Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O19114

- NOS2_RABIT

UniProt

O19114 - NOS2_RABIT

Protein

Nitric oxide synthase, inducible

Gene

NOS2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

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

    Enzyme regulationi

    Not stimulated by calcium/calmodulin.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi‹1 – 25›25FMNBy similarityAdd
    BLAST
    Nucleotide bindingi138 – 14912FADBy similarityAdd
    BLAST
    Nucleotide bindingi274 – 28411FADBy similarityAdd
    BLAST
    Nucleotide bindingi349 – 36719NADPBy similarityAdd
    BLAST
    Nucleotide bindingi447 – 46216NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. nitric-oxide synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. peptidyl-cysteine S-nitrosylation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›496›496Nitric oxide synthase, induciblePRO_0000170936Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer. Binds SLC9A3R1 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO19114.
    SMRiO19114. Positions 74-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 341241FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProiIPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view]
    PfamiPF00667. FAD_binding_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view]
    PRINTSiPR00371. FPNCR.
    SUPFAMiSSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEiPS51384. FAD_FR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    O19114-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYPHFCAFVM TSTRNCLTWA ASQLAPTGEG DELSGQEDAF RSWAVQTFRA    50
    ACETFDVRSK HCIQIPKRYT SNATWEPEQY KLTQSPEPLD LNKALSSIHA 100
    KNLFTMRLRS LQNLHSEKSS RTTLLVQLTF EGSRGPSYLP GEHLGIFPGN 150
    QTGLVQGILE RVVDCSSPDQ TVCLEVHDES GSYWVKDKRL PPCSLRQALT 200
    YFLDITTPPT QLQLHKLARF ATEETHRQRL EALCQPSEYN DWKFSNNPTF 250
    LEVLEEFPSL RVPAAFLLSQ LPILKPRYYS ISSSQDHTPS EVHLTVAVVT 300
    YRTRDGQGPL HHGVCSTWIN NLKPEDPVPC FVRSVSGFQL PEDPSQPCIL 350
    IGPGTGIAPF RSFWQQRLHD SQHRGLKGGR MTLVFGCRHP EEDHLYQEEM 400
    QEMVRKGVLF QVHTGYSRLP GKPKVYVQDI LQKELADEVF SVLHGEQGHL 450
    YVCGDVRMAR DVATTLKKLV AAKLNLSEEQ VEDYFFQLKY HEDIFG 496
    Length:496
    Mass (Da):56,397
    Last modified:January 1, 1998 - v1
    Checksum:iA0A1D303C57F0EEC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-terminal residuei496 – 4961

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85094 mRNA. Translation: AAB65618.1.
    UniGeneiOcu.2556.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85094 mRNA. Translation: AAB65618.1 .
    UniGenei Ocu.2556.

    3D structure databases

    ProteinModelPortali O19114.
    SMRi O19114. Positions 74-496.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    3.40.50.360. 1 hit.
    InterProi IPR003097. FAD-binding_1.
    IPR017927. Fd_Rdtase_FAD-bd.
    IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
    IPR029039. Flavoprotein-like.
    IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
    IPR001433. OxRdtase_FAD/NAD-bd.
    IPR017938. Riboflavin_synthase-like_b-brl.
    [Graphical view ]
    Pfami PF00667. FAD_binding_1. 1 hit.
    PF00175. NAD_binding_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00371. FPNCR.
    SUPFAMi SSF52218. SSF52218. 1 hit.
    SSF63380. SSF63380. 1 hit.
    PROSITEi PS51384. FAD_FR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rabbit iducible nitric oxide synthase gene-NOS II."
      Broner C.W., Eledath F.M.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: New Zealand white.
      Tissue: Heart.

    Entry informationi

    Entry nameiNOS2_RABIT
    AccessioniPrimary (citable) accession number: O19114
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 92 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3