

Component	Evidence Code	Pubs
located_in basolateral plasma membrane	ISO Inferred from Sequence Orthology more info
part_of canonical inflammasome complex	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in neuronal cell body	IEA Inferred from Electronic Annotation more info
located_in phagocytic vesicle	ISO Inferred from Sequence Orthology more info
is_active_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: nucleotide-binding oligomerization domain-containing protein 1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001109236.1 → NP_001102706.1 nucleotide-binding oligomerization domain-containing protein 1

See identical proteins and their annotated locations for NP_001102706.1

Status: PROVISIONAL

Source sequence(s)

CH474011

UniProtKB/TrEMBL

A6K0W2, D4ADT7

Related

ENSRNOP00000014324.4, ENSRNOT00000014324.8

Conserved Domains (4) summary

cd00116
Location:728 → 941

LRR_RI; Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond ...

sd00033
Location:730 → 757

LRR_RI; leucine-rich repeat [structural motif]

pfam05729
Location:197 → 367

NACHT; NACHT domain

cl14633
Location:21 → 104

DD; Death Domain Superfamily of protein-protein interaction domains