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O19132

- NOS1_RABIT

UniProt

O19132 - NOS1_RABIT

Protein

Nitric oxide synthase, brain

Gene

NOS1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR 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

    Stimulated by calcium/calmodulin. Inhibited by n-Nos-inhibiting protein (PIN) which may prevent the dimerization of the protein. Inhibited by NOSIP By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi421 – 4211Iron (heme axial ligand)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi887 – 91832FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi1033 – 104412FADBy similarityAdd
    BLAST
    Nucleotide bindingi1176 – 118611FADBy similarityAdd
    BLAST
    Nucleotide bindingi1251 – 126919NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1349 – 136416NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. FMN binding Source: InterPro
    3. heme binding Source: InterPro
    4. iron ion binding Source: InterPro
    5. NADP binding Source: InterPro
    6. nitric-oxide synthase activity Source: UniProtKB-EC

    GO - Biological processi

    1. nitric oxide biosynthetic process Source: InterPro

    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, brain (EC:1.14.13.39)
    Alternative name(s):
    Constitutive NOS
    NC-NOS
    NOS type I
    Neuronal NOS
    Short name:
    N-NOS
    Short name:
    nNOS
    Peptidyl-cysteine S-nitrosylase NOS1
    bNOS
    Gene namesi
    Name:NOS1
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    Cell membranesarcolemma By similarity; Peripheral membrane protein By similarity. Cell projectiondendritic spine By similarity
    Note: In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex. In neurons, enriched in dendritic spines By similarity.By similarity

    GO - Cellular componenti

    1. dendritic spine Source: UniProtKB-SubCell
    2. sarcolemma Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14351435Nitric oxide synthase, brainPRO_0000170923Add
    BLAST

    Post-translational modificationi

    Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro).By similarity

    Keywords - PTMi

    Ubl conjugation

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON. Forms a ternary complex with CAPON and RASD1. Forms a ternary complex with CAPON and SYN1. Interacts with ZDHHC23. Interacts with NOSIP; which may impair its synaptic location By similarity. Interacts with HTR4. Interacts with VAC14 By similarity. Interacts with SLC6A4 By similarity. Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains) By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000020745.

    Structurei

    3D structure databases

    ProteinModelPortaliO19132.
    SMRiO19132. Positions 7-133, 304-722, 756-1419.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 9983PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini761 – 941181Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini996 – 1243248FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 206206Interaction with NOSIPBy similarityAdd
    BLAST
    Regioni164 – 24683PIN (nNOS-inhibiting protein) bindingBy similarityAdd
    BLAST
    Regioni731 – 75121Calmodulin-bindingSequence AnalysisAdd
    BLAST
    Regioni756 – 77520Tetrahydrobiopterin-bindingBy similarityAdd
    BLAST

    Domaini

    The PDZ domain in the N-terminal part of the neuronal isoform participates in protein-protein interaction, and is responsible for targeting nNos to synaptic membranes in muscles. Mediates interaction with VAC14 By similarity.By similarity

    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
    Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG4362.
    HOGENOMiHOG000220884.
    HOVERGENiHBG000159.

    Family and domain databases

    Gene3Di1.20.990.10. 1 hit.
    2.30.42.10. 1 hit.
    3.40.50.360. 2 hits.
    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.
    IPR001478. PDZ.
    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.
    PF00595. PDZ. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000333. NOS. 1 hit.
    PRINTSiPR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SMARTiSM00228. PDZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 1 hit.
    SSF52218. 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.
    PS50106. PDZ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O19132-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEHVFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG     50
    AAEQSGLIQA GDIILAVNGR PLVDLSYDSA LEVLRGVASE THVVLILRGP 100
    EGFTTNLETT FTGDGTPKTI RVTQPLGAPT KAVDLSHQPP SAGKEQPRPV 150
    DGAAGPGSWP QPTQGHGQEA GSPSRANGLA PRTSSQDPAK KSGWAGLQGS 200
    GDKNELLKEI EPVLTLLAGG SKAVDGGGPA KAETRDTGVQ VDRDFDAKSH 250
    KPLPLGVEND RVFSDLWGKG SAPVVLNNPY SEKEQPPASG KQSPTKNGSP 300
    SKCPRFLKVK NWETDVVLTD TLHLKSTLET GCTEHICMGS IMFPSQHTRR 350
    PEDIRTKEQL FPLAKEFIDQ YYSSIKRFGS KAHMERLEEV NKEIESTSTY 400
    QLKDTELIYG AKHAWRNASR CVGRIQWSKL QVFDARDCTT AHGMFNYICN 450
    HIKYATNKGN LRSAITIFPQ RTDGKHDFRV WNSQLIRYAG YKQPDGSTLG 500
    DPANVQFTEI CIQQGWKPPR SRFDVLPLLL QANGNDPELF QIPPELVLEV 550
    PIRHPKFEWF KDLGLKWYGL PAVSNMLLEI GGLEFSACPF SGWYMGTEIG 600
    VRDYCDNSRY NILEEVAKKM NLDMRKTSSL WKDQALVEIN IAVLYSFQSD 650
    KVTIVDHHSA TESFIKHMEN EYRCRGGCPA DWVWIVPPMS GSITPVFHQE 700
    MLNYRLTPCF EYQPDPWNTH VWKGTNGTPT KRRAIGFKKL AEAVKFSAKL 750
    MGQAMAKRVK ATILYATETG KSQAYAKTLC EIFKHAFDAK VMSMEEYDIV 800
    HLEHETLVLV VTSTFGNGDP PENGEKFRCA LMEMRHPNSL QEERKSYKVR 850
    FNSVSSYSDS RKSSGDGPDV RDHFESAGPL ANVRFSVFGL GSRAYPHFCA 900
    FGHAVDTLLE ELGGERILKM REGDELCGQE EAFRTWAKKV FKAACDVFCV 950
    GDDVNIEKAN NSLISNDRSW KRNKFRLTYV AEAPGLTQGL SSVHKKRVSA 1000
    ARLLSRQNLQ SPKSSRSTIF VRLHTNGSQE LQYQPGDHLG VFPGNHEDLV 1050
    NALIERLEDA PPANQMVKVE LLEERNTALG VISNWKDEPR LPPCTVFQAF 1100
    KYYLDITTPP TPLQLQQFAS LASNEKEKQR LLVLSKGLQE YEEWKWGKNP 1150
    TIVEVLEEFP SIQMPATLLL TQLSLLQPRY YSISSSPDMY PDEVHLTVAI 1200
    VSYHTRDGEG PIHHGVCSSW LNRIPADEVV PCFVRGAPSF RLPRNPQVPC 1250
    ILVGPGTAFA PFRSFWQQRQ FDIQHKGMSP CPMVLVFGCR QSKIDHIYRE 1300
    EALQAKNKGV FRELYTAYSR EPDKPKKYVQ DILQEQLAEQ VYRALKEQGG 1350
    HIYVCGDVTM AADVLKAVQR IMAQQGKLSA EDAGVFISRL RDDNRYHEDI 1400
    FGVTLRTYEV TNRLRSESIA FIEESKKDTD EVFSS 1435
    Length:1,435
    Mass (Da):160,865
    Last modified:January 1, 1998 - v1
    Checksum:i3ED87ECDD83A7A5A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91584 mRNA. Translation: AAB68663.1.
    RefSeqiNP_001075854.1. NM_001082385.1.
    UniGeneiOcu.2169.

    Genome annotation databases

    GeneIDi100009243.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U91584 mRNA. Translation: AAB68663.1 .
    RefSeqi NP_001075854.1. NM_001082385.1.
    UniGenei Ocu.2169.

    3D structure databases

    ProteinModelPortali O19132.
    SMRi O19132. Positions 7-133, 304-722, 756-1419.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000020745.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009243.

    Organism-specific databases

    CTDi 4842.

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.

    Family and domain databases

    Gene3Di 1.20.990.10. 1 hit.
    2.30.42.10. 1 hit.
    3.40.50.360. 2 hits.
    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.
    IPR001478. PDZ.
    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.
    PF00595. PDZ. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000333. NOS. 1 hit.
    PRINTSi PR00369. FLAVODOXIN.
    PR00371. FPNCR.
    SMARTi SM00228. PDZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 1 hit.
    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.
    PS50106. PDZ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a cDNA encoding a constitutive nitric oxide synthase from rabbit brain."
      Jeong Y., Yim J.
      Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.

    Entry informationi

    Entry nameiNOS1_RABIT
    AccessioniPrimary (citable) accession number: O19132
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 125 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