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Q06518

- NOS2_RAT

UniProt

Q06518 - NOS2_RAT

Protein

Nitric oxide synthase, inducible

Gene

Nos2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2 By similarity.By similarity

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi107 – 1071ZincBy similarity
    Metal bindingi112 – 1121ZincBy similarity
    Metal bindingi197 – 1971Iron (heme axial ligand)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi620 – 65132FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi764 – 77512FADBy similarityAdd
    BLAST
    Nucleotide bindingi900 – 91011FADBy similarityAdd
    BLAST
    Nucleotide bindingi975 – 99319NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1073 – 108816NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. actin binding Source: RGD
    2. amino acid binding Source: RGD
    3. beta-catenin binding Source: RGD
    4. cadherin binding Source: RGD
    5. cAMP-dependent protein kinase regulator activity Source: RGD
    6. flavin adenine dinucleotide binding Source: RGD
    7. FMN binding Source: RGD
    8. heme binding Source: RGD
    9. Hsp90 protein binding Source: RGD
    10. iron ion binding Source: InterPro
    11. NADP binding Source: RGD
    12. NADPH-hemoprotein reductase activity Source: RefGenome
    13. nitric-oxide synthase activity Source: UniProtKB
    14. nitric-oxide synthase binding Source: RGD
    15. protein homodimerization activity Source: RGD
    16. protein kinase binding Source: RGD

    GO - Biological processi

    1. aging Source: RGD
    2. blood vessel remodeling Source: RGD
    3. cellular response to interleukin-1 Source: RGD
    4. cellular response to lipopolysaccharide Source: RGD
    5. cellular response to lithium ion Source: RGD
    6. cellular response to redox state Source: RGD
    7. cellular response to tumor necrosis factor Source: RGD
    8. cellular response to vitamin D Source: RGD
    9. cGMP-mediated signaling Source: RGD
    10. defense response to bacterium Source: UniProtKB
    11. defense response to Gram-negative bacterium Source: RGD
    12. endothelial cell proliferation Source: RGD
    13. glycoside metabolic process Source: RGD
    14. G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger Source: RGD
    15. inflammatory response Source: RefGenome
    16. intracellular signal transduction Source: RGD
    17. negative regulation of blood pressure Source: RefGenome
    18. nitric oxide biosynthetic process Source: UniProtKB
    19. nitric oxide mediated signal transduction Source: RefGenome
    20. peptidyl-cysteine S-nitrosylation Source: UniProtKB
    21. positive regulation of apoptotic process Source: RGD
    22. positive regulation of guanylate cyclase activity Source: RefGenome
    23. positive regulation of vasodilation Source: RefGenome
    24. regulation of blood pressure Source: RGD
    25. regulation of heart contraction Source: RGD
    26. regulation of protein kinase activity Source: GOC
    27. response to activity Source: RGD
    28. response to dexamethasone Source: RGD
    29. response to estradiol Source: RGD
    30. response to hormone Source: RGD
    31. response to immobilization stress Source: RGD
    32. response to lipopolysaccharide Source: RGD
    33. response to mechanical stimulus Source: RGD
    34. response to tumor necrosis factor Source: RGD
    35. retinoic acid receptor signaling pathway Source: RGD
    36. signal transduction Source: RGD
    37. superoxide metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    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
    NOS type II
    Peptidyl-cysteine S-nitrosylase NOS2
    Gene namesi
    Name:Nos2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3185. Nos2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular space Source: RGD
    4. nucleus Source: BHF-UCL
    5. perinuclear region of cytoplasm Source: RGD
    6. peroxisome Source: UniProtKB
    7. vesicle membrane Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11471147Nitric oxide synthase, induciblePRO_0000170937Add
    BLAST

    Proteomic databases

    PRIDEiQ06518.

    PTM databases

    PhosphoSiteiQ06518.

    Expressioni

    Tissue specificityi

    In normal kidney, expressed primarily in the medullary thick ascending limb, with minor amounts in the medullary collecting duct and vasa recta bundle.

    Inductioni

    By interferon gamma and lipopolysaccharides (LPS).

    Gene expression databases

    GenevestigatoriQ06518.

    Interactioni

    Subunit structurei

    Homodimer. Binds SLC9A3R1 By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-59942N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06518.
    SMRiQ06518. Positions 80-499, 700-1127.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini536 – 674139Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini727 – 967241FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni506 – 52621Calmodulin-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.
    HOVERGENiHBG000159.
    InParanoidiQ06518.
    KOiK13241.
    PhylomeDBiQ06518.

    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.

    Q06518-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACPWKFLFR VKSYQGDLKE EKDINNNVEK TPGAIPSPTT QDDPKSHKHQ     50
    NGFPQFLTGT AQNVPESLDK LHVTPSTRPQ HVRIKNWGNG EIFHDTLHHK 100
    ATSDISCKSK LCMGSIMNSK SLTRGPRDKP TPVEELLPQA IEFINQYYGS 150
    FKEAKIEEHL ARLEAVTKEI ETTGTYQLTL DELIFATKMA WRNAPRCIGR 200
    IQWSNLQVFD ARSCSTASEM FQHICRHILY ATNSGNIRSA ITVFPQRSDG 250
    KHDFRIWNSQ LIRYAGYQMP DGTIRGDPAT LEFTQLCIDL GWKPRYGRFD 300
    VLPLVLQAHG QDPEVFEIPP DLVLEVTMEH PKYEWFQELG LKWYALPAVA 350
    NMLLEVGGLE FPACPFNGWY MGTEIGVRDF CDTQRYNILE EVGRRMGLET 400
    HTLASLWKDR AVTEINAAVL HSFQKQNVTI MDHHTASESF MKHMQNEYRA 450
    RGGCPADWIW LVPPVSGSIT PVFHQEMLNY VLSPFYYYQI EPWKTHIWQD 500
    EKLRPRRREI RFTVLVKAVF FASVLMRKVM ASRVRATVLF ATETGKSEAL 550
    ARDLAALFSY AFNTKVVCME QYKANTLEEE QLLLVVTSTF GNGDCPSNGQ 600
    TLKKSLFMMK ELGHTFRYAV FGLGSSMYPQ FCAFAHDIDQ KLSHLGASQL 650
    APTGEGDELS GQEDAFRSWA VQTFRAACET FDVRSKHCIQ IPKRYTSNAT 700
    WEPEQYKLTQ SPESLDLNKA LSSIHAKNVF TMRLKSLQNL QSEKSSRTTL 750
    LVQLTFEGSR GPSYLPGEHL GIFPGNQTAL VQGILERVVD CSSPDQTVCL 800
    EVLDESGSYW VKDKRLPPCS LRQALTYFLD ITTPPTQLQL HKLARFATEE 850
    THRQRLEALC QPSEYNDWKF SNNPTFLEVL EEFPSLRVPA AFLLSQLPIL 900
    KPRYYSISSS QDHTPSEVHL TVAVVTYRTR DGQGPLHHGV CSTWINNLKP 950
    EDPVPCFVRS VSGFQLPEDP SQPCILIGPG TGIAPFRSFW QQRLHDSQHR 1000
    GLKGGRMTLV FGCRHPEEDH LYQEEMQEMV RKGVLFQVHT GYSRLPGKPK 1050
    VYVQDILQKE LADEVFSVLH GEQGHLYVCG DVRMARDVAT TLKKLVAAKL 1100
    NLSEEQVEDY FFQLKSQKRY HEDIFGAVFS YGAKKGNTLE EPKGTRL 1147
    Length:1,147
    Mass (Da):130,628
    Last modified:October 1, 1996 - v2
    Checksum:i77C77432DD8AB0A9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101R → K in BAA07994. 1 PublicationCurated
    Sequence conflicti72 – 721H → Y in BAA03138. (PubMed:7680561)Curated
    Sequence conflicti107 – 1071C → R in AAC13747. (PubMed:7513765)Curated
    Sequence conflicti128 – 1281D → V in BAA12035. (PubMed:8913516)Curated
    Sequence conflicti130 – 1301P → H in AAC13747. (PubMed:7513765)Curated
    Sequence conflicti171 – 1711E → G in BAA12035. (PubMed:8913516)Curated
    Sequence conflicti195 – 1951P → S in BAA12035. (PubMed:8913516)Curated
    Sequence conflicti248 – 2481S → N in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti248 – 2481S → T(PubMed:7513765)Curated
    Sequence conflicti248 – 2481S → T(PubMed:7682072)Curated
    Sequence conflicti264 – 2641Y → I in AAC13747. (PubMed:7513765)Curated
    Sequence conflicti271 – 2711D → A in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti277 – 2771D → E in AAC13747. (PubMed:7513765)Curated
    Sequence conflicti348 – 3481A → P in BAA03138. (PubMed:7680561)Curated
    Sequence conflicti349 – 3491V → A in CAA54208. (PubMed:7519448)Curated
    Sequence conflicti380 – 3801F → L(PubMed:7540573)Curated
    Sequence conflicti380 – 3801F → L1 PublicationCurated
    Sequence conflicti380 – 3801F → L(PubMed:8913516)Curated
    Sequence conflicti380 – 3801F → L in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti380 – 3801F → L in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti395 – 3951R → S in BAA02090. (PubMed:7693462)Curated
    Sequence conflicti399 – 3991E → G in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti412 – 4121V → A in AAC13747. (PubMed:7513765)Curated
    Sequence conflicti477 – 4771M → I1 PublicationCurated
    Sequence conflicti513 – 5131T → R in AAB18620. 1 PublicationCurated
    Sequence conflicti515 – 5151L → W in AAB31028. (PubMed:7516453)Curated
    Sequence conflicti545 – 5451G → R in AAB31028. (PubMed:7516453)Curated
    Sequence conflicti551 – 5511A → R in AAB18620. 1 PublicationCurated
    Sequence conflicti556 – 5561A → S in AAB31028. (PubMed:7516453)Curated
    Sequence conflicti559 – 5591S → T in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti559 – 5591S → T in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti564 – 5641T → N in AAB31028. (PubMed:7516453)Curated
    Sequence conflicti570 – 5701E → D in AAB31028. (PubMed:7516453)Curated
    Sequence conflicti583 – 5831L → P(PubMed:7682072)Curated
    Sequence conflicti583 – 5831L → P(PubMed:9535415)Curated
    Sequence conflicti591 – 5911G → A in AAB31028. (PubMed:7516453)Curated
    Sequence conflicti591 – 5911G → V(PubMed:7680561)Curated
    Sequence conflicti591 – 5911G → V(PubMed:7519448)Curated
    Sequence conflicti619 – 6191A → R in AAA85861. (PubMed:7540573)Curated
    Sequence conflicti640 – 6401Q → P in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti664 – 6641D → G in AAB18620. 1 PublicationCurated
    Sequence conflicti679 – 6802ET → VP in BAA03138. (PubMed:7680561)Curated
    Sequence conflicti690 – 6901Q → P in AAB18620. 1 PublicationCurated
    Sequence conflicti711 – 7111S → N in AAB18620. 1 PublicationCurated
    Sequence conflicti714 – 7152SL → TR in AAB18620. 1 PublicationCurated
    Sequence conflicti714 – 7141S → P(PubMed:7540573)Curated
    Sequence conflicti714 – 7141S → P1 PublicationCurated
    Sequence conflicti714 – 7141S → P(PubMed:8913516)Curated
    Sequence conflicti714 – 7141S → P in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti714 – 7141S → P in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti714 – 7141S → P in AAC16401. (PubMed:9535415)Curated
    Sequence conflicti719 – 7191K → R in AAB18620. 1 PublicationCurated
    Sequence conflicti721 – 7211L → P(PubMed:7519448)Curated
    Sequence conflicti722 – 7221S → R(PubMed:7680561)Curated
    Sequence conflicti722 – 7221S → R(PubMed:7519448)Curated
    Sequence conflicti722 – 7221S → R1 PublicationCurated
    Sequence conflicti724 – 7263IHA → FLN1 PublicationCurated
    Sequence conflicti730 – 7301F → I in AAB18620. 1 PublicationCurated
    Sequence conflicti731 – 7311T → A in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti740 – 7401L → P in CAA54208. (PubMed:7519448)Curated
    Sequence conflicti779 – 7791A → G in AAC13747. (PubMed:7513765)Curated
    Sequence conflicti834 – 8341P → S in BAA12035. (PubMed:8913516)Curated
    Sequence conflicti844 – 8441A → G in BAA03138. (PubMed:7680561)Curated
    Sequence conflicti895 – 8951S → L in BAA02090. (PubMed:7693462)Curated
    Sequence conflicti911 – 9111Q → L in AAC13747. (PubMed:7513765)Curated
    Sequence conflicti925 – 9251V → D in BAA12035. (PubMed:8913516)Curated
    Sequence conflicti937 – 9371H → N in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti999 – 9991H → R(PubMed:7540573)Curated
    Sequence conflicti999 – 9991H → R1 PublicationCurated
    Sequence conflicti999 – 9991H → R in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti999 – 9991H → R in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti1008 – 10092TL → NF in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti1016 – 10161P → R(PubMed:7682072)Curated
    Sequence conflicti1016 – 10161P → S(PubMed:8913516)Curated
    Sequence conflicti1017 – 10171E → R(PubMed:7682072)Curated
    Sequence conflicti1017 – 10171E → R(PubMed:8913516)Curated
    Sequence conflicti1024 – 10241E → K in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti1076 – 10761L → I in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti1084 – 10841M → I in CAA54208. (PubMed:7519448)Curated
    Sequence conflicti1129 – 11291F → V in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti1133 – 11331A → V(PubMed:7540573)Curated
    Sequence conflicti1133 – 11331A → V1 PublicationCurated
    Sequence conflicti1133 – 11331A → V in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti1133 – 11331A → V in AAC83554. (PubMed:9851365)Curated
    Sequence conflicti1138 – 11381T → A(PubMed:7540573)Curated
    Sequence conflicti1138 – 11381T → A1 PublicationCurated
    Sequence conflicti1138 – 11381T → A in AAC83553. (PubMed:9851365)Curated
    Sequence conflicti1138 – 11381T → A in AAC83554. (PubMed:9851365)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14051 mRNA. Translation: BAA03138.1.
    U26686 mRNA. Translation: AAA85861.1.
    U03699 mRNA. Translation: AAC13747.1.
    D12520 mRNA. Translation: BAA02090.1.
    L12562 mRNA. Translation: AAA41720.1.
    X76881 mRNA. Translation: CAA54208.1.
    D44591 mRNA. Translation: BAA07994.1.
    D83661 mRNA. Translation: BAA12035.1.
    AF049656 mRNA. Translation: AAC83553.1.
    AF051164 mRNA. Translation: AAC83554.1.
    AF006619 mRNA. Translation: AAC16401.1.
    AF006620 mRNA. Translation: AAC16402.1.
    U48829 mRNA. Translation: AAB18620.1.
    S71597 mRNA. Translation: AAB31028.2.
    L36063 mRNA. Translation: AAC02242.1.
    PIRiI53165.
    I56575.
    JC5027.
    S38253.
    S47647.
    RefSeqiNP_036743.3. NM_012611.3.
    UniGeneiRn.10400.

    Genome annotation databases

    GeneIDi24599.
    KEGGirno:24599.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14051 mRNA. Translation: BAA03138.1 .
    U26686 mRNA. Translation: AAA85861.1 .
    U03699 mRNA. Translation: AAC13747.1 .
    D12520 mRNA. Translation: BAA02090.1 .
    L12562 mRNA. Translation: AAA41720.1 .
    X76881 mRNA. Translation: CAA54208.1 .
    D44591 mRNA. Translation: BAA07994.1 .
    D83661 mRNA. Translation: BAA12035.1 .
    AF049656 mRNA. Translation: AAC83553.1 .
    AF051164 mRNA. Translation: AAC83554.1 .
    AF006619 mRNA. Translation: AAC16401.1 .
    AF006620 mRNA. Translation: AAC16402.1 .
    U48829 mRNA. Translation: AAB18620.1 .
    S71597 mRNA. Translation: AAB31028.2 .
    L36063 mRNA. Translation: AAC02242.1 .
    PIRi I53165.
    I56575.
    JC5027.
    S38253.
    S47647.
    RefSeqi NP_036743.3. NM_012611.3.
    UniGenei Rn.10400.

    3D structure databases

    ProteinModelPortali Q06518.
    SMRi Q06518. Positions 80-499, 700-1127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-59942N.

    Chemistry

    BindingDBi Q06518.
    ChEMBLi CHEMBL3051.

    PTM databases

    PhosphoSitei Q06518.

    Proteomic databases

    PRIDEi Q06518.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24599.
    KEGGi rno:24599.

    Organism-specific databases

    CTDi 4843.
    RGDi 3185. Nos2.

    Phylogenomic databases

    eggNOGi COG4362.
    HOVERGENi HBG000159.
    InParanoidi Q06518.
    KOi K13241.
    PhylomeDBi Q06518.

    Miscellaneous databases

    NextBioi 603804.

    Gene expression databases

    Genevestigatori Q06518.

    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 of inducible nitric oxide synthase in rat vascular smooth muscle cells."
      Nunokawa Y., Ishida N., Tanaka S.
      Biochem. Biophys. Res. Commun. 191:89-94(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Vascular smooth muscle.
    2. "Cloning and expression of cytokine-inducible nitric oxide synthase cDNA from rat islets of Langerhans."
      Karlsen A.E., Andersen H.U., Vissing H., Larsen P.M., Fey S.J., Cuartero B.G., Madsen O.D., Petersen J.S., Mortensen S.B., Mandrup-Poulsen T., Boel E., Nerup J.
      Diabetes 44:753-758(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Pancreatic islet.
    3. "Cloning and expression of inducible nitric oxide synthase from rat astrocytes."
      Galea E., Reis D.J., Feinstein D.L.
      J. Neurosci. Res. 37:406-414(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Astrocyte.
    4. "Molecular cloning of a cDNA encoding an inducible calmodulin-dependent nitric-oxide synthase from rat liver and its expression in COS 1 cells."
      Adachi H., Iida S., Oguchi S., Ohshima H., Suzuki H., Nagasaki K., Kawasaki H., Sugimura T., Esumi H.
      Eur. J. Biochem. 217:37-43(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    5. "Hepatocytes and macrophages express an identical cytokine inducible nitric oxide synthase gene."
      Wood E.R., Berger H. Jr., Sherman P.A., Lapetina E.G.
      Biochem. Biophys. Res. Commun. 191:767-774(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Hepatocyte.
    6. "cDNA cloning and expression of inducible nitric oxide synthase from rat vascular smooth muscle cells."
      Geng Y.J., Almquist M., Hansson G.K.
      Biochim. Biophys. Acta 1218:421-424(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Aorta.
    7. "Cloning of an inducible nitric oxide synthase from rat polymorphonuclear neutrophils."
      Kosuga K., Yui Y., Hattori R., Sase K., Eizawa H., Aoyama T., Inoue R., Sasayama S.
      Endothelium 2:217-221(1994)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    8. "Sequence analysis of inducible nitric oxide synthase in rat kidney, lung, and uterus."
      Tsutsumishita Y., Kawai Y., Takahara H., Onda T., Miyoshi J., Futaki S., Niwa M.
      Biol. Pharm. Bull. 19:1374-1376(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    9. "Complete coding sequence of inducible nitric oxide synthase from human heart and skeletal muscle of patients with chronic heart failure."
      Adams V., Krabbes S., Jiang H., Yu J., Rahmel A., Gielen S., Schuler G., Hambrecht R.
      Nitric Oxide 2:242-249(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    10. "Vascular smooth muscle nitric oxide synthase anomalies in Dahl/Rapp salt-sensitive rats."
      Chen P.Y., Gladish R.D., Sanders P.W.
      Hypertension 31:918-924(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 426-788.
      Strain: Dahl/Rapp salt sensitive strain.
      Tissue: Vascular smooth muscle.
    11. "Advances in the studies of NO synthesis regulation in mesanglial cells."
      Saura M., Zaragoza C., Martinez-Dalmau R., Perez-Sala D., Lamas S.
      Nefrologia 16:35-39(1996)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 509-740.
      Strain: Wistar.
      Tissue: Renal glomerulus.
    12. "Location of an inducible nitric oxide synthase mRNA in the normal kidney."
      Morrissey J.J., McCracken R., Kaneto H., Vehaskari M., Montani D., Klahr S.
      Kidney Int. 45:998-1005(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 479-655.
      Strain: Sprague-Dawley.
      Tissue: Renal glomerulus.
    13. "Isolation and characterization of iNOS from rat cardiocytes."
      Michel T., Balligand J.-L.
      Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 420-479.
      Tissue: Myocardium.

    Entry informationi

    Entry nameiNOS2_RAT
    AccessioniPrimary (citable) accession number: Q06518
    Secondary accession number(s): O35765
    , O35766, O60591, O60604, P97774, Q63267, Q64005, Q64558
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    sequence Was originally thought to originate from human but appears to be from rat.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3