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Nitric oxide synthase, brain (EC 1.14.13.39) (Constitutive NOS) (NC-NOS) (NOS type I) (Neuronal NOS) (N-NOS) (nNOS) (Peptidyl-cysteine S-nitrosylase NOS1) (bNOS)

 NOS1_HUMAN              Reviewed;        1434 AA.
P29475; E9PH30; O75713;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
05-JUL-2017, entry version 194.
RecName: Full=Nitric oxide synthase, brain;
EC=1.14.13.39;
AltName: Full=Constitutive NOS;
AltName: Full=NC-NOS;
AltName: Full=NOS type I;
AltName: Full=Neuronal NOS;
Short=N-NOS;
Short=nNOS;
AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
AltName: Full=bNOS;
Name=NOS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=7528745;
Hall A.V., Antoniou H., Wang Y., Cheung A.H., Arbus A.M., Olson S.L.,
Lu W.C., Kau C.-L., Marsden P.A.;
"Structural organization of the human neuronal nitric oxide synthase
gene (NOS1).";
J. Biol. Chem. 269:33082-33090(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum;
PubMed=7515942;
Fujisawa H., Ogura T., Kurashima Y., Yokoyama T., Yamashita J.,
Esumi H.;
"Expression of two types of nitric oxide synthase mRNA in human
neuroblastoma cell lines.";
J. Neurochem. 63:140-145(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=7678401; DOI=10.1016/0014-5793(93)81210-Q;
Nakane M., Schmidt H.H.H.W., Pollock J.S., Foerstermann U., Murad F.;
"Cloned human brain nitric oxide synthase is highly expressed in
skeletal muscle.";
FEBS Lett. 316:175-180(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
PubMed=8879752; DOI=10.1007/BF02150230;
Park C.-S., Gianotti C., Park R., Krishna G.;
"Neuronal isoform of nitric oxide synthase is expressed at low levels
in human retina.";
Cell. Mol. Neurobiol. 16:499-515(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4).
TISSUE=Testis;
PubMed=9111048; DOI=10.1074/jbc.272.17.11128;
Wang Y., Goligorsky M.S., Lin M., Wilcox J.N., Marsden P.A.;
"A novel, testis-specific mRNA transcript encoding an NH2-terminal
truncated nitric-oxide synthase.";
J. Biol. Chem. 272:11392-11401(1997).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-228; ALA-394;
ASP-725; ASP-864 AND ARG-1064.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 835-901 (ISOFORM 5), AND ALTERNATIVE
SPLICING.
TISSUE=Skeletal muscle;
PubMed=9791007; DOI=10.1006/bbrc.1998.9578;
Larsson B., Phillips S.C.;
"Isolation and characterization of a novel, human neuronal nitric
oxide synthase cDNA.";
Biochem. Biophys. Res. Commun. 251:898-902(1998).
-!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule
with diverse functions throughout the body. In the brain and
peripheral nervous system, NO displays many properties of a
neurotransmitter. Probably has nitrosylase activity and mediates
cysteine S-nitrosylation of cytoplasmic target proteins such SRR.
-!- CATALYTIC ACTIVITY: 2 L-arginine + 3 NADPH + 4 O(2) = 2 L-
citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD.;
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Note=Binds 1 FMN.;
-!- COFACTOR:
Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
Xref=ChEBI:CHEBI:59560;
Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of
the enzyme.;
-!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by
n-Nos-inhibiting protein (PIN) which may prevent the dimerization
of the protein. Inhibited by NOSIP.
-!- SUBUNIT: Homodimer. Interacts with DLG4; the interaction possibly
being prevented by the association between NOS1 and CAPON. Forms a
ternary complex with CAPON and RASD1. Forms a ternary complex with
CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP;
which may impair its synaptic location (By similarity). Interacts
with HTR4. Interacts with VAC14 (By similarity). Interacts with
SLC6A4 (By similarity). Interacts (via N-terminal domain) with
DLG4 (via N-terminal tandem pair of PDZ domains) (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q08AM6:VAC14; NbExp=5; IntAct=EBI-7164065, EBI-2107455;
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
membrane protein. Cell projection, dendritic spine {ECO:0000250}.
Note=In skeletal muscle, it is localized beneath the sarcolemma of
fast-twitch muscle fiber by associating with the dystrophin
glycoprotein complex. In neurons, enriched in dendritic spines (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Isoform 3 is produced by different alternative splicing
events implicating either the untranslated exons TEX1 (TN-NOS)
or TEX1B (TN-NOSB) leading to a N-terminally truncated protein
which possesses enzymatic activity comparable to that of isoform
1. The C-terminally truncated isoform 4 is produced by insertion
of the TEX2 exon between exons 3 and 4 of isoform 1, leading to
a frameshift and a premature stop codon.
{ECO:0000269|PubMed:9791007};
Name=1; Synonyms=N-NOS-1;
IsoId=P29475-1; Sequence=Displayed;
Name=2; Synonyms=N-NOS-2;
IsoId=P29475-2; Sequence=VSP_003574;
Name=3; Synonyms=TN-NOS, TN-NOSB;
IsoId=P29475-3; Sequence=VSP_003571;
Name=4; Synonyms=TEX2-insertion;
IsoId=P29475-4; Sequence=VSP_003572, VSP_003573;
Name=5; Synonyms=nNOSmu;
IsoId=P29475-5; Sequence=VSP_044916;
-!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed: detected
in skeletal muscle and brain, also in testis, lung and kidney, and
at low levels in heart, adrenal gland and retina. Not detected in
the platelets. Isoform 3 is expressed only in testis. Isoform 4 is
detected in testis, skeletal muscle, lung, and kidney, at low
levels in the brain, but not in the heart and adrenal gland.
-!- DOMAIN: The PDZ domain in the N-terminal part of the neuronal
isoform participates in protein-protein interaction, and is
responsible for targeting nNos to synaptic membranes in muscles.
Mediates interaction with VAC14 (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of
Hsp70 and Hsp40 (in vitro). {ECO:0000250}.
-!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nos1/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Nitric oxide synthase entry;
URL="https://en.wikipedia.org/wiki/Nitric_oxide_synthase";
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EMBL; U17327; AAA62405.1; -; mRNA.
EMBL; U17326; AAB60654.1; ALT_SEQ; Genomic_DNA.
EMBL; U17299; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17300; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17301; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17302; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17303; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17304; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17305; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17307; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17308; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17309; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17310; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17311; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17312; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17313; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17314; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17315; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17316; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17317; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17318; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17319; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17320; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17321; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17322; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17323; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17324; AAB60654.1; JOINED; Genomic_DNA.
EMBL; U17325; AAB60654.1; JOINED; Genomic_DNA.
EMBL; D16408; BAA03895.1; -; mRNA.
EMBL; L02881; AAA36376.1; -; mRNA.
EMBL; U31466; AAB49040.1; -; mRNA.
EMBL; U66362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY445095; AAR07069.1; -; Genomic_DNA.
EMBL; AC026364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ004918; CAA06218.1; -; mRNA.
CCDS; CCDS41842.1; -. [P29475-1]
CCDS; CCDS55890.1; -. [P29475-5]
PIR; G01946; G01946.
RefSeq; NP_000611.1; NM_000620.4. [P29475-1]
RefSeq; NP_001191142.1; NM_001204213.1. [P29475-3]
RefSeq; NP_001191143.1; NM_001204214.1. [P29475-3]
RefSeq; NP_001191147.1; NM_001204218.1. [P29475-5]
RefSeq; XP_011536700.1; XM_011538398.2. [P29475-5]
RefSeq; XP_016874834.1; XM_017019345.1. [P29475-5]
RefSeq; XP_016874835.1; XM_017019346.1. [P29475-5]
RefSeq; XP_016874836.1; XM_017019347.1. [P29475-1]
UniGene; Hs.654410; -.
UniGene; Hs.684465; -.
UniGene; Hs.684466; -.
UniGene; Hs.684467; -.
UniGene; Hs.735734; -.
PDB; 4D1N; X-ray; 2.03 A; A/B/C/D=302-721.
PDB; 4UCH; X-ray; 2.20 A; A/B=302-723.
PDB; 4UH5; X-ray; 1.98 A; A/B=302-722.
PDB; 4UH6; X-ray; 1.98 A; A/B=302-722.
PDB; 4V3U; X-ray; 2.30 A; A/B/C/D=302-721.
PDB; 5ADF; X-ray; 1.97 A; A/B=302-722.
PDB; 5ADG; X-ray; 1.98 A; A/B=302-722.
PDB; 5ADI; X-ray; 2.20 A; A/B=302-722.
PDB; 5FVU; X-ray; 2.22 A; A/B=302-722.
PDB; 5FVV; X-ray; 2.05 A; A/B=302-722.
PDB; 5FVW; X-ray; 2.20 A; A/B=302-722.
PDB; 5FVX; X-ray; 2.30 A; A/B=302-722.
PDB; 5UO1; X-ray; 1.90 A; A/B=302-722.
PDB; 5UO2; X-ray; 1.95 A; A/B=302-722.
PDB; 5UO3; X-ray; 2.20 A; A/B=302-722.
PDB; 5UO4; X-ray; 2.00 A; A/B=302-722.
PDB; 5UO5; X-ray; 2.00 A; A/B=302-722.
PDB; 5UO6; X-ray; 1.96 A; A/B=302-722.
PDB; 5UO7; X-ray; 2.06 A; A/B=302-722.
PDBsum; 4D1N; -.
PDBsum; 4UCH; -.
PDBsum; 4UH5; -.
PDBsum; 4UH6; -.
PDBsum; 4V3U; -.
PDBsum; 5ADF; -.
PDBsum; 5ADG; -.
PDBsum; 5ADI; -.
PDBsum; 5FVU; -.
PDBsum; 5FVV; -.
PDBsum; 5FVW; -.
PDBsum; 5FVX; -.
PDBsum; 5UO1; -.
PDBsum; 5UO2; -.
PDBsum; 5UO3; -.
PDBsum; 5UO4; -.
PDBsum; 5UO5; -.
PDBsum; 5UO6; -.
PDBsum; 5UO7; -.
ProteinModelPortal; P29475; -.
SMR; P29475; -.
BioGrid; 110905; 15.
DIP; DIP-40999N; -.
IntAct; P29475; 3.
MINT; MINT-122019; -.
STRING; 9606.ENSP00000337459; -.
BindingDB; P29475; -.
ChEMBL; CHEMBL3568; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB01997; 3-Bromo-7-Nitroindazole.
DrugBank; DB03892; 5-N-Allyl-Arginine.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB01942; Formic Acid.
DrugBank; DB00155; L-Citrulline.
DrugBank; DB02077; L-N(Omega)-Nitroarginine-(4r)-Amino-L-Proline Amide.
DrugBank; DB09241; Methylene blue.
DrugBank; DB02044; N-(3-(Aminomethyl)Benzyl)Acetamidine.
DrugBank; DB03449; N-(4-(2-((3-Chlorophenylmethyl)Amino)Ethyl)Phenyl)-2-Thiophecarboxamidine.
DrugBank; DB02727; N-Butyl-N'-Hydroxyguanidine.
DrugBank; DB02143; N-Isopropyl-N'-Hydroxyguanidine.
DrugBank; DB03144; N-Omega-Hydroxy-L-Arginine.
DrugBank; DB02644; N-Omega-Propyl-L-Arginine.
DrugBank; DB02027; N-{(4s)-4-Amino-5-[(2-Aminoethyl)Amino]Pentyl}-N'-Nitroguanidine.
DrugBank; DB03710; N5-(1-Imino-3-Butenyl)-L-Ornithine.
DrugBank; DB04223; Nitroarginine.
DrugBank; DB06096; NXN-188.
DrugBank; DB03247; Riboflavin Monophosphate.
DrugBank; DB02991; S-Ethyl-N-[4-(Trifluoromethyl)Phenyl]Isothiourea.
DrugBank; DB03707; S-Ethyl-N-Phenyl-Isothiourea.
GuidetoPHARMACOLOGY; 1251; -.
iPTMnet; P29475; -.
PhosphoSitePlus; P29475; -.
BioMuta; NOS1; -.
DMDM; 1709333; -.
EPD; P29475; -.
MaxQB; P29475; -.
PaxDb; P29475; -.
PeptideAtlas; P29475; -.
PRIDE; P29475; -.
DNASU; 4842; -.
Ensembl; ENST00000317775; ENSP00000320758; ENSG00000089250. [P29475-1]
Ensembl; ENST00000338101; ENSP00000337459; ENSG00000089250. [P29475-5]
Ensembl; ENST00000618760; ENSP00000477999; ENSG00000089250. [P29475-5]
GeneID; 4842; -.
KEGG; hsa:4842; -.
UCSC; uc001twm.3; human. [P29475-1]
CTD; 4842; -.
DisGeNET; 4842; -.
GeneCards; NOS1; -.
HGNC; HGNC:7872; NOS1.
HPA; CAB002167; -.
HPA; HPA058312; -.
MalaCards; NOS1; -.
MIM; 163731; gene.
neXtProt; NX_P29475; -.
OpenTargets; ENSG00000089250; -.
PharmGKB; PA252; -.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
eggNOG; COG4362; LUCA.
GeneTree; ENSGT00840000129757; -.
HOGENOM; HOG000220884; -.
HOVERGEN; HBG000159; -.
InParanoid; P29475; -.
KO; K13240; -.
OMA; DDNRYHE; -.
OrthoDB; EOG091G10Z0; -.
PhylomeDB; P29475; -.
TreeFam; TF324410; -.
BioCyc; MetaCyc:HS01647-MONOMER; -.
BRENDA; 1.14.13.39; 2681.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-392154; Nitric oxide stimulates guanylate cyclase.
Reactome; R-HSA-5578775; Ion homeostasis.
SIGNOR; P29475; -.
ChiTaRS; NOS1; human.
GeneWiki; NOS1; -.
GenomeRNAi; 4842; -.
PMAP-CutDB; P29475; -.
PRO; PR:P29475; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000089250; -.
CleanEx; HS_NOS1; -.
ExpressionAtlas; P29475; baseline and differential.
Genevisible; P29475; HS.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; TAS:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0045121; C:membrane raft; ISS:BHF-UCL.
GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
GO; GO:0001917; C:photoreceptor inner segment; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0043234; C:protein complex; ISS:BHF-UCL.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0045202; C:synapse; ISS:BHF-UCL.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0034618; F:arginine binding; TAS:BHF-UCL.
GO; GO:0046870; F:cadmium ion binding; ISS:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:BHF-UCL.
GO; GO:0010181; F:FMN binding; ISS:BHF-UCL.
GO; GO:0020037; F:heme binding; ISS:BHF-UCL.
GO; GO:0044325; F:ion channel binding; ISS:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; ISS:BHF-UCL.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
GO; GO:0004517; F:nitric-oxide synthase activity; IDA:CACAO.
GO; GO:0097110; F:scaffold protein binding; ISS:BHF-UCL.
GO; GO:0017080; F:sodium channel regulator activity; ISS:BHF-UCL.
GO; GO:0034617; F:tetrahydrobiopterin binding; NAS:BHF-UCL.
GO; GO:0006527; P:arginine catabolic process; IC:BHF-UCL.
GO; GO:0045454; P:cell redox homeostasis; TAS:Reactome.
GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:BHF-UCL.
GO; GO:0042738; P:exogenous drug catabolic process; ISS:BHF-UCL.
GO; GO:0033555; P:multicellular organismal response to stress; IMP:BHF-UCL.
GO; GO:0007520; P:myoblast fusion; TAS:BHF-UCL.
GO; GO:1901205; P:negative regulation of adrenergic receptor signaling pathway involved in heart process; TAS:BHF-UCL.
GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central.
GO; GO:0051926; P:negative regulation of calcium ion transport; ISS:BHF-UCL.
GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; TAS:BHF-UCL.
GO; GO:0051346; P:negative regulation of hydrolase activity; ISS:BHF-UCL.
GO; GO:0043267; P:negative regulation of potassium ion transport; ISS:BHF-UCL.
GO; GO:0051612; P:negative regulation of serotonin uptake; ISS:BHF-UCL.
GO; GO:0042136; P:neurotransmitter biosynthetic process; TAS:BHF-UCL.
GO; GO:0006809; P:nitric oxide biosynthetic process; ISS:BHF-UCL.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISS:BHF-UCL.
GO; GO:1901206; P:positive regulation of adrenergic receptor signaling pathway involved in heart process; IEA:Ensembl.
GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:GO_Central.
GO; GO:0035066; P:positive regulation of histone acetylation; ISS:BHF-UCL.
GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; ISS:BHF-UCL.
GO; GO:0098735; P:positive regulation of the force of heart contraction; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
GO; GO:1902514; P:regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; TAS:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0055117; P:regulation of cardiac muscle contraction; TAS:BHF-UCL.
GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; TAS:BHF-UCL.
GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL.
GO; GO:0009408; P:response to heat; IDA:BHF-UCL.
GO; GO:0001666; P:response to hypoxia; IEP:BHF-UCL.
GO; GO:0098924; P:retrograde trans-synaptic signaling by nitric oxide; IEA:Ensembl.
GO; GO:0006941; P:striated muscle contraction; ISS:BHF-UCL.
GO; GO:0042311; P:vasodilation; IDA:BHF-UCL.
Gene3D; 3.40.50.360; -; 1.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_dom.
InterPro; IPR012144; NOS_euk.
InterPro; IPR004030; NOS_N.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR001478; PDZ.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
Pfam; PF02898; NO_synthase; 1.
Pfam; PF00595; PDZ; 1.
PIRSF; PIRSF000333; NOS; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF56512; SSF56512; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PROSITE; PS60001; NOS; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane;
Cell projection; Complete proteome; FAD; Flavoprotein; FMN; Heme;
Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 1434 Nitric oxide synthase, brain.
/FTId=PRO_0000170921.
DOMAIN 17 99 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 760 940 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 995 1242 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 886 917 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 1032 1043 FAD. {ECO:0000250}.
NP_BIND 1175 1185 FAD. {ECO:0000250}.
NP_BIND 1250 1268 NADP. {ECO:0000250}.
NP_BIND 1348 1363 NADP. {ECO:0000250}.
REGION 1 205 Interaction with NOSIP. {ECO:0000250}.
REGION 163 245 PIN (nNOS-inhibiting protein) binding.
REGION 730 750 Calmodulin-binding. {ECO:0000255}.
REGION 755 774 Tetrahydrobiopterin-binding.
{ECO:0000250}.
METAL 420 420 Iron (heme axial ligand). {ECO:0000250}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000250|UniProtKB:P29476}.
MOD_RES 862 862 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0J4}.
MOD_RES 863 863 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0J4}.
VAR_SEQ 1 336 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_003571.
VAR_SEQ 285 407 PPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKS
TLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEF
IDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELI
-> MRKLRITEGFGVQRGSHNHPPPQENSPPQRMAAPPSVH
ASSRSRTGRLRWFSLTPSTLRAHWKRDALSTSAWAPSCILL
SMQGGLKTSAQKDSSSLSPKSLLINTIHQLKDLAPKPTWKG
WKR (in isoform 4). {ECO:0000305}.
/FTId=VSP_003572.
VAR_SEQ 408 1434 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_003573.
VAR_SEQ 509 613 Missing (in isoform 2).
{ECO:0000303|PubMed:7515942,
ECO:0000303|PubMed:7678401}.
/FTId=VSP_003574.
VAR_SEQ 844 844 K -> KYPEPLRFFPRKGPPLPNGDTEVHGLAAARDSQHR
(in isoform 5).
{ECO:0000303|PubMed:9791007}.
/FTId=VSP_044916.
VARIANT 228 228 P -> S (in dbSNP:rs9658279).
{ECO:0000269|Ref.6}.
/FTId=VAR_018948.
VARIANT 394 394 D -> A (in dbSNP:rs9658356).
{ECO:0000269|Ref.6}.
/FTId=VAR_018949.
VARIANT 725 725 N -> D (in dbSNP:rs9658403).
{ECO:0000269|Ref.6}.
/FTId=VAR_018950.
VARIANT 864 864 G -> D (in dbSNP:rs9658445).
{ECO:0000269|Ref.6}.
/FTId=VAR_018951.
VARIANT 1064 1064 Q -> R (in dbSNP:rs9658482).
{ECO:0000269|Ref.6}.
/FTId=VAR_018952.
CONFLICT 131 131 K -> E (in Ref. 4; AAB49040).
{ECO:0000305}.
CONFLICT 178 184 LAPRPPG -> WPQAPR (in Ref. 3 and 4).
{ECO:0000305}.
CONFLICT 492 493 QP -> HR (in Ref. 3; AAA36376).
{ECO:0000305}.
CONFLICT 549 549 V -> L (in Ref. 3; AAA36376).
{ECO:0000305}.
CONFLICT 563 563 G -> A (in Ref. 3; AAA36376).
{ECO:0000305}.
CONFLICT 1407 1407 Y -> I (in Ref. 3; AAA36376).
{ECO:0000305}.
STRAND 306 310 {ECO:0000244|PDB:5ADF}.
TURN 311 313 {ECO:0000244|PDB:5ADF}.
STRAND 316 319 {ECO:0000244|PDB:5ADF}.
HELIX 321 324 {ECO:0000244|PDB:5ADF}.
STRAND 333 336 {ECO:0000244|PDB:5FVU}.
HELIX 356 373 {ECO:0000244|PDB:5ADF}.
HELIX 380 396 {ECO:0000244|PDB:5ADF}.
HELIX 403 415 {ECO:0000244|PDB:5ADF}.
HELIX 423 425 {ECO:0000244|PDB:5ADF}.
STRAND 430 433 {ECO:0000244|PDB:5ADF}.
HELIX 440 455 {ECO:0000244|PDB:5ADF}.
HELIX 456 458 {ECO:0000244|PDB:5ADF}.
STRAND 463 466 {ECO:0000244|PDB:5ADF}.
STRAND 471 475 {ECO:0000244|PDB:5ADF}.
STRAND 481 485 {ECO:0000244|PDB:5ADF}.
STRAND 489 491 {ECO:0000244|PDB:5ADF}.
STRAND 497 499 {ECO:0000244|PDB:5ADF}.
HELIX 501 503 {ECO:0000244|PDB:5ADF}.
HELIX 504 512 {ECO:0000244|PDB:5ADF}.
STRAND 520 522 {ECO:0000244|PDB:4D1N}.
STRAND 527 530 {ECO:0000244|PDB:5ADF}.
STRAND 537 539 {ECO:0000244|PDB:5ADF}.
HELIX 543 545 {ECO:0000244|PDB:5ADF}.
STRAND 548 550 {ECO:0000244|PDB:5ADF}.
HELIX 557 562 {ECO:0000244|PDB:5ADF}.
STRAND 565 568 {ECO:0000244|PDB:5ADF}.
STRAND 576 579 {ECO:0000244|PDB:5ADF}.
STRAND 582 585 {ECO:0000244|PDB:5ADF}.
HELIX 595 599 {ECO:0000244|PDB:5ADF}.
HELIX 601 604 {ECO:0000244|PDB:5ADF}.
TURN 606 609 {ECO:0000244|PDB:5ADF}.
HELIX 612 618 {ECO:0000244|PDB:5ADF}.
HELIX 626 628 {ECO:0000244|PDB:5ADF}.
HELIX 630 648 {ECO:0000244|PDB:5ADF}.
HELIX 656 674 {ECO:0000244|PDB:5ADF}.
HELIX 681 684 {ECO:0000244|PDB:5ADF}.
STRAND 687 689 {ECO:0000244|PDB:5ADF}.
HELIX 690 692 {ECO:0000244|PDB:5ADF}.
HELIX 694 697 {ECO:0000244|PDB:5ADF}.
STRAND 706 710 {ECO:0000244|PDB:5ADF}.
HELIX 715 718 {ECO:0000244|PDB:5ADF}.
SEQUENCE 1434 AA; 160970 MW; 99235793B953BF37 CRC64;
MEDHMFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA
GDIILAVNGR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI
RVTQPLGPPT KAVDLSHQPP AGKEQPLAVD GASGPGNGPQ HAYDDGQEAG SLPHANGLAP
RPPGQDPAKK ATRVSLQGRG ENNELLKEIE PVLSLLTSGS RGVKGGAPAK AEMKDMGIQV
DRDLDGKSHK PLPLGVENDR VFNDLWGKGN VPVVLNNPYS EKEQPPTSGK QSPTKNGSPS
KCPRFLKVKN WETEVVLTDT LHLKSTLETG CTEYICMGSI MHPSQHARRP EDVRTKGQLF
PLAKEFIDQY YSSIKRFGSK AHMERLEEVN KEIDTTSTYQ LKDTELIYGA KHAWRNASRC
VGRIQWSKLQ VFDARDCTTA HGMFNYICNH VKYATNKGNL RSAITIFPQR TDGKHDFRVW
NSQLIRYAGY KQPDGSTLGD PANVQFTEIC IQQGWKPPRG RFDVLPLLLQ ANGNDPELFQ
IPPELVLEVP IRHPKFEWFK DLGLKWYGLP AVSNMLLEIG GLEFSACPFS GWYMGTEIGV
RDYCDNSRYN ILEEVAKKMN LDMRKTSSLW KDQALVEINI AVLYSFQSDK VTIVDHHSAT
ESFIKHMENE YRCRGGCPAD WVWIVPPMSG SITPVFHQEM LNYRLTPSFE YQPDPWNTHV
WKGTNGTPTK RRAIGFKKLA EAVKFSAKLM GQAMAKRVKA TILYATETGK SQAYAKTLCE
IFKHAFDAKV MSMEEYDIVH LEHETLVLVV TSTFGNGDPP ENGEKFGCAL MEMRHPNSVQ
EERKSYKVRF NSVSSYSDSQ KSSGDGPDLR DNFESAGPLA NVRFSVFGLG SRAYPHFCAF
GHAVDTLLEE LGGERILKMR EGDELCGQEE AFRTWAKKVF KAACDVFCVG DDVNIEKANN
SLISNDRSWK RNKFRLTFVA EAPELTQGLS NVHKKRVSAA RLLSRQNLQS PKSSRSTIFV
RLHTNGSQEL QYQPGDHLGV FPGNHEDLVN ALIERLEDAP PVNQMVKVEL LEERNTALGV
ISNWTDELRL PPCTIFQAFK YYLDITTPPT PLQLQQFASL ATSEKEKQRL LVLSKGLQEY
EEWKWGKNPT IVEVLEEFPS IQMPATLLLT QLSLLQPRYY SISSSPDMYP DEVHLTVAIV
SYRTRDGEGP IHHGVCSSWL NRIQADELVP CFVRGAPSFH LPRNPQVPCI LVGPGTGIAP
FRSFWQQRQF DIQHKGMNPC PMVLVFGCRQ SKIDHIYREE TLQAKNKGVF RELYTAYSRE
PDKPKKYVQD ILQEQLAESV YRALKEQGGH IYVCGDVTMA ADVLKAIQRI MTQQGKLSAE
DAGVFISRMR DDNRYHEDIF GVTLRTYEVT NRLRSESIAF IEESKKDTDE VFSS


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