Misplaced Pages

NOS1

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
(Redirected from NNOS)

Protein-coding gene in the species Homo sapiens
NOS1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4D1N, 4UCH, 4UH5, 4UH6, 4V3U, 5ADF, 5ADG, 5ADI, 5FVX, 5FVW, 5FVU, 5FVV

Identifiers
AliasesNOS1, IHPS1, N-NOS, NC-NOS, NOS, bNOS, nNOS, nitric oxide synthase 1
External IDsOMIM: 163731; MGI: 97360; HomoloGene: 37327; GeneCards: NOS1; OMA:NOS1 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)
Chromosome 12 (human)Genomic location for NOS1Genomic location for NOS1
Band12q24.22Start117,208,142 bp
End117,452,170 bp
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)
Chromosome 5 (mouse)Genomic location for NOS1Genomic location for NOS1
Band5 F|5 57.29 cMStart117,919,097 bp
End118,096,905 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
BioGPS


More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4842

18125

Ensembl

ENSG00000089250

ENSMUSG00000029361

UniProt

P29475

Q9Z0J4

RefSeq (mRNA)

NM_000620
NM_001204213
NM_001204214
NM_001204218

NM_008712

RefSeq (protein)

NP_000611
NP_001191142
NP_001191143
NP_001191147

NP_032738

Location (UCSC)Chr 12: 117.21 – 117.45 MbChr 5: 117.92 – 118.1 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

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

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. 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.

Clinical significance

It has been implicated in asthma, schizophrenia, restless leg syndrome, and psychostimulant neurotoxicity. It has also been investigated with respect to bipolar disorder and air pollution exposure.

Interactions

NOS1 has been shown to interact with DLG4 and NOS1AP.

See also

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000089250 – Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000029361 – Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. 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.
  7. 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.
  8. "Entrez Gene: NOS1 Nitric oxide synthase 1 (neuronal)".
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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.
  15. 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.
  16. ^ 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.
  17. 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.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

PDB gallery
  • 1b8q: SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE 1b8q: SOLUTION STRUCTURE OF THE EXTENDED NEURONAL NITRIC OXIDE SYNTHASE PDZ DOMAIN COMPLEXED WITH AN ASSOCIATED PEPTIDE
  • 1f20: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION. 1f20: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE FAD/NADP+ DOMAIN AT 1.9A RESOLUTION.
  • 1k2r: Structure of rat brain nNOS heme domain complexed with NG-nitro-L-arginine 1k2r: Structure of rat brain nNOS heme domain complexed with NG-nitro-L-arginine
  • 1k2s: Structure of rat brain nNOS heme domain complexed with NG-allyl-L-arginine 1k2s: Structure of rat brain nNOS heme domain complexed with NG-allyl-L-arginine
  • 1k2t: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-phenyl-isothiourea 1k2t: Structure of rat brain nNOS heme domain complexed with S-ethyl-N-phenyl-isothiourea
  • 1k2u: Structure of rat brain nNOS heme domain complexed with S-ethyl-N- isothiourea 1k2u: Structure of rat brain nNOS heme domain complexed with S-ethyl-N- isothiourea
  • 1lzx: Rat neuronal NOS heme domain with NG-hydroxy-L-arginine bound 1lzx: Rat neuronal NOS heme domain with NG-hydroxy-L-arginine bound
  • 1lzz: Rat neuronal NOS heme domain with N-isopropyl-N'-hydroxyguanidine bound 1lzz: Rat neuronal NOS heme domain with N-isopropyl-N'-hydroxyguanidine bound
  • 1m00: Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound 1m00: Rat neuronal NOS heme domain with N-butyl-N'-hydroxyguanidine bound
  • 1mmv: Rat neuronal NOS heme domain with NG-propyl-L-arginine bound 1mmv: Rat neuronal NOS heme domain with NG-propyl-L-arginine bound
  • 1mmw: Rat neuronal NOS heme domain with vinyl-L-NIO bound 1mmw: Rat neuronal NOS heme domain with vinyl-L-NIO bound
  • 1om4: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH L-ARGININE BOUND 1om4: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH L-ARGININE BOUND
  • 1om5: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH 3-BROMO-7-NITROINDAZOLE BOUND 1om5: STRUCTURE OF RAT NEURONAL NOS HEME DOMAIN WITH 3-BROMO-7-NITROINDAZOLE BOUND
  • 1p6h: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound 1p6h: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound
  • 1p6i: Rat neuronal NOS heme domain with (4S)-N-(4-amino-5-aminopentyl)-N'-nitroguanidine bound 1p6i: Rat neuronal NOS heme domain with (4S)-N-(4-amino-5-aminopentyl)-N'-nitroguanidine bound
  • 1p6j: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-(4R)-amino-L-proline amide bound 1p6j: Rat neuronal NOS heme domain with L-N(omega)-nitroarginine-(4R)-amino-L-proline amide bound
  • 1p6k: Rat neuronal NOS D597N mutant heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound 1p6k: Rat neuronal NOS D597N mutant heme domain with L-N(omega)-nitroarginine-2,4-L-diaminobutyric amide bound
  • 1qau: UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX 1qau: UNEXPECTED MODES OF PDZ DOMAIN SCAFFOLDING REVEALED BY STRUCTURE OF NNOS-SYNTROPHIN COMPLEX
  • 1qav: Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of NNOS-Syntrophin Complex 1qav: Unexpected Modes of PDZ Domain Scaffolding Revealed by Structure of NNOS-Syntrophin Complex
  • 1qw6: Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg. 1qw6: Rat neuronal nitric oxide synthase oxygenase domain in complex with N-omega-propyl-L-Arg.
  • 1qwc: Rat neuronal nitric oxide synthase oxygenase domain in complex with W1400 inhibitor. 1qwc: Rat neuronal nitric oxide synthase oxygenase domain in complex with W1400 inhibitor.
  • 1rs6: Rat neuronal NOS heme domain with D-lysine-D-nitroarginine amide bound 1rs6: Rat neuronal NOS heme domain with D-lysine-D-nitroarginine amide bound
  • 1rs7: Rat neuronal NOS heme domain with D-phenylalanine-D-nitroarginine amide bound 1rs7: Rat neuronal NOS heme domain with D-phenylalanine-D-nitroarginine amide bound
  • 1tll: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE REDUCTASE MODULE AT 2.3 A RESOLUTION. 1tll: CRYSTAL STRUCTURE OF RAT NEURONAL NITRIC-OXIDE SYNTHASE REDUCTASE MODULE AT 2.3 A RESOLUTION.
  • 1vag: Neuronal nitric oxide synthase oxygenase domain complexed with the inhibitor AR-R17477 1vag: Neuronal nitric oxide synthase oxygenase domain complexed with the inhibitor AR-R17477
  • 1zvi: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain 1zvi: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain
  • 1zvl: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed with natural substrate L-Arg. 1zvl: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain complexed with natural substrate L-Arg.
  • 1zzq: Rat nNOS D597N mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound 1zzq: Rat nNOS D597N mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound
  • 1zzr: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound 1zzr: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-(4R)-amino-L-proline amide bound
  • 1zzu: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-2,4-L-Diaminobutyric Amide Bound 1zzu: Rat nNOS D597N/M336V double mutant with L-N(omega)-Nitroarginine-2,4-L-Diaminobutyric Amide Bound
  • 2g6h: Structure of rat nNOS heme domain (BH4 bound) in the reduced form 2g6h: Structure of rat nNOS heme domain (BH4 bound) in the reduced form
  • 2g6i: Structure of rat nNOS heme domain (BH2-bound) in the reduced form 2g6i: Structure of rat nNOS heme domain (BH2-bound) in the reduced form
  • 2g6j: Structure of rat nNOS (L337N) heme domain (4-aminobiopterin bound) complexed with NO 2g6j: Structure of rat nNOS (L337N) heme domain (4-aminobiopterin bound) complexed with NO
  • 2g6k: Structure of rat nNOS heme domain (BH4 bound) complexed with NO 2g6k: Structure of rat nNOS heme domain (BH4 bound) complexed with NO
  • 2g6l: Structure of rat nNOS heme domain (BH2 bound) complexed with NO 2g6l: Structure of rat nNOS heme domain (BH2 bound) complexed with NO
  • 2g6m: Structure of rat nNOS heme domain (BH4 bound) complexed with CO 2g6m: Structure of rat nNOS heme domain (BH4 bound) complexed with CO
  • 2g6n: Structure of rat nNOS heme domain (BH2 bound) complexed with CO 2g6n: Structure of rat nNOS heme domain (BH2 bound) complexed with CO
  • 2hx3: Rat nNOS heme domain complexed with (4S)-N-{4-Amino-5--pentyl}-N'-nitroguanidine 2hx3: Rat nNOS heme domain complexed with (4S)-N-{4-Amino-5--pentyl}-N'-nitroguanidine
  • 2hx4: Rat nNOS heme domain complexed with 4-N-(Nw-nitro-L-argininyl)-trans-4-hydroxyamino-L-proline amide 2hx4: Rat nNOS heme domain complexed with 4-N-(Nw-nitro-L-argininyl)-trans-4-hydroxyamino-L-proline amide
Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)
1.14.11: 2-oxoglutarate
1.14.13: NADH or NADPH
1.14.14: reduced flavin or flavoprotein
1.14.15: reduced iron–sulfur protein
1.14.16: reduced pteridine (BH4 dependent)
1.14.17: reduced ascorbate
1.14.18-19: other
1.14.99 - miscellaneous
Enzymes involved in neurotransmission
monoamine
histidine → histamine
anabolism:
catabolism:
tyrosine→dopamine→epinephrine
anabolism:
catabolism:
glutamate→GABA
anabolism:
catabolism:
tryptophan→serotonin→melatonin
arginine→NO
choline→Acetylcholine
anabolism:
catabolism:
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Nitric oxide signaling modulators
Forms
Targets
sGC
  • Inhibitors: ODQ
NO donors
(prodrugs)
Enzyme
(inhibitors)
NOS
nNOS
iNOS
eNOS
Unsorted
Arginase
CAMK
Others
See also: Receptor/signaling modulators
Portal:


Stub icon

This article on a gene on human chromosome 12 is a stub. You can help Misplaced Pages by expanding it.

Categories: