NOS1

NOS1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4D1N, 4UCH, 4UH5, 4UH6, 4V3U, 5ADF, 5ADG, 5ADI, 5FVX, 5FVW, 5FVU, 5FVV
Identifiers
Aliases	NOS1, IHPS1, N-NOS, NC-NOS, NOS, bNOS, nNOS, nitric oxide synthase 1
External IDs	OMIM: 163731; MGI: 97360; HomoloGene: 37327; GeneCards: NOS1; OMA:NOS1 - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	117,452,170 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	118,096,905 bp
RNA expression pattern
	Top expressed in
	body of tongue; ; biceps brachii; ; Skeletal muscle tissue of biceps brachii; ; Skeletal muscle tissue of rectus abdominis; ; muscle of thigh; ; pons; ; gastrocnemius muscle; ; spinal ganglia; ; buccal mucosa cell; ; vastus lateralis muscle;
	Top expressed in
	anterior amygdaloid area; ; pontine nuclei; ; subiculum; ; digastric muscle; ; temporal muscle; ; mammillary body; ; dorsal tegmental nucleus; ; ventromedial nucleus; ; lateral hypothalamus; ; sternocleidomastoid muscle;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	transmembrane transporter binding; tetrahydrobiopterin binding; NADP binding; cadmium ion binding; FMN binding; metal ion binding; heme binding; oxidoreductase activity; scaffold protein binding; calmodulin binding; protein binding; sodium channel regulator activity; flavin adenine dinucleotide binding; arginine binding; nitric-oxide synthase activity; NADPH-hemoprotein reductase activity;
Cellular component	membrane; photoreceptor inner segment; T-tubule; synapse; ryanodine receptor complex; mitochondrion; perinuclear region of cytoplasm; caveola; cytoskeleton; cell projection; dendritic spine; Z discdkac; sarcoplasmic reticulum membrane; membrane raft; sarcoplasmic reticulum; sarcolemma; cytosol; cytoplasm; nucleoplasm; plasma membrane; protein-containing complex; calyx of Held; nucleus; vesicle membrane; postsynaptic density;
Biological process	multicellular organismal response to stress; positive regulation of guanylate cyclase activity; regulation of sodium ion transport; positive regulation of the force of heart contraction; negative regulation of hydrolase activity; striated muscle contraction; regulation of neurogenesis; negative regulation of serotonin uptake; positive regulation of transcription, DNA-templated; peptidyl-cysteine S-nitrosylation; cell redox homeostasis; arginine catabolic process; negative regulation of potassium ion transport; nitric oxide mediated signal transduction; negative regulation of calcium ion transport into cytosol; myoblast fusion; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; regulation of ryanodine-sensitive calcium-release channel activity; regulation of cardiac conduction; nitric oxide biosynthetic process; positive regulation of sodium ion transmembrane transport; cellular response to growth factor stimulus; neurotransmitter biosynthetic process; positive regulation of histone acetylation; negative regulation of calcium ion transport; regulation of cardiac muscle contraction; positive regulation of transcription by RNA polymerase II; response to hypoxia; response to heat; negative regulation of blood pressure; retrograde trans-synaptic signaling by nitric oxide; vasodilation; positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; synaptic signaling by nitric oxide; response to hormone; response to lipopolysaccharide; positive regulation of peptidyl-serine phosphorylation;
	Sources:Amigo / QuickGO
Orthologs
	4842
	18125
	ENSG00000089250
	ENSMUSG00000029361
	P29475
	Q9Z0J4
	NM_000620; NM_001204213; NM_001204214; NM_001204218
	NM_008712
	NP_000611; NP_001191142; NP_001191143; NP_001191147
	NP_032738
	Wikidata
View/Edit Human	View/Edit Mouse

Nitric oxide synthase 1 (neuronal), also known as NOS1, is an enzyme that in humans is encoded by the NOS1 gene.^[5]^[6]

Function

Nitric oxide synthases (EC 1.14.13.39) (NOSs) are a family of synthases that catalyze the production of nitric oxide (NO) from L-arginine. NO is a chemical messenger with diverse functions throughout the body depending on its enzymatic source and tissue localization. In the brain and peripheral nervous system, where NOS1 is largely present, NO displays many properties of a neurotransmitter and may be involved in long term potentiation. It is implicated in neurotoxicity associated with stroke and neurodegenerative diseases, neural regulation of smooth muscle, including peristalsis and sphincter relaxation, and penile erection. NO is also responsible for endothelium-derived relaxing factor activity regulating blood pressure as produced from its related enzyme NOS3. In macrophages, NO mediates tumoricidal and bactericidal actions, as produced from its related enzyme NOS2. Various pharmacological inhibitors of NO synthases (NOS) block these effects, but further distinction of their function has been elucidated by animal models in which these specific genes have been inactivated. Neuronal NOS (NOS1), Endothelial NOS (NOS3), and Inducible NOS macrophage NOS are distinct isoforms.^[7] Both the neuronal and the macrophage forms are unusual among oxidative enzymes in requiring several electron donors: flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN), NADPH, and tetrahydrobiopterin.^[8]

Clinical significance

It has been implicated in asthma,^[9]^[10] schizophrenia,^[11]^[12] restless leg syndrome,^[13] and psychostimulant neurotoxicity. It has also been investigated with respect to bipolar disorder^[14] and air pollution exposure.^[15]

Interactions

NOS1 has been shown to interact with DLG4^[16]^[17] and NOS1AP.^[16]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000089250 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000029361 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Kishimoto J, Spurr N, Liao M, Lizhi L, Emson P, Xu W (November 1992). "Localization of brain nitric oxide synthase (NOS) to human chromosome 12". Genomics. 14 (3): 802–4. doi:10.1016/S0888-7543(05)80192-2. PMID 1385308.
^ Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR (April 1993). "Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes". Proc. Natl. Acad. Sci. U.S.A. 90 (8): 3491–5. Bibcode:1993PNAS...90.3491G. doi:10.1073/pnas.90.8.3491. PMC 46326. PMID 7682706.
^ Lowenstein CJ, Glatt CS, Bredt DS, Snyder SH (August 1992). "Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme". Proc. Natl. Acad. Sci. U.S.A. 89 (15): 6711–5. Bibcode:1992PNAS...89.6711L. doi:10.1073/pnas.89.15.6711. PMC 49573. PMID 1379716.
^ "Entrez Gene: NOS1 Nitric oxide synthase 1 (neuronal)".
^ Grasemann H, Yandava CN, Drazen JM (December 1999). "Neuronal NO synthase (NOS1) is a major candidate gene for asthma". Clin. Exp. Allergy. 29. 29 (Suppl 4): 39–41. PMID 10641565. Archived from the original on 2013-01-05.
^ Leung TF, Liu EK, Tang NL, Ko FW, Li CY, Lam CW, Wong GW (October 2005). "Nitric oxide synthase polymorphisms and asthma phenotypes in Chinese children". Clin. Exp. Allergy. 35 (10): 1288–94. doi:10.1111/j.1365-2222.2005.02342.x. PMID 16238787. S2CID 24110873.
^ Shinkai T, Ohmori O, Hori H, Nakamura J (2002). "Allelic association of the neuronal nitric oxide synthase (NOS1) gene with schizophrenia". Mol. Psychiatry. 7 (6): 560–3. doi:10.1038/sj.mp.4001041. PMID 12140778.
^ Reif A, Herterich S, Strobel A, Ehlis AC, Saur D, Jacob CP, Wienker T, Töpner T, Fritzen S, Walter U, Schmitt A, Fallgatter AJ, Lesch KP (March 2006). "A neuronal nitric oxide synthase (NOS-I) haplotype associated with schizophrenia modifies prefrontal cortex function". Mol. Psychiatry. 11 (3): 286–300. doi:10.1038/sj.mp.4001779. PMID 16389274.
^ Winkelmann J, Lichtner P, Schormair B, Uhr M, Hauk S, Stiasny-Kolster K, Trenkwalder C, Paulus W, Peglau I, Eisensehr I, Illig T, Wichmann HE, Pfister H, Golic J, Bettecken T, Pütz B, Holsboer F, Meitinger T, Müller-Myhsok B (February 2008). "Variants in the neuronal nitric oxide synthase (nNOS, NOS1) gene are associated with restless legs syndrome". Mov. Disord. 23 (3): 350–8. doi:10.1002/mds.21647. PMID 18058820. S2CID 42425890.
^ Buttenschön HN, Mors O, Ewald H, McQuillin A, Kalsi G, Lawrence J, Gurling H, Kruse TA (January 2004). "No association between a neuronal nitric oxide synthase (NOS1) gene polymorphism on chromosome 12q24 and bipolar disorder". Am. J. Med. Genet. B Neuropsychiatr. Genet. 124B (1): 73–5. doi:10.1002/ajmg.b.20040. PMID 14681919. S2CID 45596789.
^ Steenackers W, De Herdt E, De Boever P, Bos I, Int Panis L (2013). "Neuroinflammation induced by air pollution: gene expression analysis in laboratory animals". Master Thesis, GROUP T – Leuven Engineering College.
^ ^a ^b Jaffrey SR, Snowman AM, Eliasson MJ, Cohen NA, Snyder SH (January 1998). "CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95". Neuron. 20 (1): 115–24. doi:10.1016/S0896-6273(00)80439-0. PMID 9459447. S2CID 14613261.
^ Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, Santillano DR, Wu Z, Huang F, Xia H, Peters MF, Froehner SC, Bredt DS (March 1996). "Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains". Cell. 84 (5): 757–67. doi:10.1016/S0092-8674(00)81053-3. PMID 8625413. S2CID 15834673.

NOS1

Contents

Function

Clinical significance

Interactions

See also

References

Further reading