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Nitric oxide synthase, inducible (EC 1.14.13.39) (Hepatocyte NOS) (HEP-NOS) (Inducible NO synthase) (Inducible NOS) (iNOS) (NOS type II) (Peptidyl-cysteine S-nitrosylase NOS2)

 NOS2_HUMAN              Reviewed;        1153 AA.
P35228; A1L3U5; B7ZLY2; O60757; O94994; Q16263; Q16692; Q4TTS5;
Q9UD42;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
27-SEP-2017, entry version 205.
RecName: Full=Nitric oxide synthase, inducible;
EC=1.14.13.39;
AltName: Full=Hepatocyte NOS;
Short=HEP-NOS;
AltName: Full=Inducible NO synthase;
Short=Inducible NOS;
Short=iNOS;
AltName: Full=NOS type II;
AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2;
Name=NOS2; Synonyms=NOS2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
TISSUE=Colon adenocarcinoma;
PubMed=7692964; DOI=10.1021/bi00094a017;
Sherman P.A., Laubach V.E., Reep B.R., Wood E.R.;
"Purification and cDNA sequence of an inducible nitric oxide synthase
from a human tumor cell line.";
Biochemistry 32:11600-11605(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=7682706; DOI=10.1073/pnas.90.8.3491;
Geller D.A., Lowenstein C.J., Shapiro R.A., Nussler A.K.,
di Silvio M., Wang S.C., Nakayama D.K., Simmons R.L., Snyder S.H.,
Billiar T.R.;
"Molecular cloning and expression of inducible nitric oxide synthase
from human hepatocytes.";
Proc. Natl. Acad. Sci. U.S.A. 90:3491-3495(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Chondrocyte;
PubMed=7504305; DOI=10.1073/pnas.90.23.11419;
Charles I.G., Palmer R.M.J., Hickery M.S., Bayliss M.T., Chubb A.P.,
Hall V.S., Moss D.W., Moncada S.;
"Cloning, characterization, and expression of a cDNA encoding an
inducible nitric oxide synthase from the human chondrocyte.";
Proc. Natl. Acad. Sci. U.S.A. 90:11419-11423(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Articular chondrocyte;
PubMed=7522054; DOI=10.1016/0167-4838(94)90171-6;
Maier R., Bilbe G., Rediske J., Lotz M.;
"Inducible nitric oxide synthase from human articular chondrocytes:
cDNA cloning and analysis of mRNA expression.";
Biochim. Biophys. Acta 1208:145-150(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-608, AND FUNCTION.
TISSUE=Retina;
PubMed=7528017; DOI=10.1006/bbrc.1994.2633;
Park C.S., Pardhasaradhi K., Gianotti C., Villegas E., Krishna G.;
"Human retina expresses both constitutive and inducible isoforms of
nitric oxide synthase mRNA.";
Biochem. Biophys. Res. Commun. 205:85-91(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-608.
TISSUE=Glioblastoma;
PubMed=7531687;
Hokari A., Zeniya M., Esumi H.;
"Cloning and functional expression of human inducible nitric oxide
synthase (NOS) cDNA from a glioblastoma cell line A-172.";
J. Biochem. 116:575-581(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Airway epithelium;
PubMed=7544004; DOI=10.1073/pnas.92.17.7809;
Guo F.H., de Raeve R.H., Rice T.W., Stuehr D.J., Thunnissen F.B.J.M.,
Erzurum S.C.;
"Continuous nitric oxide synthesis by inducible nitric oxide synthase
in normal human airway epithelium in vivo.";
Proc. Natl. Acad. Sci. U.S.A. 92:7809-7813(1995).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Cardiac myocyte;
PubMed=9160867; DOI=10.1006/jmcc.1996.0349;
Luss H., Li R.-K., Shapiro R.A., Tzeng E., McGowan F.X., Yoneyama T.,
Hatakayama K., Geller D.A., Mickle D.A.G., Simmons R.L., Billiar T.R.;
"Dedifferentiated human ventricular cardiac myocytes express inducible
nitric oxide synthase mRNA but not protein in response to IL-1, TNF,
IFNgamma, and LPS.";
J. Mol. Cell. Cardiol. 29:1153-1165(1997).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Ogawa Y., Nishijima S., Goto M., Ida M.;
"Cloning and characterization of a novel splice valiant of human
inducible nitric oxide synthase.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-221; LEU-608;
ALA-747 AND CYS-1009.
NIEHS SNPs program;
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 380-473.
TISSUE=Kidney;
PubMed=7532248; DOI=10.1038/ki.1994.365;
McLay J.S., Chatterjee P., Nicolson A.G., Jardine A.G., McKay N.G.,
Ralston S.H., Grabowski P., Haites N.E., Macleod A.M.,
Hawksworth G.M.;
"Nitric oxide production by human proximal tubular cells: a novel
immunomodulatory mechanism?";
Kidney Int. 46:1043-1049(1994).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 667-831, AND INDUCTION.
TISSUE=Glioblastoma;
PubMed=7528267;
Fujisawa H., Ogura T., Hokari A., Weisz A., Yamashita J., Esumi H.;
"Inducible nitric oxide synthase in a human glioblastoma cell line.";
J. Neurochem. 64:85-91(1995).
[15]
CHARACTERIZATION.
PubMed=7558036; DOI=10.1006/geno.1995.1086;
Bloch K.D., Wolfram J.R., Brown D.M., Roberts J.D. Jr., Zapol D.G.,
Lepore J.J., Filippov G., Thomas J.E., Jacob H.J., Bloch D.B.;
"Three members of the nitric oxide synthase II gene family (NOS2A,
NOS2B, and NOS2C) colocalize to human chromosome 17.";
Genomics 27:526-530(1995).
[16]
CHARACTERIZATION.
PubMed=9721329;
Taylor B.S., Alarcon L.H., Billiar T.R.;
"Inducible nitric oxide synthase in the liver: regulation and
function.";
Biochemistry (Mosc.) 63:766-781(1998).
[17]
INTERACTION WITH SLC9A3R1.
PubMed=12080081; DOI=10.1074/jbc.M205764200;
Glynne P.A., Darling K.E.A., Picot J., Evans T.J.;
"Epithelial inducible nitric-oxide synthase is an apical EBP50-binding
protein that directs vectorial nitric oxide output.";
J. Biol. Chem. 277:33132-33138(2002).
[18]
POLYMORPHISM, AND INVOLVEMENT IN RESISTANCE TO MALARIA.
PubMed=12433515; DOI=10.1016/S0140-6736(02)11474-7;
Hobbs M.R., Udhayakumar V., Levesque M.C., Booth J., Roberts J.M.,
Tkachuk A.N., Pole A., Coon H., Kariuki S., Nahlen B.L.,
Mwaikambo E.D., Lal A.L., Granger D.L., Anstey N.M., Weinberg J.B.;
"A new NOS2 promoter polymorphism associated with increased nitric
oxide production and protection from severe malaria in Tanzanian and
Kenyan children.";
Lancet 360:1468-1475(2002).
[19]
FUNCTION.
PubMed=19688109; DOI=10.1155/2009/345838;
Vuolteenaho K., Koskinen A., Kukkonen M., Nieminen R.,
Paeivaerinta U., Moilanen T., Moilanen E.;
"Leptin enhances synthesis of proinflammatory mediators in human
osteoarthritic cartilage--mediator role of NO in leptin-induced PGE2,
IL-6, and IL-8 production.";
Mediators Inflamm. 2009:345838-345838(2009).
[20]
FUNCTION, INTERACTION WITH S100A8 AND S100A9, ASSEMBLY IN THE
INOS-S100A8/A9 COMPLEX, AND INDUCTION BY LDL.
PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L.,
Fox P.L.;
"Target-selective protein S-nitrosylation by sequence motif
recognition.";
Cell 159:623-634(2014).
[21]
INDUCTION.
PubMed=25180171; DOI=10.1016/j.redox.2014.06.011;
Cortese-Krott M.M., Kulakov L., Oplaender C., Kolb-Bachofen V.,
Kroencke K.D., Suschek C.V.;
"Zinc regulates iNOS-derived nitric oxide formation in endothelial
cells.";
Redox Biol. 2:945-954(2014).
[22]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 74-504.
PubMed=10409685; DOI=10.1074/jbc.274.30.21276;
Li H., Raman C.S., Glaser C.B., Blasko E., Young T.A., Parkinson J.F.,
Whitlow M., Poulos T.L.;
"Crystal structures of zinc-free and -bound heme domain of human
inducible nitric-oxide synthase. Implications for dimer stability and
comparison with endothelial nitric-oxide synthase.";
J. Biol. Chem. 274:21276-21284(1999).
[23]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 82-528.
PubMed=10074942; DOI=10.1038/6675;
Fischmann T.O., Hruza A., Niu X.D., Fossetta J.D., Lunn C.A.,
Dolphin E., Prongay A.J., Reichert P., Lundell D.J., Narula S.K.,
Weber P.C.;
"Structural characterization of nitric oxide synthase isoforms reveals
striking active-site conservation.";
Nat. Struct. Biol. 6:233-242(1999).
[24]
VARIANT [LARGE SCALE ANALYSIS] SER-679.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[25]
VARIANT LEU-608, AND CHARACTERIZATION OF VARIANT LEU-608.
PubMed=24430113; DOI=10.1038/ctg.2013.17;
Dhillon S.S., Mastropaolo L.A., Murchie R., Griffiths C., Thoeni C.,
Elkadri A., Xu W., Mack A., Walters T., Guo C., Mack D., Huynh H.,
Baksh S., Silverberg M.S., Brumell J.H., Snapper S.B., Muise A.M.;
"Higher activity of the inducible nitric oxide synthase contributes to
very early onset inflammatory bowel disease.";
Clin. Transl. Gastroenterol. 5:E46-E46(2014).
-!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule
with diverse functions throughout the body (PubMed:7531687,
PubMed:7544004). In macrophages, NO mediates tumoricidal and
bactericidal actions. Also has nitrosylase activity and mediates
cysteine S-nitrosylation of cytoplasmic target proteins such
PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9
transnitrosylase complex involved in the selective inflammatory
stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247'
implicated in regulation of the GAIT complex activity and probably
multiple targets including ANXA5, EZR, MSN and VIM
(PubMed:25417112). Involved in inflammation, enhances the
synthesis of proinflammatory mediators such as IL6 and IL8
(PubMed:19688109). {ECO:0000250|UniProtKB:P29477,
ECO:0000269|PubMed:19688109, ECO:0000269|PubMed:25417112,
ECO:0000269|PubMed:7531687, ECO:0000269|PubMed:7544004}.
-!- 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; Evidence={ECO:0000250};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD. {ECO:0000250};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
Note=Binds 1 FMN. {ECO:0000250};
-!- COFACTOR:
Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250};
Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of
the enzyme. {ECO:0000250};
-!- ENZYME REGULATION: Regulated by calcium/calmodulin. Aspirin
inhibits expression and function of this enzyme and effects may be
exerted at the level of translational/post-translational
modification and directly on the catalytic activity (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Binds SLC9A3R1. Interacts with GAPDH; induced
by oxidatively-modified low-densitity lipoprotein (LDL(ox)).
Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9
transnitrosylase complex. {ECO:0000269|PubMed:25417112}.
-!- INTERACTION:
P04406:GAPDH; NbExp=8; IntAct=EBI-6662224, EBI-354056;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P35228-1; Sequence=Displayed;
Name=2;
IsoId=P35228-2; Sequence=VSP_003582, VSP_003583;
-!- TISSUE SPECIFICITY: Expressed in the liver, retina, bone cells and
airway epithelial cells of the lung. Not expressed in the
platelets.
-!- INDUCTION: By endotoxins and cytokines. Induced by IFNG/IFN-gamma
acting synergistically with bacterial lipopolysaccharides (LPS),
TNF or IL1B/interleukin-1 beta (PubMed:7528267). Down-regulated by
zinc due to inhibition of NF-kappa-B transactivation activity
(PubMed:25180171). By oxidatively-modified low-densitity
lipoprotein (LDL(ox)) (PubMed:25417112).
{ECO:0000269|PubMed:25180171, ECO:0000269|PubMed:25417112,
ECO:0000269|PubMed:7528267}.
-!- POLYMORPHISM: Note=Genetic variations in NOS2 are involved in
resistance to malaria [MIM:611162]. {ECO:0000269|PubMed:12433515}.
-!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/nos2a/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Nitric oxide synthase entry;
URL="https://en.wikipedia.org/wiki/Nitric_oxide_synthase";
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EMBL; L24553; AAA36375.1; -; mRNA.
EMBL; L09210; AAA59171.1; -; mRNA.
EMBL; X73029; CAA51512.1; -; mRNA.
EMBL; U05810; AAA56666.1; -; mRNA.
EMBL; U31511; AAB49041.1; -; mRNA.
EMBL; D26525; BAA05531.1; -; mRNA.
EMBL; U20141; AAB60366.1; -; mRNA.
EMBL; AF068236; AAC19133.1; -; mRNA.
EMBL; AB022318; BAA37123.1; -; mRNA.
EMBL; DQ060518; AAY43131.1; -; Genomic_DNA.
EMBL; EU332854; ABY87543.1; -; Genomic_DNA.
EMBL; BC130283; AAI30284.1; -; mRNA.
EMBL; BC144126; AAI44127.1; -; mRNA.
EMBL; S75615; AAD14179.1; -; mRNA.
CCDS; CCDS11223.1; -. [P35228-1]
PIR; A49676; A49676.
RefSeq; NP_000616.3; NM_000625.4. [P35228-1]
RefSeq; XP_011523161.1; XM_011524859.2. [P35228-1]
UniGene; Hs.709191; -.
PDB; 1NSI; X-ray; 2.55 A; A/B/C/D=74-504.
PDB; 2LL6; NMR; -; B=515-531.
PDB; 2NSI; X-ray; 3.00 A; A/B/C/D=74-504.
PDB; 3E7G; X-ray; 2.20 A; A/B/C/D=82-505.
PDB; 3EJ8; X-ray; 2.55 A; A/B/C/D=82-505.
PDB; 3HR4; X-ray; 2.50 A; A/C/E/G=503-715.
PDB; 4CX7; X-ray; 3.16 A; A/B/C/D=74-504.
PDB; 4NOS; X-ray; 2.25 A; A/B/C/D=82-508.
PDBsum; 1NSI; -.
PDBsum; 2LL6; -.
PDBsum; 2NSI; -.
PDBsum; 3E7G; -.
PDBsum; 3EJ8; -.
PDBsum; 3HR4; -.
PDBsum; 4CX7; -.
PDBsum; 4NOS; -.
ProteinModelPortal; P35228; -.
SMR; P35228; -.
BioGrid; 110906; 146.
CORUM; P35228; -.
DIP; DIP-59359N; -.
IntAct; P35228; 4.
STRING; 9606.ENSP00000327251; -.
BindingDB; P35228; -.
ChEMBL; CHEMBL4481; -.
DrugBank; DB01997; 3-Bromo-7-Nitroindazole.
DrugBank; DB08214; 4-(1H-IMIDAZOL-1-YL)PHENOL.
DrugBank; DB07002; 4-({4-[(4-methoxypyridin-2-yl)amino]piperidin-1-yl}carbonyl)benzonitrile.
DrugBank; DB01835; 4r-Fluoro-N6-Ethanimidoyl-L-Lysine.
DrugBank; DB04534; 5-Nitroindazole.
DrugBank; DB03100; 6-Nitroindazole.
DrugBank; DB02207; 7-Nitroindazole.
DrugBank; DB05252; ACCLAIM.
DrugBank; DB02533; Aminoguanidine.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB07306; ETHYL 4-[(4-CHLOROPYRIDIN-2-YL)AMINO]PIPERIDINE-1-CARBOXYLATE.
DrugBank; DB07388; ETHYL 4-[(4-METHYLPYRIDIN-2-YL)AMINO]PIPERIDINE-1-CARBOXYLATE.
DrugBank; DB02234; Ethylisothiourea.
DrugBank; DB05214; KD7040.
DrugBank; DB00125; L-Arginine.
DrugBank; DB00155; L-Citrulline.
DrugBank; DB03953; L-Thiocitrulline.
DrugBank; DB01110; Miconazole.
DrugBank; DB02044; N-(3-(Aminomethyl)Benzyl)Acetamidine.
DrugBank; DB03449; N-(4-(2-((3-Chlorophenylmethyl)Amino)Ethyl)Phenyl)-2-Thiophecarboxamidine.
DrugBank; DB07389; N-[2-(6-AMINO-4-METHYLPYRIDIN-2-YL)ETHYL]-4-CYANOBENZAMIDE.
DrugBank; DB03144; N-Omega-Hydroxy-L-Arginine.
DrugBank; DB02644; N-Omega-Propyl-L-Arginine.
DrugBank; DB02539; S-Ethylisothiourea.
DrugBank; DB02462; Thiocoumarin.
DrugBank; DB08814; Triflusal.
GuidetoPHARMACOLOGY; 1250; -.
iPTMnet; P35228; -.
PhosphoSitePlus; P35228; -.
SwissPalm; P35228; -.
BioMuta; NOS2; -.
DMDM; 1352513; -.
EPD; P35228; -.
PaxDb; P35228; -.
PeptideAtlas; P35228; -.
PRIDE; P35228; -.
Ensembl; ENST00000313735; ENSP00000327251; ENSG00000007171. [P35228-1]
Ensembl; ENST00000621962; ENSP00000482291; ENSG00000007171. [P35228-2]
GeneID; 4843; -.
KEGG; hsa:4843; -.
UCSC; uc002gzu.4; human. [P35228-1]
CTD; 4843; -.
DisGeNET; 4843; -.
EuPathDB; HostDB:ENSG00000007171.16; -.
GeneCards; NOS2; -.
H-InvDB; HIX0027239; -.
HGNC; HGNC:7873; NOS2.
HPA; CAB002014; -.
MalaCards; NOS2; -.
MIM; 163730; gene.
MIM; 611162; phenotype.
neXtProt; NX_P35228; -.
OpenTargets; ENSG00000007171; -.
PharmGKB; PA164724093; -.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
eggNOG; COG4362; LUCA.
GeneTree; ENSGT00840000129757; -.
HOVERGEN; HBG000159; -.
InParanoid; P35228; -.
KO; K13241; -.
OMA; TNSPTFL; -.
OrthoDB; EOG091G10Z0; -.
PhylomeDB; P35228; -.
TreeFam; TF324410; -.
BioCyc; MetaCyc:HS00205-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-6785807; Interleukin-4 and 13 signaling.
SignaLink; P35228; -.
SIGNOR; P35228; -.
ChiTaRS; NOS2; human.
EvolutionaryTrace; P35228; -.
GeneWiki; Nitric_oxide_synthase_2_(inducible); -.
GenomeRNAi; 4843; -.
PRO; PR:P35228; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000007171; -.
CleanEx; HS_NOS2; -.
Genevisible; P35228; HS.
GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IMP:BHF-UCL.
GO; GO:0005622; C:intracellular; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0034618; F:arginine 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:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; TAS:BHF-UCL.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
GO; GO:0004517; F:nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0034617; F:tetrahydrobiopterin binding; ISS:BHF-UCL.
GO; GO:0006527; P:arginine catabolic process; IDA:BHF-UCL.
GO; GO:0045454; P:cell redox homeostasis; TAS:Reactome.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IMP:BHF-UCL.
GO; GO:0050829; P:defense response to Gram-negative bacterium; NAS:BHF-UCL.
GO; GO:0002227; P:innate immune response in mucosa; NAS:BHF-UCL.
GO; GO:0072604; P:interleukin-6 secretion; IDA:UniProtKB.
GO; GO:0072606; P:interleukin-8 secretion; IDA:UniProtKB.
GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central.
GO; GO:0010629; P:negative regulation of gene expression; IGI:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISS:UniProtKB.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IBA:GO_Central.
GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:GO_Central.
GO; GO:0051712; P:positive regulation of killing of cells of other organism; IMP:BHF-UCL.
GO; GO:0001912; P:positive regulation of leukocyte mediated cytotoxicity; TAS:BHF-UCL.
GO; GO:0032310; P:prostaglandin secretion; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043457; P:regulation of cellular respiration; TAS:BHF-UCL.
GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; IDA:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; IMP:BHF-UCL.
GO; GO:0009617; P:response to bacterium; NAS:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0006801; P:superoxide metabolic process; ISS:UniProtKB.
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; 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.
PIRSF; PIRSF000333; NOS; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Calmodulin-binding;
Complete proteome; FAD; Flavoprotein; FMN; Heme; Iron; Metal-binding;
NADP; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome; Zinc.
CHAIN 1 1153 Nitric oxide synthase, inducible.
/FTId=PRO_0000170930.
DOMAIN 539 677 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 730 970 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 623 654 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 767 778 FAD. {ECO:0000250}.
NP_BIND 903 913 FAD. {ECO:0000250}.
NP_BIND 978 996 NADP. {ECO:0000250}.
NP_BIND 1076 1091 NADP. {ECO:0000250}.
REGION 509 529 Calmodulin-binding. {ECO:0000255}.
METAL 110 110 Zinc.
METAL 115 115 Zinc.
METAL 200 200 Iron (heme axial ligand).
MOD_RES 234 234 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 575 575 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q06518}.
MOD_RES 578 578 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 892 892 Phosphoserine; by PKA. {ECO:0000255}.
VAR_SEQ 264 288 Missing (in isoform 2).
{ECO:0000303|Ref.9}.
/FTId=VSP_003582.
VAR_SEQ 298 311 Missing (in isoform 2).
{ECO:0000303|Ref.9}.
/FTId=VSP_003583.
VARIANT 221 221 R -> W (in dbSNP:rs3730017).
{ECO:0000269|Ref.10}.
/FTId=VAR_024548.
VARIANT 608 608 S -> L (polymorphism; found in patients
with very early onset inflammatory bowel
disease; increases NOS2 activity;
dbSNP:rs2297518).
{ECO:0000269|PubMed:24430113,
ECO:0000269|PubMed:7528017,
ECO:0000269|PubMed:7531687,
ECO:0000269|Ref.10}.
/FTId=VAR_022127.
VARIANT 679 679 A -> S (in a breast cancer sample;
somatic mutation; dbSNP:rs769900089).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036302.
VARIANT 747 747 T -> A (in dbSNP:rs28944173).
{ECO:0000269|Ref.10}.
/FTId=VAR_025020.
VARIANT 1009 1009 R -> C (in dbSNP:rs28944201).
{ECO:0000269|Ref.10}.
/FTId=VAR_025021.
CONFLICT 23 23 D -> G (in Ref. 4; AAA56666).
{ECO:0000305}.
CONFLICT 154 154 F -> L (in Ref. 4; AAA56666).
{ECO:0000305}.
CONFLICT 177 177 G -> V (in Ref. 4; AAA56666).
{ECO:0000305}.
CONFLICT 266 266 R -> H (in Ref. 8; AAC19133).
{ECO:0000305}.
CONFLICT 423 423 L -> I (in Ref. 2; AAA59171).
{ECO:0000305}.
CONFLICT 439 439 A -> T (in Ref. 8; AAC19133).
{ECO:0000305}.
CONFLICT 552 552 A -> G (in Ref. 12; AAI44127).
{ECO:0000305}.
CONFLICT 676 676 T -> I (in Ref. 7; AAB60366).
{ECO:0000305}.
CONFLICT 800 800 T -> A (in Ref. 4; AAA56666).
{ECO:0000305}.
CONFLICT 805 805 A -> D (in Ref. 2; AAA59171).
{ECO:0000305}.
CONFLICT 831 832 FL -> SP (in Ref. 2; AAA59171).
{ECO:0000305}.
CONFLICT 913 913 S -> P (in Ref. 4; AAA56666).
{ECO:0000305}.
CONFLICT 933 933 R -> G (in Ref. 2; AAA59171 and 7;
AAB60366). {ECO:0000305}.
CONFLICT 966 966 G -> A (in Ref. 2; AAA59171 and 7;
AAB60366). {ECO:0000305}.
CONFLICT 987 987 A -> V (in Ref. 2; AAA59171).
{ECO:0000305}.
STRAND 85 89 {ECO:0000244|PDB:3E7G}.
TURN 90 92 {ECO:0000244|PDB:3E7G}.
STRAND 95 98 {ECO:0000244|PDB:3E7G}.
HELIX 100 103 {ECO:0000244|PDB:3E7G}.
STRAND 104 106 {ECO:0000244|PDB:4NOS}.
HELIX 123 125 {ECO:0000244|PDB:3E7G}.
HELIX 136 152 {ECO:0000244|PDB:3E7G}.
STRAND 154 156 {ECO:0000244|PDB:1NSI}.
HELIX 159 175 {ECO:0000244|PDB:3E7G}.
HELIX 183 195 {ECO:0000244|PDB:3E7G}.
HELIX 203 205 {ECO:0000244|PDB:3E7G}.
STRAND 210 213 {ECO:0000244|PDB:3E7G}.
HELIX 220 235 {ECO:0000244|PDB:3E7G}.
HELIX 236 238 {ECO:0000244|PDB:3E7G}.
STRAND 243 246 {ECO:0000244|PDB:3E7G}.
STRAND 251 255 {ECO:0000244|PDB:3E7G}.
STRAND 261 265 {ECO:0000244|PDB:3E7G}.
STRAND 269 271 {ECO:0000244|PDB:3E7G}.
STRAND 277 279 {ECO:0000244|PDB:3E7G}.
HELIX 281 283 {ECO:0000244|PDB:3E7G}.
HELIX 284 292 {ECO:0000244|PDB:3E7G}.
STRAND 307 310 {ECO:0000244|PDB:3E7G}.
STRAND 317 319 {ECO:0000244|PDB:3E7G}.
HELIX 323 325 {ECO:0000244|PDB:3E7G}.
STRAND 328 330 {ECO:0000244|PDB:3E7G}.
HELIX 337 342 {ECO:0000244|PDB:3E7G}.
STRAND 345 348 {ECO:0000244|PDB:3E7G}.
STRAND 356 359 {ECO:0000244|PDB:3E7G}.
STRAND 362 365 {ECO:0000244|PDB:3E7G}.
HELIX 375 379 {ECO:0000244|PDB:3E7G}.
HELIX 381 384 {ECO:0000244|PDB:3E7G}.
TURN 386 389 {ECO:0000244|PDB:3E7G}.
HELIX 392 399 {ECO:0000244|PDB:3E7G}.
HELIX 406 408 {ECO:0000244|PDB:3E7G}.
HELIX 410 428 {ECO:0000244|PDB:3E7G}.
HELIX 436 454 {ECO:0000244|PDB:3E7G}.
HELIX 461 464 {ECO:0000244|PDB:3E7G}.
STRAND 467 469 {ECO:0000244|PDB:3E7G}.
HELIX 470 472 {ECO:0000244|PDB:3E7G}.
HELIX 474 477 {ECO:0000244|PDB:3E7G}.
STRAND 486 491 {ECO:0000244|PDB:3E7G}.
HELIX 495 498 {ECO:0000244|PDB:3E7G}.
HELIX 515 534 {ECO:0000244|PDB:3HR4}.
STRAND 538 544 {ECO:0000244|PDB:3HR4}.
STRAND 546 548 {ECO:0000244|PDB:3HR4}.
HELIX 549 561 {ECO:0000244|PDB:3HR4}.
TURN 562 564 {ECO:0000244|PDB:3HR4}.
STRAND 565 571 {ECO:0000244|PDB:3HR4}.
HELIX 572 574 {ECO:0000244|PDB:3HR4}.
HELIX 577 581 {ECO:0000244|PDB:3HR4}.
STRAND 584 591 {ECO:0000244|PDB:3HR4}.
TURN 594 596 {ECO:0000244|PDB:3HR4}.
HELIX 600 602 {ECO:0000244|PDB:3HR4}.
HELIX 603 611 {ECO:0000244|PDB:3HR4}.
STRAND 620 627 {ECO:0000244|PDB:3HR4}.
STRAND 631 633 {ECO:0000244|PDB:3HR4}.
HELIX 636 648 {ECO:0000244|PDB:3HR4}.
STRAND 651 654 {ECO:0000244|PDB:3HR4}.
STRAND 657 660 {ECO:0000244|PDB:3HR4}.
HELIX 665 683 {ECO:0000244|PDB:3HR4}.
HELIX 689 691 {ECO:0000244|PDB:3HR4}.
SEQUENCE 1153 AA; 131117 MW; 47671E5385CB3A52 CRC64;
MACPWKFLFK TKFHQYAMNG EKDINNNVEK APCATSSPVT QDDLQYHNLS KQQNESPQPL
VETGKKSPES LVKLDATPLS SPRHVRIKNW GSGMTFQDTL HHKAKGILTC RSKSCLGSIM
TPKSLTRGPR DKPTPPDELL PQAIEFVNQY YGSFKEAKIE EHLARVEAVT KEIETTGTYQ
LTGDELIFAT KQAWRNAPRC IGRIQWSNLQ VFDARSCSTA REMFEHICRH VRYSTNNGNI
RSAITVFPQR SDGKHDFRVW NAQLIRYAGY QMPDGSIRGD PANVEFTQLC IDLGWKPKYG
RFDVVPLVLQ ANGRDPELFE IPPDLVLEVA MEHPKYEWFR ELELKWYALP AVANMLLEVG
GLEFPGCPFN GWYMGTEIGV RDFCDVQRYN ILEEVGRRMG LETHKLASLW KDQAVVEINI
AVLHSFQKQN VTIMDHHSAA ESFMKYMQNE YRSRGGCPAD WIWLVPPMSG SITPVFHQEM
LNYVLSPFYY YQVEAWKTHV WQDEKRRPKR REIPLKVLVK AVLFACMLMR KTMASRVRVT
ILFATETGKS EALAWDLGAL FSCAFNPKVV CMDKYRLSCL EEERLLLVVT STFGNGDCPG
NGEKLKKSLF MLKELNNKFR YAVFGLGSSM YPRFCAFAHD IDQKLSHLGA SQLTPMGEGD
ELSGQEDAFR SWAVQTFKAA CETFDVRGKQ HIQIPKLYTS NVTWDPHHYR LVQDSQPLDL
SKALSSMHAK NVFTMRLKSR QNLQSPTSSR ATILVELSCE DGQGLNYLPG EHLGVCPGNQ
PALVQGILER VVDGPTPHQT VRLEALDESG SYWVSDKRLP PCSLSQALTY FLDITTPPTQ
LLLQKLAQVA TEEPERQRLE ALCQPSEYSK WKFTNSPTFL EVLEEFPSLR VSAGFLLSQL
PILKPRFYSI SSSRDHTPTE IHLTVAVVTY HTRDGQGPLH HGVCSTWLNS LKPQDPVPCF
VRNASGFHLP EDPSHPCILI GPGTGIAPFR SFWQQRLHDS QHKGVRGGRM TLVFGCRRPD
EDHIYQEEML EMAQKGVLHA VHTAYSRLPG KPKVYVQDIL RQQLASEVLR VLHKEPGHLY
VCGDVRMARD VAHTLKQLVA AKLKLNEEQV EDYFFQLKSQ KRYHEDIFGA VFPYEAKKDR
VAVQPSSLEM SAL


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