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

 NOS2_MOUSE              Reviewed;        1144 AA.
P29477; O70515; O70516; Q5SXT3; Q6P6A0; Q8R410;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
22-NOV-2017, entry version 194.
RecName: Full=Nitric oxide synthase, inducible;
EC=1.14.13.39;
AltName: Full=Inducible NO synthase;
Short=Inducible NOS;
Short=iNOS;
AltName: Full=Macrophage NOS;
Short=MAC-NOS;
AltName: Full=NOS type II;
AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2;
Name=Nos2; Synonyms=Inosl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1373522; DOI=10.1126/science.1373522;
Xie Q.-W., Cho H.J., Calaycay J., Mumford R.A., Swiderek K.M.,
Lee T.D., Ding A., Troso T., Nathan C.;
"Cloning and characterization of inducible nitric oxide synthase from
mouse macrophages.";
Science 256:225-228(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1379716; DOI=10.1073/pnas.89.15.6711;
Lowenstein C.J., Glatt C.S., Bredt D.S., Snyder S.H.;
"Cloned and expressed macrophage nitric oxide synthase contrasts with
the brain enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 89:6711-6715(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1372907;
Lyons C.R., Orloff G.J., Cunningham J.M.;
"Molecular cloning and functional expression of an inducible nitric
oxide synthase from a murine macrophage cell line.";
J. Biol. Chem. 267:6370-6374(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=7503239;
Kone B.C., Schwoebel J., Turner P., Mohaupt M.G., Cangro C.B.;
"Role of NF-kappa B in the regulation of inducible nitric oxide
synthase in an MTAL cell line.";
Am. J. Physiol. 269:F718-F729(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-211; LEU-967 AND PHE-968.
STRAIN=B10.S/J, BALB/cByJ, DBA/2J, NOD/LtJ, and SJL/J; TISSUE=Spleen;
PubMed=10438970;
Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W.,
Blankenhorn E.P.;
"Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2
(monocyte chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are
candidates for eae7, a locus controlling susceptibility to monophasic
remitting/nonrelapsing experimental allergic encephalomyelitis.";
J. Immunol. 163:2262-2266(1999).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CD-1;
Coge F., Levacher B., Rique H., Leopold O., Boutin J.A.,
Galizzi J.-P.;
"Genomic structure of the murine inducible nitric oxide synthase (i-
NOS) gene.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR;
Hagiwara K., Endo Y., Xin H., Takahashi M., Huqun X., Nukiwa T.;
"Mouse inducible nitric oxide synthase mRNA.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary tumor;
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).
[10]
PROTEIN SEQUENCE OF 733-744, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[11]
EFFECT OF ASPIRIN.
TISSUE=Macrophage;
PubMed=7544010; DOI=10.1073/pnas.92.17.7926;
Amin A.R., Vyas P., Attur M., Leszczynska-Piziak J., Patel I.R.,
Weissmann G., Abramson S.B.;
"The mode of action of aspirin-like drugs: effect on inducible nitric
oxide synthase.";
Proc. Natl. Acad. Sci. U.S.A. 92:7926-7930(1995).
[12]
FUNCTION AS NITROSYLASE.
PubMed=16373578; DOI=10.1126/science.1119407;
Kim S.F., Huri D.A., Snyder S.H.;
"Inducible nitric oxide synthase binds, S-nitrosylates, and activates
cyclooxygenase-2.";
Science 310:1966-1970(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
INDUCTION.
PubMed=22073225; DOI=10.1371/journal.pone.0026954;
Niu S., Shingle D.L., Garbarino-Pico E., Kojima S., Gilbert M.,
Green C.B.;
"The circadian deadenylase Nocturnin is necessary for stabilization of
the iNOS mRNA in mice.";
PLoS ONE 6:E26954-E26954(2011).
[15]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 116-496.
PubMed=9334294; DOI=10.1126/science.278.5337.425;
Crane B.R., Arvai A.S., Gachhui R., Wu C., Ghosh D.K., Getzoff E.D.,
Stuehr D.J., Tainer J.A.;
"The structure of nitric oxide synthase oxygenase domain and inhibitor
complexes.";
Science 278:425-431(1997).
[16]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 77-496.
PubMed=9516116; DOI=10.1126/science.279.5359.2121;
Crane B.R., Arvai A.S., Ghosh D.K., Wu C., Getzoff E.D., Stuehr D.J.,
Tainer J.A.;
"Structure of nitric oxide synthase oxygenase dimer with pterin and
substrate.";
Science 279:2121-2126(1998).
[17]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
PubMed=10562538; DOI=10.1093/emboj/18.22.6260;
Ghosh D.K., Crane B.R., Ghosh S., Wolan D., Gachhui R., Crooks C.,
Presta A., Tainer J.A., Getzoff E.D., Stuehr D.J.;
"Inducible nitric oxide synthase: role of the N-terminal beta-hairpin
hook and pterin-binding segment in dimerization and
tetrahydrobiopterin interaction.";
EMBO J. 18:6260-6270(1999).
[18]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-499.
PubMed=10562539; DOI=10.1093/emboj/18.22.6271;
Crane B.R., Rosenfeld R.J., Arvai A.S., Ghosh D.K., Ghosh S.,
Tainer J.A., Stuehr D.J., Getzoff E.D.;
"N-terminal domain swapping and metal ion binding in nitric oxide
synthase dimerization.";
EMBO J. 18:6271-6281(1999).
[19]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
PubMed=10769116; DOI=10.1021/bi992409a;
Crane B.R., Arvai A.S., Ghosh S., Getzoff E.D., Stuehr D.J.,
Tainer J.A.;
"Structures of the N(omega)-hydroxy-L-arginine complex of inducible
nitric oxide synthase oxygenase dimer with active and inactive
pterins.";
Biochemistry 39:4608-4621(2000).
[20]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF TRP-457 MUTANTS.
PubMed=11669619; DOI=10.1021/bi011183k;
Aoyagi M., Arvai A.S., Ghosh S., Stuehr D.J., Tainer J.A.,
Getzoff E.D.;
"Structures of tetrahydrobiopterin binding-site mutants of inducible
nitric oxide synthase oxygenase dimer and implicated roles of
Trp457.";
Biochemistry 40:12826-12832(2001).
[21]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
PubMed=12437348; DOI=10.1021/bi026313j;
Rosenfeld R.J., Garcin E.D., Panda K., Andersson G., Aberg A.,
Wallace A.V., Morris G.M., Olson A.J., Stuehr D.J., Tainer J.A.,
Getzoff E.D.;
"Conformational changes in nitric oxide synthases induced by
chlorzoxazone and nitroindazoles: crystallographic and computational
analyses of inhibitor potency.";
Biochemistry 41:13915-13925(2002).
[22]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-495.
PubMed=12464241; DOI=10.1016/S0003-9861(02)00555-6;
Fedorov R., Ghosh D.K., Schlichting I.;
"Crystal structures of cyanide complexes of P450cam and the oxygenase
domain of inducible nitric oxide synthase -- structural models of the
short-lived oxygen complexes.";
Arch. Biochem. Biophys. 409:25-31(2003).
-!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule
with diverse functions throughout the body (PubMed:7503239). In
macrophages, NO mediates tumoricidal and bactericidal actions.
Also has nitrosylase activity and mediates cysteine S-
nitrosylation of cytoplasmic target proteins such PTGS2/COX2
(PubMed:16373578). As component of the iNOS-S100A8/9
transnitrosylase complex involved in the selective inflammatory
stimulus-dependent S-nitrosylation of GAPDH implicated in
regulation of the GAIT complex activity and probably multiple
targets including ANXA5, EZR, MSN and VIM (By similarity).
Involved in inflammation, enhances the synthesis of
proinflammatory mediators such as IL6 and IL8 (By similarity).
{ECO:0000250|UniProtKB:P35228, ECO:0000250|UniProtKB:P79290,
ECO:0000269|PubMed:16373578, ECO:0000269|PubMed:7503239}.
-!- 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: Not stimulated 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.
-!- SUBUNIT: Homodimer. Binds SLC9A3R1 (By similarity). Interacts with
GAPDH. Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9
transnitrosylase complex (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P35228}.
-!- INTERACTION:
Q04207:Rela; NbExp=3; IntAct=EBI-298897, EBI-644400;
-!- TISSUE SPECIFICITY: Macrophages.
-!- INDUCTION: By treatment with endotoxins or cytokines. By
lipopolysaccharides (LPS) (in vitro). Expression in the liver
oscillates in a circadian manner with peak levels occurring during
the late night. {ECO:0000269|PubMed:22073225}.
-!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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EMBL; M87039; AAA39315.1; -; mRNA.
EMBL; M92649; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M84373; AAA39834.1; -; mRNA.
EMBL; U43428; AAC52356.1; -; mRNA.
EMBL; AF065919; AAC17914.1; -; mRNA.
EMBL; AF065920; AAC17915.1; -; mRNA.
EMBL; AF065921; AAC17916.2; -; mRNA.
EMBL; AF065922; AAC17917.2; -; mRNA.
EMBL; AF065923; AAC17918.2; -; mRNA.
EMBL; AF427516; AAL24076.1; -; Genomic_DNA.
EMBL; AY090567; AAM11887.1; -; mRNA.
EMBL; AL592185; CAI25275.1; -; Genomic_DNA.
EMBL; BC062378; AAH62378.1; -; mRNA.
CCDS; CCDS25115.1; -.
PIR; A43271; A43271.
RefSeq; NP_001300850.1; NM_001313921.1.
RefSeq; NP_001300851.1; NM_001313922.1.
RefSeq; NP_035057.1; NM_010927.4.
UniGene; Mm.2893; -.
PDB; 1DD7; X-ray; 2.25 A; A=114-498.
PDB; 1DF1; X-ray; 2.35 A; A/B=77-499.
PDB; 1DWV; X-ray; 2.35 A; A/B=77-496.
PDB; 1DWW; X-ray; 2.35 A; A/B=77-496.
PDB; 1DWX; X-ray; 2.60 A; A/B=77-496.
PDB; 1JWJ; X-ray; 2.60 A; A/B=66-498.
PDB; 1JWK; X-ray; 2.30 A; A/B=66-498.
PDB; 1M8D; X-ray; 2.35 A; A/B=65-498.
PDB; 1M8E; X-ray; 2.90 A; A/B=65-498.
PDB; 1M8H; X-ray; 2.85 A; A/B=65-498.
PDB; 1M8I; X-ray; 2.70 A; A/B=65-498.
PDB; 1M9T; X-ray; 2.40 A; A/B=65-498.
PDB; 1N2N; X-ray; 2.40 A; A/B=77-495.
PDB; 1NOC; X-ray; 2.60 A; A=115-498.
PDB; 1NOD; X-ray; 2.60 A; A/B=77-499.
PDB; 1NOS; X-ray; 2.10 A; A=115-498.
PDB; 1QOM; X-ray; 2.70 A; A/B=65-498.
PDB; 1QW4; X-ray; 2.40 A; A/B=77-495.
PDB; 1QW5; X-ray; 2.70 A; A/B=77-495.
PDB; 1R35; X-ray; 2.30 A; A/B=66-498.
PDB; 1VAF; X-ray; 2.90 A; A/B=77-495.
PDB; 2BHJ; X-ray; 3.20 A; A=77-498.
PDB; 2NOD; X-ray; 2.60 A; A/B=77-499.
PDB; 2NOS; X-ray; 2.30 A; A=115-498.
PDB; 2ORO; X-ray; 2.00 A; A=114-498.
PDB; 2ORP; X-ray; 1.97 A; A=114-498.
PDB; 2ORQ; X-ray; 2.10 A; A=114-498.
PDB; 2ORR; X-ray; 2.00 A; A=114-498.
PDB; 2ORS; X-ray; 2.00 A; A=114-498.
PDB; 2ORT; X-ray; 1.87 A; A=114-498.
PDB; 2Y37; X-ray; 2.60 A; A/B=66-498.
PDB; 3DWJ; X-ray; 2.75 A; A/B=66-496.
PDB; 3E65; X-ray; 2.05 A; A/B=66-498.
PDB; 3E67; X-ray; 2.60 A; A/B=66-498.
PDB; 3E68; X-ray; 2.20 A; A/B=66-498.
PDB; 3E6L; X-ray; 2.30 A; A/B=66-498.
PDB; 3E6N; X-ray; 2.40 A; A/B=66-498.
PDB; 3E6O; X-ray; 2.60 A; A/B=66-498.
PDB; 3E6T; X-ray; 2.50 A; A/B=66-498.
PDB; 3E7I; X-ray; 2.90 A; A/B=66-498.
PDB; 3E7M; X-ray; 2.00 A; A/B=66-498.
PDB; 3E7T; X-ray; 2.60 A; A/B=66-498.
PDB; 3EAI; X-ray; 2.20 A; A/B=66-498.
PDB; 3EBD; X-ray; 2.40 A; A/B=66-498.
PDB; 3EBF; X-ray; 2.29 A; A/B=66-498.
PDB; 3GOF; X-ray; 1.45 A; C/D=503-518.
PDB; 3NOD; X-ray; 2.70 A; A/B=77-499.
PDB; 3NQS; X-ray; 2.20 A; A/B=66-498.
PDB; 3NW2; X-ray; 2.80 A; A/B=77-499.
PDB; 4JS9; X-ray; 2.78 A; A/B=66-496.
PDB; 4UX6; X-ray; 3.00 A; A=77-100, B=108-496.
PDBsum; 1DD7; -.
PDBsum; 1DF1; -.
PDBsum; 1DWV; -.
PDBsum; 1DWW; -.
PDBsum; 1DWX; -.
PDBsum; 1JWJ; -.
PDBsum; 1JWK; -.
PDBsum; 1M8D; -.
PDBsum; 1M8E; -.
PDBsum; 1M8H; -.
PDBsum; 1M8I; -.
PDBsum; 1M9T; -.
PDBsum; 1N2N; -.
PDBsum; 1NOC; -.
PDBsum; 1NOD; -.
PDBsum; 1NOS; -.
PDBsum; 1QOM; -.
PDBsum; 1QW4; -.
PDBsum; 1QW5; -.
PDBsum; 1R35; -.
PDBsum; 1VAF; -.
PDBsum; 2BHJ; -.
PDBsum; 2NOD; -.
PDBsum; 2NOS; -.
PDBsum; 2ORO; -.
PDBsum; 2ORP; -.
PDBsum; 2ORQ; -.
PDBsum; 2ORR; -.
PDBsum; 2ORS; -.
PDBsum; 2ORT; -.
PDBsum; 2Y37; -.
PDBsum; 3DWJ; -.
PDBsum; 3E65; -.
PDBsum; 3E67; -.
PDBsum; 3E68; -.
PDBsum; 3E6L; -.
PDBsum; 3E6N; -.
PDBsum; 3E6O; -.
PDBsum; 3E6T; -.
PDBsum; 3E7I; -.
PDBsum; 3E7M; -.
PDBsum; 3E7T; -.
PDBsum; 3EAI; -.
PDBsum; 3EBD; -.
PDBsum; 3EBF; -.
PDBsum; 3GOF; -.
PDBsum; 3NOD; -.
PDBsum; 3NQS; -.
PDBsum; 3NW2; -.
PDBsum; 4JS9; -.
PDBsum; 4UX6; -.
ProteinModelPortal; P29477; -.
SMR; P29477; -.
BioGrid; 201806; 6.
DIP; DIP-31080N; -.
IntAct; P29477; 2.
MINT; MINT-202500; -.
STRING; 10090.ENSMUSP00000018610; -.
BindingDB; P29477; -.
ChEMBL; CHEMBL3464; -.
iPTMnet; P29477; -.
PhosphoSitePlus; P29477; -.
SwissPalm; P29477; -.
MaxQB; P29477; -.
PaxDb; P29477; -.
PRIDE; P29477; -.
Ensembl; ENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826.
GeneID; 18126; -.
KEGG; mmu:18126; -.
UCSC; uc007kkc.1; mouse.
CTD; 4843; -.
MGI; MGI:97361; Nos2.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
eggNOG; COG4362; LUCA.
GeneTree; ENSGT00840000129757; -.
HOGENOM; HOG000220884; -.
HOVERGEN; HBG000159; -.
InParanoid; P29477; -.
KO; K13241; -.
OMA; TNSPTFL; -.
OrthoDB; EOG091G10Z0; -.
PhylomeDB; P29477; -.
TreeFam; TF324410; -.
BRENDA; 1.14.13.39; 3474.
Reactome; R-MMU-1222556; ROS, RNS production in phagocytes.
Reactome; R-MMU-392154; Nitric oxide stimulates guanylate cyclase.
EvolutionaryTrace; P29477; -.
PRO; PR:P29477; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020826; -.
CleanEx; MM_NOS2; -.
ExpressionAtlas; P29477; baseline and differential.
Genevisible; P29477; MM.
GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005622; C:intracellular; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0034618; F:arginine binding; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; TAS:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:BHF-UCL.
GO; GO:0010181; F:FMN binding; IDA:BHF-UCL.
GO; GO:0020037; F:heme binding; IDA:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0034617; F:tetrahydrobiopterin binding; IDA:BHF-UCL.
GO; GO:0006527; P:arginine catabolic process; IDA:BHF-UCL.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
GO; GO:0035690; P:cellular response to drug; IDA:MGI.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0072604; P:interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0072606; P:interleukin-8 secretion; ISS: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; IDA:BHF-UCL.
GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA: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; ISO:MGI.
GO; GO:0032310; P:prostaglandin secretion; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:1900015; P:regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IDA:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
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_sf.
InterPro; IPR012144; NOS_euk.
InterPro; IPR004030; NOS_N.
InterPro; IPR036119; NOS_N_sf.
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; Calmodulin-binding; Complete proteome;
Direct protein sequencing; FAD; Flavoprotein; FMN; Heme; Iron;
Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Polymorphism;
Reference proteome; Zinc.
CHAIN 1 1144 Nitric oxide synthase, inducible.
/FTId=PRO_0000170934.
DOMAIN 533 671 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 724 964 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 617 648 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 761 772 FAD. {ECO:0000250}.
NP_BIND 897 907 FAD. {ECO:0000250}.
NP_BIND 972 990 NADP. {ECO:0000250}.
NP_BIND 1070 1085 NADP. {ECO:0000250}.
REGION 503 523 Calmodulin-binding. {ECO:0000255}.
METAL 104 104 Zinc.
METAL 109 109 Zinc.
METAL 194 194 Iron (heme axial ligand).
MOD_RES 569 569 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q06518}.
VARIANT 211 211 C -> R (in strain: NOD/LtJ).
{ECO:0000269|PubMed:10438970}.
VARIANT 967 967 P -> L (in strain: SJL/J).
{ECO:0000269|PubMed:10438970}.
VARIANT 968 968 S -> F (in strain: BALB/CBYJ).
{ECO:0000269|PubMed:10438970}.
CONFLICT 19 19 K -> T (in Ref. 4; AAC52356).
{ECO:0000305}.
CONFLICT 72 72 T -> TP (in Ref. 7; AAM11887 and 9;
AAH62378). {ECO:0000305}.
CONFLICT 191 191 A -> V (in Ref. 2; M92649).
{ECO:0000305}.
CONFLICT 245 245 S -> T (in Ref. 7; AAM11887 and 9;
AAH62378). {ECO:0000305}.
CONFLICT 844 844 A -> G (in Ref. 2; M92649).
{ECO:0000305}.
CONFLICT 1075 1075 I -> V (in Ref. 9; AAH62378).
{ECO:0000305}.
STRAND 79 83 {ECO:0000244|PDB:3E7M}.
TURN 84 86 {ECO:0000244|PDB:3E7M}.
STRAND 89 92 {ECO:0000244|PDB:3E7M}.
HELIX 94 97 {ECO:0000244|PDB:3E7M}.
STRAND 103 107 {ECO:0000244|PDB:1QOM}.
HELIX 117 119 {ECO:0000244|PDB:3E7M}.
HELIX 130 146 {ECO:0000244|PDB:2ORT}.
TURN 147 150 {ECO:0000244|PDB:2ORT}.
HELIX 153 170 {ECO:0000244|PDB:2ORT}.
HELIX 177 189 {ECO:0000244|PDB:2ORT}.
HELIX 195 199 {ECO:0000244|PDB:2ORT}.
STRAND 204 207 {ECO:0000244|PDB:2ORT}.
HELIX 208 210 {ECO:0000244|PDB:2BHJ}.
HELIX 214 229 {ECO:0000244|PDB:2ORT}.
HELIX 230 232 {ECO:0000244|PDB:2ORT}.
STRAND 237 240 {ECO:0000244|PDB:2ORT}.
STRAND 245 249 {ECO:0000244|PDB:2ORT}.
STRAND 255 259 {ECO:0000244|PDB:2ORT}.
STRAND 263 265 {ECO:0000244|PDB:2ORP}.
STRAND 267 269 {ECO:0000244|PDB:2BHJ}.
STRAND 271 273 {ECO:0000244|PDB:2ORP}.
HELIX 275 277 {ECO:0000244|PDB:2ORT}.
HELIX 278 286 {ECO:0000244|PDB:2ORT}.
STRAND 294 296 {ECO:0000244|PDB:1DF1}.
STRAND 301 304 {ECO:0000244|PDB:2ORT}.
STRAND 311 313 {ECO:0000244|PDB:2ORT}.
HELIX 317 319 {ECO:0000244|PDB:2ORT}.
STRAND 322 324 {ECO:0000244|PDB:2ORT}.
HELIX 332 334 {ECO:0000244|PDB:2ORO}.
TURN 335 337 {ECO:0000244|PDB:2ORO}.
STRAND 339 342 {ECO:0000244|PDB:2ORT}.
STRAND 350 353 {ECO:0000244|PDB:2ORT}.
STRAND 356 359 {ECO:0000244|PDB:2ORT}.
HELIX 369 373 {ECO:0000244|PDB:3E7M}.
HELIX 375 378 {ECO:0000244|PDB:3E7M}.
TURN 380 383 {ECO:0000244|PDB:3E7M}.
HELIX 386 392 {ECO:0000244|PDB:3E7M}.
HELIX 400 402 {ECO:0000244|PDB:3E7M}.
HELIX 415 422 {ECO:0000244|PDB:2ORT}.
HELIX 430 442 {ECO:0000244|PDB:2ORT}.
HELIX 455 458 {ECO:0000244|PDB:3E7M}.
STRAND 461 463 {ECO:0000244|PDB:3E7M}.
HELIX 464 466 {ECO:0000244|PDB:3E7M}.
HELIX 468 471 {ECO:0000244|PDB:3E7M}.
STRAND 480 485 {ECO:0000244|PDB:2ORT}.
HELIX 489 492 {ECO:0000244|PDB:2ORT}.
HELIX 509 517 {ECO:0000244|PDB:3GOF}.
SEQUENCE 1144 AA; 130575 MW; 0735BE676113457F CRC64;
MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG SPQLLTGTAQ
NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS DFTCKSKSCL GSIMNPKSLT
RGPRDKPTPL EELLPHAIEF INQYYGSFKE AKIEEHLARL EAVTKEIETT GTYQLTLDEL
IFATKMAWRN APRCIGRIQW SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV
FPQRSDGKHD FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP
LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML LEVGGLEFPA
CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL ASLWKDRAVT EINVAVLHSF
QKQNVTIMDH HTASESFMKH MQNEYRARGG CPADWIWLVP PVSGSITPVF HQEMLNYVLS
PFYYYQIEPW KTHIWQNEKL RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE
TGKSEALARD LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK
KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT GEGDELSGQE
DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP QQYRLIQSPE PLDLNRALSS
IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ LTFEGSRGPS YLPGEHLGIF PGNQTALVQG
ILERVVDCPT PHQTVCLEVL DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL
ARFATDETDR QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR
YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP VPCFVRSVSG
FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK GGRMSLVFGC RHPEEDHLYQ
EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV QDILQKQLAN EVLSVLHGEQ GHLYICGDVR
MARDVATTLK KLVATKLNLS EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK
ATRL


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