NOS3 nitric oxide synthase 3 [Bos taurus (domestic cattle)] - Gene

Summary

Official Symbol: NOS3provided by VGNC
Official Full Name: nitric oxide synthase 3provided by VGNC
Primary source: VGNC:VGNC:32174
See related: BGD:BT18122; Ensembl:ENSBTAG00000017680
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Bos taurus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 4

Exon count:: 27

Annotation release	Status	Assembly	Chr	Location
RS_2023_09	current	ARS-UCD2.0 (GCF_002263795.3)	4	NC_037331.1 (113577075..113595527)

Chromosome 4 - NC_037331.1 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_037331.1 Chromosome 4 Reference ARS-UCD2.0 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Regulation of O-GlcNAcylation on endothelial nitric oxide synthase by glucose deprivation and identification of its O-GlcNAcylation sites.
Title: Regulation of O-GlcNAcylation on endothelial nitric oxide synthase by glucose deprivation and identification of its O-GlcNAcylation sites.
S1179D substitution in eNOS increased the rate of flavin reduction, altered the conformational equilibrium of the reductase domain, and increased the rate of its conformational transitions.
Title: Phosphorylation Controls Endothelial Nitric-oxide Synthase by Regulating Its Conformational Dynamics.
These data define the mechanism responsible for the repressive effects of nitric oxide (NO) on the transcriptional activity of beta-catenin and link eNOS-derived NO to the modulation by VEGF of Wnt/beta-catenin-induced endothelial cell proliferation.
Title: Endothelial NO Synthase-Dependent S-Nitrosylation of β-Catenin Prevents Its Association with TCF4 and Inhibits Proliferation of Endothelial Cells Stimulated by Wnt3a.
Endothelial cell autophagy maintains shear stress-induced nitric oxide generation via glycolysis-dependent ATP/P2Y1 receptor signaling to endothelial nitric oxide synthase.
Title: Endothelial Cell Autophagy Maintains Shear Stress-Induced Nitric Oxide Generation via Glycolysis-Dependent Purinergic Signaling to Endothelial Nitric Oxide Synthase.
TNFalpha reduces eNOS activity in bovine endothelial cells through serine 116 phosphorylation and Pin1 binding.
Title: TNFα reduces eNOS activity in endothelial cells through serine 116 phosphorylation and Pin1 binding: Confirmation of a direct, inhibitory interaction of Pin1 with eNOS.
Pomanox supplementation hinders hyperlipemia-induced coronary endothelial dysfunction by activating the Akt/endothelial nitric oxide-synthase pathway and favorably counteracting vascular inflammation and oxidative damage.
Title: Polyphenol-enriched diet prevents coronary endothelial dysfunction by activating the Akt/eNOS pathway.
Signals that activate and phosphorylate eNOS are transmitted through distinct membrane domains in endothelial cells. Cholesterol domains, but not individual caveolae, mediate HDL stimulation of eNOS. VEGF and shear stress may act through caveolae.
Title: Activation of Endothelial Nitric Oxide (eNOS) Occurs through Different Membrane Domains in Endothelial Cells.
eNOS serine 1179 phosphorylation, in addition to enhancing NO production, also profoundly affects superoxide generation
Title: Serine 1179 Phosphorylation of Endothelial Nitric Oxide Synthase Increases Superoxide Generation and Alters Cofactor Regulation.
In addition to the heme center of eNOS oxygenase domain, we confirmed another O2.- generation site in the eNOS reductase domain and characterized its regulatory properties.
Title: The Characteristics and Regulatory Mechanisms of Superoxide Generation from eNOS Reductase Domain.
A dimer-destabilized mutant of bovine eNOS where cysteine 101 was replaced by alanine, cloned and introduced into an eNOS-deficient mouse strain and that results provide the first in vivo evidence that eNOS-dependent oxidative stress is unlikely to be an initial cause of impaired endothelium-dependent vasodilation and/or a pathologic factor promoting intimal hyperplasia.
Title: Impact of eNOS-Dependent Oxidative Stress on Endothelial Function and Neointima Formation.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Nos3 (e-PCR), detects polymorphism
- UniSTS:499129

MARC_12821-12822:999873106:1 (e-PCR)
- UniSTS:267454

Gene Ontology Provided by RefSeq

Function	Evidence Code	Pubs
enables FMN binding	IEA Inferred from Electronic Annotation more info	PubMed
enables NADP binding	IEA Inferred from Electronic Annotation more info	PubMed
enables calmodulin binding	IEA Inferred from Electronic Annotation more info	PubMed
enables flavin adenine dinucleotide binding	IEA Inferred from Electronic Annotation more info	PubMed
enables heme binding	IEA Inferred from Electronic Annotation more info	PubMed
enables nitric-oxide synthase activity	IEA Inferred from Electronic Annotation more info	PubMed

Process	Evidence Code	Pubs
involved_in nitric oxide biosynthetic process	IEA Inferred from Electronic Annotation more info	PubMed

General protein information

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Preferred Names: nitric oxide synthase 3

Names: EC-NOS; NOS type III; NOSIII; cNOS; constitutive NOS; eNOS; endothelial NOS; endothelial nitric oxide synthase; nitric oxide synthase 3 (endothelial cell); nitric oxide synthase, endothelial

NP_851380.2

EC 1.14.13.39

XP_024846258.1

EC 1.14.13.39

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_181037.3 → NP_851380.2 nitric oxide synthase 3

Status: VALIDATED

Source sequence(s)

AAFC03032796, AAFC03082583, AAFC03082584

UniProtKB/TrEMBL

A0AAA9SAA9, F1MY54

Related

ENSBTAP00000023515.6, ENSBTAT00000023515.6

Conserved Domains (4) summary

COG0369
Location:521 → 1161

CysJ; Sulfite reductase, alpha subunit (flavoprotein) [Inorganic ion transport and metabolism]

cd00795
Location:70 → 482

NOS_oxygenase_euk; Nitric oxide synthase (NOS) eukaryotic oxygenase domain. NOS produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N ...

pfam00258
Location:524 → 700

Flavodoxin_1; Flavodoxin

cl06868
Location:764 → 1166

FNR_like; Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport ...

RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2023_09

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference ARS-UCD2.0 Primary Assembly

Genomic

NC_037331.1 Reference ARS-UCD2.0 Primary Assembly

Range

113577075..113595527

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_024990490.2 → XP_024846258.1 nitric oxide synthase 3 isoform X1

UniProtKB/TrEMBL

A0AAA9SAA9

Conserved Domains (3) summary

pfam00258
Location:316 → 492

Flavodoxin_1; Flavodoxin

cl00254
Location:1 → 274

NOS_oxygenase; Nitric oxide synthase (NOS) produces nitric oxide (NO) by catalyzing a five-electron heme-based oxidation of a guanidine nitrogen of L-arginine to L-citrulline via two successive monooxygenation reactions producing N(omega)-hydroxy-L-arginine (NHA) as an ...

cl06868
Location:556 → 958

FNR_like; Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport ...