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P29477

- NOS2_MOUSE

UniProt

P29477 - NOS2_MOUSE

Protein

Nitric oxide synthase, inducible

Gene

Nos2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    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 COX2.1 Publication

    Catalytic activityi

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

    Cofactori

    Heme group.
    Binds 1 FAD.
    Binds 1 FMN.
    Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

    Enzyme regulationi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi104 – 1041Zinc
    Metal bindingi109 – 1091Zinc
    Metal bindingi194 – 1941Iron (heme axial ligand)

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi617 – 64832FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi761 – 77212FADBy similarityAdd
    BLAST
    Nucleotide bindingi897 – 90711FADBy similarityAdd
    BLAST
    Nucleotide bindingi972 – 99019NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1070 – 108516NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. arginine binding Source: BHF-UCL
    2. calmodulin binding Source: UniProtKB
    3. flavin adenine dinucleotide binding Source: BHF-UCL
    4. FMN binding Source: BHF-UCL
    5. heme binding Source: BHF-UCL
    6. iron ion binding Source: InterPro
    7. NADP binding Source: InterPro
    8. NADPH-hemoprotein reductase activity Source: RefGenome
    9. nitric-oxide synthase activity Source: BHF-UCL
    10. protein binding Source: UniProtKB
    11. protein homodimerization activity Source: BHF-UCL
    12. tetrahydrobiopterin binding Source: BHF-UCL

    GO - Biological processi

    1. arginine catabolic process Source: BHF-UCL
    2. cellular response to interferon-gamma Source: MGI
    3. cellular response to lipopolysaccharide Source: MGI
    4. circadian rhythm Source: UniProtKB
    5. defense response to bacterium Source: MGI
    6. inflammatory response Source: UniProtKB
    7. negative regulation of blood pressure Source: RefGenome
    8. negative regulation of gene expression Source: UniProtKB
    9. negative regulation of protein catabolic process Source: BHF-UCL
    10. nitric oxide biosynthetic process Source: BHF-UCL
    11. nitric oxide mediated signal transduction Source: RefGenome
    12. peptidyl-cysteine S-nitrosylation Source: UniProtKB
    13. positive regulation of guanylate cyclase activity Source: RefGenome
    14. positive regulation of killing of cells of other organism Source: Ensembl
    15. positive regulation of vasodilation Source: RefGenome
    16. regulation of cell proliferation Source: MGI
    17. regulation of insulin secretion Source: Ensembl
    18. response to hypoxia Source: MGI
    19. response to lipopolysaccharide Source: UniProtKB
    20. superoxide metabolic process Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Nos2
    Synonyms:Inosl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:97361. Nos2.

    Subcellular locationi

    GO - Cellular componenti

    1. cortical cytoskeleton Source: MGI
    2. cytoplasm Source: MGI
    3. cytosol Source: UniProtKB
    4. perinuclear region of cytoplasm Source: MGI
    5. peroxisome Source: Ensembl

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11441144Nitric oxide synthase, induciblePRO_0000170934Add
    BLAST

    Proteomic databases

    MaxQBiP29477.
    PRIDEiP29477.

    PTM databases

    PhosphoSiteiP29477.

    Expressioni

    Tissue specificityi

    Macrophages.

    Inductioni

    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.1 Publication

    Gene expression databases

    BgeeiP29477.
    CleanExiMM_NOS2.
    GenevestigatoriP29477.

    Interactioni

    Subunit structurei

    Homodimer. Binds SLC9A3R1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201806. 6 interactions.
    DIPiDIP-31080N.
    IntActiP29477. 1 interaction.
    MINTiMINT-202500.

    Structurei

    Secondary structure

    1
    1144
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi79 – 835
    Turni84 – 863
    Beta strandi89 – 924
    Helixi94 – 974
    Beta strandi103 – 1075
    Helixi117 – 1193
    Helixi130 – 14617
    Turni147 – 1504
    Helixi153 – 17018
    Helixi177 – 18913
    Helixi195 – 1995
    Beta strandi204 – 2074
    Helixi208 – 2103
    Helixi214 – 22916
    Helixi230 – 2323
    Beta strandi237 – 2404
    Beta strandi245 – 2495
    Beta strandi255 – 2595
    Beta strandi263 – 2653
    Beta strandi267 – 2693
    Beta strandi271 – 2733
    Helixi275 – 2773
    Helixi278 – 2869
    Beta strandi294 – 2963
    Beta strandi301 – 3044
    Beta strandi311 – 3133
    Helixi317 – 3193
    Beta strandi322 – 3243
    Helixi332 – 3343
    Turni335 – 3373
    Beta strandi339 – 3424
    Beta strandi350 – 3534
    Beta strandi356 – 3594
    Helixi369 – 3735
    Helixi375 – 3784
    Turni380 – 3834
    Helixi386 – 3927
    Helixi400 – 4023
    Helixi415 – 4228
    Helixi430 – 44213
    Helixi455 – 4584
    Beta strandi461 – 4633
    Helixi464 – 4663
    Helixi468 – 4714
    Beta strandi480 – 4856
    Helixi489 – 4924
    Helixi509 – 5179

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    4JS9X-ray2.78A/B66-496[»]
    ProteinModelPortaliP29477.
    SMRiP29477. Positions 77-497, 505-1126.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29477.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini533 – 671139Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini724 – 964241FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni503 – 52321Calmodulin-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the NOS family.Curated
    Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation
    Contains 1 flavodoxin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4362.
    GeneTreeiENSGT00620000087711.
    HOGENOMiHOG000220884.
    HOVERGENiHBG000159.
    InParanoidiP29477.
    KOiK13241.
    OMAiKFTNSPT.
    OrthoDBiEOG79SDW7.
    PhylomeDBiP29477.
    TreeFamiTF324410.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    3.90.340.10. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR012144. NOS_euk.
    IPR004030. NOS_N.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF02898. NO_synthase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000333. NOS. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF56512. SSF56512. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    PS60001. NOS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29477-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACPWKFLFK VKSYQSDLKE EKDINNNVKK TPCAVLSPTI QDDPKSHQNG     50
    SPQLLTGTAQ NVPESLDKLH VTSTRPQYVR IKNWGSGEIL HDTLHHKATS 100
    DFTCKSKSCL GSIMNPKSLT RGPRDKPTPL EELLPHAIEF INQYYGSFKE 150
    AKIEEHLARL EAVTKEIETT GTYQLTLDEL IFATKMAWRN APRCIGRIQW 200
    SNLQVFDARN CSTAQEMFQH ICRHILYATN NGNIRSAITV FPQRSDGKHD 250
    FRLWNSQLIR YAGYQMPDGT IRGDAATLEF TQLCIDLGWK PRYGRFDVLP 300
    LVLQADGQDP EVFEIPPDLV LEVTMEHPKY EWFQELGLKW YALPAVANML 350
    LEVGGLEFPA CPFNGWYMGT EIGVRDFCDT QRYNILEEVG RRMGLETHTL 400
    ASLWKDRAVT EINVAVLHSF QKQNVTIMDH HTASESFMKH MQNEYRARGG 450
    CPADWIWLVP PVSGSITPVF HQEMLNYVLS PFYYYQIEPW KTHIWQNEKL 500
    RPRRREIRFR VLVKVVFFAS MLMRKVMASR VRATVLFATE TGKSEALARD 550
    LATLFSYAFN TKVVCMDQYK ASTLEEEQLL LVVTSTFGNG DCPSNGQTLK 600
    KSLFMLRELN HTFRYAVFGL GSSMYPQFCA FAHDIDQKLS HLGASQLAPT 650
    GEGDELSGQE DAFRSWAVQT FRAACETFDV RSKHHIQIPK RFTSNATWEP 700
    QQYRLIQSPE PLDLNRALSS IHAKNVFTMR LKSQQNLQSE KSSRTTLLVQ 750
    LTFEGSRGPS YLPGEHLGIF PGNQTALVQG ILERVVDCPT PHQTVCLEVL 800
    DESGSYWVKD KRLPPCSLSQ ALTYFLDITT PPTQLQLHKL ARFATDETDR 850
    QRLEALCQPS EYNDWKFSNN PTFLEVLEEF PSLHVPAAFL LSQLPILKPR 900
    YYSISSSQDH TPSEVHLTVA VVTYRTRDGQ GPLHHGVCST WIRNLKPQDP 950
    VPCFVRSVSG FQLPEDPSQP CILIGPGTGI APFRSFWQQR LHDSQHKGLK 1000
    GGRMSLVFGC RHPEEDHLYQ EEMQEMVRKR VLFQVHTGYS RLPGKPKVYV 1050
    QDILQKQLAN EVLSVLHGEQ GHLYICGDVR MARDVATTLK KLVATKLNLS 1100
    EEQVEDYFFQ LKSQKRYHED IFGAVFSYGA KKGSALEEPK ATRL 1144
    Length:1,144
    Mass (Da):130,575
    Last modified:April 1, 1993 - v1
    Checksum:i0735BE676113457F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 191K → T in AAC52356. (PubMed:7503239)Curated
    Sequence conflicti72 – 721T → TP in AAM11887. 1 PublicationCurated
    Sequence conflicti72 – 721T → TP in AAH62378. (PubMed:15489334)Curated
    Sequence conflicti191 – 1911A → V in M92649. (PubMed:1379716)Curated
    Sequence conflicti245 – 2451S → T in AAM11887. 1 PublicationCurated
    Sequence conflicti245 – 2451S → T in AAH62378. (PubMed:15489334)Curated
    Sequence conflicti844 – 8441A → G in M92649. (PubMed:1379716)Curated
    Sequence conflicti1075 – 10751I → V in AAH62378. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti211 – 2111C → R in strain: NOD/LtJ. 1 Publication
    Natural varianti967 – 9671P → L in strain: SJL/J. 1 Publication
    Natural varianti968 – 9681S → F in strain: BALB/CBYJ. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS25115.1.
    PIRiA43271.
    RefSeqiNP_035057.1. NM_010927.3.
    UniGeneiMm.2893.

    Genome annotation databases

    EnsembliENSMUST00000018610; ENSMUSP00000018610; ENSMUSG00000020826.
    GeneIDi18126.
    KEGGimmu:18126.
    UCSCiuc007kkc.1. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS25115.1.
    PIRi A43271.
    RefSeqi NP_035057.1. NM_010927.3.
    UniGenei Mm.2893.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DD7 X-ray 2.25 A 114-498 [» ]
    1DF1 X-ray 2.35 A/B 77-499 [» ]
    1DWV X-ray 2.35 A/B 77-496 [» ]
    1DWW X-ray 2.35 A/B 77-496 [» ]
    1DWX X-ray 2.60 A/B 77-496 [» ]
    1JWJ X-ray 2.60 A/B 66-498 [» ]
    1JWK X-ray 2.30 A/B 66-498 [» ]
    1M8D X-ray 2.35 A/B 65-498 [» ]
    1M8E X-ray 2.90 A/B 65-498 [» ]
    1M8H X-ray 2.85 A/B 65-498 [» ]
    1M8I X-ray 2.70 A/B 65-498 [» ]
    1M9T X-ray 2.40 A/B 65-498 [» ]
    1N2N X-ray 2.40 A/B 77-495 [» ]
    1NOC X-ray 2.60 A 115-498 [» ]
    1NOD X-ray 2.60 A/B 77-499 [» ]
    1NOS X-ray 2.10 A 115-498 [» ]
    1QOM X-ray 2.70 A/B 65-498 [» ]
    1QW4 X-ray 2.40 A/B 77-495 [» ]
    1QW5 X-ray 2.70 A/B 77-495 [» ]
    1R35 X-ray 2.30 A/B 66-498 [» ]
    1VAF X-ray 2.90 A/B 77-495 [» ]
    2BHJ X-ray 3.20 A 77-498 [» ]
    2NOD X-ray 2.60 A/B 77-499 [» ]
    2NOS X-ray 2.30 A 115-498 [» ]
    2ORO X-ray 2.00 A 114-498 [» ]
    2ORP X-ray 1.97 A 114-498 [» ]
    2ORQ X-ray 2.10 A 114-498 [» ]
    2ORR X-ray 2.00 A 114-498 [» ]
    2ORS X-ray 2.00 A 114-498 [» ]
    2ORT X-ray 1.87 A 114-498 [» ]
    2Y37 X-ray 2.60 A/B 66-498 [» ]
    3DWJ X-ray 2.75 A/B 66-496 [» ]
    3E65 X-ray 2.05 A/B 66-498 [» ]
    3E67 X-ray 2.60 A/B 66-498 [» ]
    3E68 X-ray 2.20 A/B 66-498 [» ]
    3E6L X-ray 2.30 A/B 66-498 [» ]
    3E6N X-ray 2.40 A/B 66-498 [» ]
    3E6O X-ray 2.60 A/B 66-498 [» ]
    3E6T X-ray 2.50 A/B 66-498 [» ]
    3E7I X-ray 2.90 A/B 66-498 [» ]
    3E7M X-ray 2.00 A/B 66-498 [» ]
    3E7T X-ray 2.60 A/B 66-498 [» ]
    3EAI X-ray 2.20 A/B 66-498 [» ]
    3EBD X-ray 2.40 A/B 66-498 [» ]
    3EBF X-ray 2.29 A/B 66-498 [» ]
    3GOF X-ray 1.45 C/D 503-518 [» ]
    3NOD X-ray 2.70 A/B 77-499 [» ]
    3NQS X-ray 2.20 A/B 66-498 [» ]
    3NW2 X-ray 2.80 A/B 77-499 [» ]
    4JS9 X-ray 2.78 A/B 66-496 [» ]
    ProteinModelPortali P29477.
    SMRi P29477. Positions 77-497, 505-1126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201806. 6 interactions.
    DIPi DIP-31080N.
    IntActi P29477. 1 interaction.
    MINTi MINT-202500.

    Chemistry

    BindingDBi P29477.
    ChEMBLi CHEMBL3464.

    PTM databases

    PhosphoSitei P29477.

    Proteomic databases

    MaxQBi P29477.
    PRIDEi P29477.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018610 ; ENSMUSP00000018610 ; ENSMUSG00000020826 .
    GeneIDi 18126.
    KEGGi mmu:18126.
    UCSCi uc007kkc.1. mouse.

    Organism-specific databases

    CTDi 4843.
    MGIi MGI:97361. Nos2.

    Phylogenomic databases

    eggNOGi COG4362.
    GeneTreei ENSGT00620000087711.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.
    InParanoidi P29477.
    KOi K13241.
    OMAi KFTNSPT.
    OrthoDBi EOG79SDW7.
    PhylomeDBi P29477.
    TreeFami TF324410.

    Enzyme and pathway databases

    Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).

    Miscellaneous databases

    EvolutionaryTracei P29477.
    NextBioi 293348.
    PROi P29477.
    SOURCEi Search...

    Gene expression databases

    Bgeei P29477.
    CleanExi MM_NOS2.
    Genevestigatori P29477.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    3.90.340.10. 1 hit.
    InterProi IPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001094. Flavdoxin.
    IPR008254. Flavodoxin/NO_synth.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR012144. NOS_euk.
    IPR004030. NOS_N.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00667. FAD_binding_1. 1 hit.
    PF00258. Flavodoxin_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    PF02898. NO_synthase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000333. NOS. 1 hit.
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SUPFAMi SSF52218. SSF52218. 1 hit.
    SSF56512. SSF56512. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    PS50902. FLAVODOXIN_LIKE. 1 hit.
    PS60001. NOS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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 circadian deadenylase Nocturnin is necessary for stabilization of the iNOS mRNA in mice."
      Niu S., Shingle D.L., Garbarino-Pico E., Kojima S., Gilbert M., Green C.B.
      PLoS ONE 6:E26954-E26954(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. "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.

    Entry informationi

    Entry nameiNOS2_MOUSE
    AccessioniPrimary (citable) accession number: P29477
    Secondary accession number(s): O70515
    , O70516, Q5SXT3, Q6P6A0, Q8R410
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 161 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3