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P29477 (NOS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nitric oxide synthase, inducible

EC=1.14.13.39
Alternative name(s):
Inducible NO synthase
Short name=Inducible NOS
Short name=iNOS
Macrophage NOS
Short name=MAC-NOS
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2
Gene names
Name:Nos2
Synonyms:Inosl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1144 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2. Ref.12

Catalytic activity

2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

Cofactor

Heme group.

Binds 1 FAD.

Binds 1 FMN.

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 structure

Homodimer. Binds SLC9A3R1 By similarity.

Tissue specificity

Macrophages.

Induction

By treatment with endotoxins or cytokines.

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   LigandCalmodulin-binding
FAD
Flavoprotein
FMN
Heme
Iron
Metal-binding
NADP
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process

Inferred from direct assay PubMed 1383204. Source: BHF-UCL

cellular response to interferon-gamma

Inferred from direct assay PubMed 18025219. Source: MGI

cellular response to lipopolysaccharide

Inferred from direct assay PubMed 18025219PubMed 18791161. Source: MGI

defense response to bacterium

Inferred from mutant phenotype PubMed 12933833. Source: MGI

inflammatory response

Traceable author statement PubMed 12855682. Source: UniProtKB

negative regulation of blood pressure

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of gene expression

Inferred from genetic interaction PubMed 12085352. Source: UniProtKB

negative regulation of protein catabolic process

Inferred from direct assay PubMed 18003616. Source: BHF-UCL

nitric oxide biosynthetic process

Inferred from direct assay PubMed 1383204PubMed 9271491. Source: BHF-UCL

nitric oxide mediated signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

peptidyl-cysteine S-nitrosylation

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of guanylate cyclase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of killing of cells of other organism

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cell proliferation

Inferred from genetic interaction PubMed 11606502PubMed 11731407. Source: MGI

regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from direct assay PubMed 12960352. Source: MGI

superoxide metabolic process

Inferred from mutant phenotype PubMed 12933833. Source: MGI

   Cellular_componentcortical cytoskeleton

Inferred from direct assay PubMed 12960352. Source: MGI

cytoplasm

Inferred from direct assay PubMed 11732991PubMed 12960352. Source: MGI

cytosol

Traceable author statement PubMed 12855682. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12960352. Source: MGI

peroxisome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionFMN binding

Inferred from direct assay PubMed 1383204. Source: BHF-UCL

NADP binding

Inferred from electronic annotation. Source: InterPro

NADPH-hemoprotein reductase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

arginine binding

Inferred from direct assay PubMed 9271491. Source: BHF-UCL

calmodulin binding

Traceable author statement PubMed 12855682. Source: UniProtKB

flavin adenine dinucleotide binding

Inferred from direct assay PubMed 1383204. Source: BHF-UCL

heme binding

Inferred from direct assay PubMed 1383204PubMed 9271491. Source: BHF-UCL

iron ion binding

Inferred from electronic annotation. Source: InterPro

nitric-oxide synthase activity

Inferred from direct assay PubMed 1383204PubMed 9271491. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 9271491. Source: BHF-UCL

tetrahydrobiopterin binding

Inferred from direct assay PubMed 9271491. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11441144Nitric oxide synthase, inducible
PRO_0000170934

Regions

Domain533 – 671139Flavodoxin-like
Domain724 – 964241FAD-binding FR-type
Nucleotide binding617 – 64832FMN By similarity
Nucleotide binding761 – 77212FAD By similarity
Nucleotide binding897 – 90711FAD By similarity
Nucleotide binding972 – 99019NADP By similarity
Nucleotide binding1070 – 108516NADP By similarity
Region503 – 52321Calmodulin-binding Potential

Sites

Metal binding1041Zinc
Metal binding1091Zinc
Metal binding1941Iron (heme axial ligand)

Natural variations

Natural variant2111C → R in strain: NOD/LtJ. Ref.5
Natural variant9671P → L in strain: SJL/J. Ref.5
Natural variant9681S → F in strain: BALB/CBYJ. Ref.5

Experimental info

Sequence conflict191K → T in AAC52356. Ref.4
Sequence conflict721T → TP in AAM11887. Ref.7
Sequence conflict721T → TP in AAH62378. Ref.9
Sequence conflict1911A → V in M92649. Ref.2
Sequence conflict2451S → T in AAM11887. Ref.7
Sequence conflict2451S → T in AAH62378. Ref.9
Sequence conflict8441A → G in M92649. Ref.2
Sequence conflict10751I → V in AAH62378. Ref.9

Secondary structure

........................................................................................ 1144
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29477 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 0735BE676113457F

FASTA1,144130,575
        10         20         30         40         50         60 
MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG SPQLLTGTAQ 

        70         80         90        100        110        120 
NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS DFTCKSKSCL GSIMNPKSLT 

       130        140        150        160        170        180 
RGPRDKPTPL EELLPHAIEF INQYYGSFKE AKIEEHLARL EAVTKEIETT GTYQLTLDEL 

       190        200        210        220        230        240 
IFATKMAWRN APRCIGRIQW SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV 

       250        260        270        280        290        300 
FPQRSDGKHD FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP 

       310        320        330        340        350        360 
LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML LEVGGLEFPA 

       370        380        390        400        410        420 
CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL ASLWKDRAVT EINVAVLHSF 

       430        440        450        460        470        480 
QKQNVTIMDH HTASESFMKH MQNEYRARGG CPADWIWLVP PVSGSITPVF HQEMLNYVLS 

       490        500        510        520        530        540 
PFYYYQIEPW KTHIWQNEKL RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE 

       550        560        570        580        590        600 
TGKSEALARD LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK 

       610        620        630        640        650        660 
KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT GEGDELSGQE 

       670        680        690        700        710        720 
DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP QQYRLIQSPE PLDLNRALSS 

       730        740        750        760        770        780 
IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ LTFEGSRGPS YLPGEHLGIF PGNQTALVQG 

       790        800        810        820        830        840 
ILERVVDCPT PHQTVCLEVL DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL 

       850        860        870        880        890        900 
ARFATDETDR QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR 

       910        920        930        940        950        960 
YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP VPCFVRSVSG 

       970        980        990       1000       1010       1020 
FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK GGRMSLVFGC RHPEEDHLYQ 

      1030       1040       1050       1060       1070       1080 
EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV QDILQKQLAN EVLSVLHGEQ GHLYICGDVR 

      1090       1100       1110       1120       1130       1140 
MARDVATTLK KLVATKLNLS EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK 


ATRL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of inducible nitric oxide synthase from mouse macrophages."
Xie Q.-W., Cho H.J., Calaycay J., Mumford R.A., Swiderek K.M., Lee T.D., Ding A., Troso T., Nathan C.
Science 256:225-228(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloned and expressed macrophage nitric oxide synthase contrasts with the brain enzyme."
Lowenstein C.J., Glatt C.S., Bredt D.S., Snyder S.H.
Proc. Natl. Acad. Sci. U.S.A. 89:6711-6715(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Molecular cloning and functional expression of an inducible nitric oxide synthase from a murine macrophage cell line."
Lyons C.R., Orloff G.J., Cunningham J.M.
J. Biol. Chem. 267:6370-6374(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Role of NF-kappa B in the regulation of inducible nitric oxide synthase in an MTAL cell line."
Kone B.C., Schwoebel J., Turner P., Mohaupt M.G., Cangro C.B.
Am. J. Physiol. 269:F718-F729(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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."
Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W., Blankenhorn E.P.
J. Immunol. 163:2262-2266(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-211; LEU-967 AND PHE-968.
Strain: B10.S/J, BALB/cByJ, DBA/2J, NOD/LtJ and SJL/J.
Tissue: Spleen.
[6]"Genomic structure of the murine inducible nitric oxide synthase (i-NOS) gene."
Coge F., Levacher B., Rique H., Leopold O., Boutin J.A., Galizzi J.-P.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CD-1.
[7]"Mouse inducible nitric oxide synthase mRNA."
Hagiwara K., Endo Y., Xin H., Takahashi M., Huqun X., Nukiwa T.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
[8]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NMRI.
Tissue: Mammary tumor.
[10]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 733-744, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[11]"The mode of action of aspirin-like drugs: effect on inducible nitric oxide synthase."
Amin A.R., Vyas P., Attur M., Leszczynska-Piziak J., Patel I.R., Weissmann G., Abramson S.B.
Proc. Natl. Acad. Sci. U.S.A. 92:7926-7930(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: EFFECT OF ASPIRIN.
Tissue: Macrophage.
[12]"Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2."
Kim S.F., Huri D.A., Snyder S.H.
Science 310:1966-1970(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NITROSYLASE.
[13]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"The structure of nitric oxide synthase oxygenase domain and inhibitor complexes."
Crane B.R., Arvai A.S., Gachhui R., Wu C., Ghosh D.K., Getzoff E.D., Stuehr D.J., Tainer J.A.
Science 278:425-431(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 116-496.
[15]"Structure of nitric oxide synthase oxygenase dimer with pterin and substrate."
Crane B.R., Arvai A.S., Ghosh D.K., Wu C., Getzoff E.D., Stuehr D.J., Tainer J.A.
Science 279:2121-2126(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 77-496.
[16]"Inducible nitric oxide synthase: role of the N-terminal beta-hairpin hook and pterin-binding segment in dimerization and tetrahydrobiopterin interaction."
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.
EMBO J. 18:6260-6270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
[17]"N-terminal domain swapping and metal ion binding in nitric oxide synthase dimerization."
Crane B.R., Rosenfeld R.J., Arvai A.S., Ghosh D.K., Ghosh S., Tainer J.A., Stuehr D.J., Getzoff E.D.
EMBO J. 18:6271-6281(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-499.
[18]"Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins."
Crane B.R., Arvai A.S., Ghosh S., Getzoff E.D., Stuehr D.J., Tainer J.A.
Biochemistry 39:4608-4621(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
[19]"Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase oxygenase dimer and implicated roles of Trp457."
Aoyagi M., Arvai A.S., Ghosh S., Stuehr D.J., Tainer J.A., Getzoff E.D.
Biochemistry 40:12826-12832(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF TRP-457 MUTANTS.
[20]"Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency."
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.
Biochemistry 41:13915-13925(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 77-496.
[21]"Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase -- structural models of the short-lived oxygen complexes."
Fedorov R., Ghosh D.K., Schlichting I.
Arch. Biochem. Biophys. 409:25-31(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-495.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M87039 mRNA. Translation: AAA39315.1.
M92649 mRNA. No translation available.
M84373 mRNA. Translation: AAA39834.1.
U43428 mRNA. Translation: AAC52356.1.
AF065919 mRNA. Translation: AAC17914.1.
AF065920 mRNA. Translation: AAC17915.1.
AF065921 mRNA. Translation: AAC17916.2.
AF065922 mRNA. Translation: AAC17917.2.
AF065923 mRNA. Translation: AAC17918.2.
AF427516 Genomic DNA. Translation: AAL24076.1.
AY090567 mRNA. Translation: AAM11887.1.
AL592185 Genomic DNA. Translation: CAI25275.1.
BC062378 mRNA. Translation: AAH62378.1.
PIRA43271.
RefSeqNP_035057.1. NM_010927.3.
UniGeneMm.2893.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DD7X-ray2.25A114-498[»]
1DF1X-ray2.35A/B77-499[»]
1DWVX-ray2.35A/B77-496[»]
1DWWX-ray2.35A/B77-496[»]
1DWXX-ray2.60A/B77-496[»]
1JWJX-ray2.60A/B66-498[»]
1JWKX-ray2.30A/B66-498[»]
1M8DX-ray2.35A/B65-498[»]
1M8EX-ray2.90A/B65-498[»]
1M8HX-ray2.85A/B65-498[»]
1M8IX-ray2.70A/B65-498[»]
1M9TX-ray2.40A/B65-498[»]
1N2NX-ray2.40A/B77-495[»]
1NOCX-ray2.60A115-498[»]
1NODX-ray2.60A/B77-499[»]
1NOSX-ray2.10A115-498[»]
1QOMX-ray2.70A/B65-498[»]
1QW4X-ray2.40A/B77-495[»]
1QW5X-ray2.70A/B77-495[»]
1R35X-ray2.30A/B66-498[»]
1VAFX-ray2.90A/B77-495[»]
2BHJX-ray3.20A77-498[»]
2NODX-ray2.60A/B77-499[»]
2NOSX-ray2.30A115-498[»]
2OROX-ray2.00A114-498[»]
2ORPX-ray1.97A114-498[»]
2ORQX-ray2.10A114-498[»]
2ORRX-ray2.00A114-498[»]
2ORSX-ray2.00A114-498[»]
2ORTX-ray1.87A114-498[»]
2Y37X-ray2.60A/B66-498[»]
3DWJX-ray2.75A/B66-496[»]
3E65X-ray2.05A/B66-498[»]
3E67X-ray2.60A/B66-498[»]
3E68X-ray2.20A/B66-498[»]
3E6LX-ray2.30A/B66-498[»]
3E6NX-ray2.40A/B66-498[»]
3E6OX-ray2.60A/B66-498[»]
3E6TX-ray2.50A/B66-498[»]
3E7IX-ray2.90A/B66-498[»]
3E7MX-ray2.00A/B66-498[»]
3E7TX-ray2.60A/B66-498[»]
3EAIX-ray2.20A/B66-498[»]
3EBDX-ray2.40A/B66-498[»]
3EBFX-ray2.29A/B66-498[»]
3GOFX-ray1.45C/D503-518[»]
3NODX-ray2.70A/B77-499[»]
3NQSX-ray2.20A/B66-498[»]
3NW2X-ray2.80A/B77-499[»]
ProteinModelPortalP29477.
SMRP29477. Positions 77-497, 505-1126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201806. 6 interactions.
DIPDIP-31080N.
IntActP29477. 1 interaction.
MINTMINT-202500.

Chemistry

BindingDBP29477.
ChEMBLCHEMBL3464.

PTM databases

PhosphoSiteP29477.

Proteomic databases

PRIDEP29477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826.
GeneID18126.
KEGGmmu:18126.
UCSCuc007kkc.1. mouse.

Organism-specific databases

CTD4843.
MGIMGI:97361. Nos2.

Phylogenomic databases

eggNOGCOG4362.
GeneTreeENSGT00620000087711.
HOGENOMHOG000220884.
HOVERGENHBG000159.
InParanoidP29477.
KOK13241.
OMAKFTNSPT.
OrthoDBEOG79SDW7.
PhylomeDBP29477.
TreeFamTF324410.

Gene expression databases

BgeeP29477.
CleanExMM_NOS2.
GenevestigatorP29477.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
3.90.340.10. 1 hit.
InterProIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR004030. NO_synthase_oxygenase_dom.
IPR012144. NOS_euk.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR19384:SF5. PTHR19384:SF5. 1 hit.
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF02898. NO_synthase. 1 hit.
[Graphical view]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29477.
NextBio293348.
PROP29477.
SOURCESearch...

Entry information

Entry nameNOS2_MOUSE
AccessionPrimary (citable) accession number: P29477
Secondary accession number(s): O70515 expand/collapse secondary AC list , O70516, Q5SXT3, Q6P6A0, Q8R410
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: April 16, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot