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P29476

- NOS1_RAT

UniProt

P29476 - NOS1_RAT

Protein

Nitric oxide synthase, brain

Gene

Nos1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (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 the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in the colorectum.

    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 By similarity. Inhibited by NOSIP.By similarity1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi415 – 4151Iron (heme axial ligand)By similarity
    Binding sitei588 – 5881Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi881 – 91232FMNPROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi1027 – 103812FADBy similarityAdd
    BLAST
    Nucleotide bindingi1170 – 118011FADBy similarityAdd
    BLAST
    Nucleotide bindingi1245 – 126319NADPBy similarityAdd
    BLAST
    Nucleotide bindingi1343 – 135816NADPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. amino acid binding Source: RGD
    2. cadmium ion binding Source: BHF-UCL
    3. calmodulin binding Source: RGD
    4. enzyme binding Source: RGD
    5. flavin adenine dinucleotide binding Source: BHF-UCL
    6. FMN binding Source: BHF-UCL
    7. heme binding Source: BHF-UCL
    8. ion channel binding Source: BHF-UCL
    9. iron ion binding Source: InterPro
    10. NADP binding Source: BHF-UCL
    11. NADPH-hemoprotein reductase activity Source: RefGenome
    12. nitric-oxide synthase activity Source: BHF-UCL
    13. protein binding Source: UniProtKB
    14. protein homodimerization activity Source: RGD
    15. scaffold protein binding Source: BHF-UCL
    16. sodium channel regulator activity Source: BHF-UCL

    GO - Biological processi

    1. aging Source: RGD
    2. arginine catabolic process Source: BHF-UCL
    3. behavioral response to cocaine Source: RGD
    4. cellular response to mechanical stimulus Source: RGD
    5. female pregnancy Source: RGD
    6. muscle contraction Source: RefGenome
    7. negative regulation of apoptotic process Source: RGD
    8. negative regulation of blood pressure Source: RGD
    9. negative regulation of cell proliferation Source: RGD
    10. negative regulation of cytosolic calcium ion concentration Source: RGD
    11. negative regulation of heart contraction Source: RGD
    12. negative regulation of insulin secretion Source: RGD
    13. negative regulation of vasoconstriction Source: RGD
    14. nitric oxide biosynthetic process Source: BHF-UCL
    15. nitric oxide mediated signal transduction Source: RefGenome
    16. peptidyl-cysteine S-nitrosylation Source: BHF-UCL
    17. positive regulation of guanylate cyclase activity Source: RefGenome
    18. positive regulation of long-term synaptic potentiation Source: RGD
    19. positive regulation of neuron death Source: RGD
    20. positive regulation of sodium ion transmembrane transport Source: BHF-UCL
    21. positive regulation of vasodilation Source: RGD
    22. regulation of heart contraction Source: RGD
    23. regulation of sensory perception of pain Source: RGD
    24. response to activity Source: RGD
    25. response to estrogen Source: RGD
    26. response to ethanol Source: RGD
    27. response to heat Source: RGD
    28. response to hypoxia Source: BHF-UCL
    29. response to lead ion Source: RGD
    30. response to lipopolysaccharide Source: RGD
    31. response to nicotine Source: RGD
    32. response to nitric oxide Source: RGD
    33. response to nutrient levels Source: RGD
    34. response to organic cyclic compound Source: RGD
    35. response to organonitrogen compound Source: RGD
    36. response to peptide hormone Source: RGD
    37. response to vitamin E Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SABIO-RKP29476.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nitric oxide synthase, brain (EC:1.14.13.39)
    Alternative name(s):
    BNOS
    Constitutive NOS
    NC-NOS
    NOS type I
    Neuronal NOS
    Short name:
    N-NOS
    Short name:
    nNOS
    Peptidyl-cysteine S-nitrosylase NOS1
    Gene namesi
    Name:Nos1
    Synonyms:Bnos
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3184. Nos1.

    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 By similarity. In neurons, enriched in dendritic spines.By similarity1 Publication

    GO - Cellular componenti

    1. azurophil granule Source: RGD
    2. cytoplasm Source: RGD
    3. cytosol Source: RGD
    4. dendrite Source: RGD
    5. dendritic spine Source: UniProtKB-SubCell
    6. membrane Source: RGD
    7. mitochondrial outer membrane Source: RGD
    8. mitochondrion Source: MGI
    9. nuclear membrane Source: RGD
    10. nucleus Source: RGD
    11. perinuclear region of cytoplasm Source: BHF-UCL
    12. photoreceptor inner segment Source: BHF-UCL
    13. plasma membrane Source: RGD
    14. postsynaptic density Source: RGD
    15. protein complex Source: BHF-UCL
    16. sarcolemma Source: BHF-UCL
    17. synapse Source: RGD
    18. vesicle membrane Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi588 – 5881Y → F: No decrease in activity. 1 Publication
    Mutagenesisi588 – 5881Y → H: 50% decrease of activity. 1 Publication
    Mutagenesisi588 – 5881Y → S: 30% decrease of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14291429Nitric oxide synthase, brainPRO_0000170924Add
    BLAST

    Post-translational modificationi

    Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro).1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiP29476.
    PRIDEiP29476.

    PTM databases

    PhosphoSiteiP29476.

    Expressioni

    Tissue specificityi

    Isoform N-NOS-1 is expressed in brain and colorectum. Found in the Auerbach's plexus of the enteric nervous system. Isoform PNNOS is expressed in the penis, urethra, prostate, and skeletal muscle, and coexists with the cerebellar nnos in the pelvic plexus, bladder and liver, and is detectable in the cerebellum.1 Publication

    Gene expression databases

    GenevestigatoriP29476.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with DLG4; the interaction possibly being prevented by the association between NOS1 and CAPON By similarity. 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. Interacts with HTR4 By similarity. Interacts with SLC6A4 By similarity. Interacts with VAC14. Interacts (via N-terminal domain) with DLG4 (via N-terminal tandem pair of PDZ domains).By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CALMP621572EBI-349460,EBI-397403From a different organism.

    Protein-protein interaction databases

    BioGridi246738. 10 interactions.
    IntActiP29476. 6 interactions.
    MINTiMINT-89230.
    STRINGi10116.ENSRNOP00000062735.

    Structurei

    Secondary structure

    1
    1429
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 124
    Beta strandi15 – 217
    Turni24 – 263
    Beta strandi29 – 346
    Beta strandi36 – 394
    Beta strandi41 – 466
    Helixi51 – 555
    Turni60 – 623
    Beta strandi63 – 675
    Beta strandi73 – 753
    Helixi77 – 8610
    Beta strandi89 – 9810
    Beta strandi103 – 1119
    Beta strandi113 – 1153
    Beta strandi117 – 1248
    Beta strandi301 – 3055
    Turni306 – 3083
    Beta strandi311 – 3144
    Helixi316 – 3194
    Beta strandi328 – 3314
    Beta strandi340 – 3423
    Beta strandi345 – 3473
    Helixi351 – 36818
    Beta strandi372 – 3743
    Helixi375 – 39117
    Helixi398 – 41013
    Helixi418 – 4203
    Beta strandi425 – 4284
    Helixi435 – 45016
    Helixi451 – 4533
    Beta strandi458 – 4614
    Beta strandi466 – 4705
    Beta strandi476 – 4805
    Beta strandi484 – 4863
    Beta strandi490 – 4945
    Helixi496 – 4983
    Helixi499 – 5079
    Beta strandi515 – 5173
    Beta strandi522 – 5254
    Beta strandi527 – 5293
    Beta strandi532 – 5343
    Helixi538 – 5403
    Beta strandi543 – 5453
    Helixi554 – 5574
    Beta strandi560 – 5634
    Beta strandi571 – 5744
    Beta strandi577 – 5804
    Helixi590 – 5945
    Helixi596 – 5994
    Turni601 – 6044
    Helixi607 – 6137
    Helixi621 – 6233
    Helixi625 – 64319
    Helixi651 – 66919
    Helixi676 – 6794
    Beta strandi682 – 6843
    Helixi685 – 6873
    Helixi689 – 6924
    Beta strandi696 – 6983
    Beta strandi701 – 7055
    Helixi710 – 7134
    Beta strandi754 – 7607
    Beta strandi762 – 7643
    Helixi765 – 77713
    Turni778 – 7803
    Beta strandi781 – 7877
    Turni788 – 7903
    Helixi796 – 7983
    Beta strandi800 – 8067
    Turni810 – 8123
    Helixi816 – 8183
    Helixi819 – 82810
    Helixi841 – 8444
    Turni873 – 8764
    Beta strandi878 – 8858
    Beta strandi889 – 8913
    Helixi894 – 90512
    Beta strandi909 – 9124
    Beta strandi915 – 9184
    Turni919 – 9224
    Helixi923 – 94220
    Beta strandi946 – 9483
    Beta strandi961 – 9633
    Beta strandi968 – 9736
    Helixi980 – 9889
    Beta strandi993 – 100210
    Beta strandi1012 – 10187
    Helixi1023 – 10253
    Beta strandi1032 – 10354
    Helixi1041 – 10488
    Beta strandi1051 – 10533
    Beta strandi1061 – 107212
    Beta strandi1076 – 10816
    Helixi1090 – 10967
    Helixi1106 – 11138
    Helixi1119 – 112810
    Helixi1133 – 114210
    Helixi1146 – 11527
    Helixi1160 – 11667
    Beta strandi1173 – 11764
    Turni1181 – 11833
    Beta strandi1187 – 11937
    Beta strandi1196 – 11983
    Helixi1200 – 12023
    Beta strandi1206 – 12083
    Helixi1210 – 12156
    Beta strandi1223 – 12297
    Helixi1232 – 12343
    Beta strandi1244 – 12474
    Helixi1250 – 12534
    Helixi1254 – 127017
    Beta strandi1277 – 12848
    Turni1286 – 12883
    Helixi1293 – 13019
    Beta strandi1304 – 131411
    Helixi1323 – 13308
    Helixi1332 – 13409
    Beta strandi1345 – 13506
    Helixi1352 – 136918
    Helixi1374 – 138613
    Beta strandi1390 – 13945
    Helixi1401 – 141111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B8QNMR-A11-133[»]
    1CMIX-ray2.50C/D225-237[»]
    1F20X-ray1.90A963-1397[»]
    1K2RX-ray2.15A/B299-717[»]
    1K2SX-ray2.55A/B299-717[»]
    1K2TX-ray2.20A/B299-717[»]
    1K2UX-ray2.20A/B299-717[»]
    1LZXX-ray2.00A/B299-717[»]
    1LZZX-ray2.05A/B299-717[»]
    1M00X-ray2.05A/B299-717[»]
    1MMVX-ray2.00A/B299-717[»]
    1MMWX-ray2.00A/B299-717[»]
    1OM4X-ray1.75A/B297-718[»]
    1OM5X-ray2.30A/B297-717[»]
    1P6HX-ray1.98A/B297-717[»]
    1P6IX-ray1.90A/B297-717[»]
    1P6JX-ray2.00A/B297-717[»]
    1P6KX-ray1.78A/B297-717[»]
    1QAUX-ray1.25A14-125[»]
    1QAVX-ray1.90B12-126[»]
    1QW6X-ray2.10A298-716[»]
    1QWCX-ray2.30A298-716[»]
    1RS6X-ray1.95A/B297-717[»]
    1RS7X-ray1.95A/B297-717[»]
    1TLLX-ray2.30A/B742-1429[»]
    1VAGX-ray2.00A298-716[»]
    1ZVIX-ray2.00A298-716[»]
    1ZVLX-ray2.50A/B298-716[»]
    1ZZQX-ray1.90A/B299-718[»]
    1ZZRX-ray2.05A/B299-718[»]
    1ZZUX-ray1.90A/B299-718[»]
    2G6HX-ray2.00A/B299-718[»]
    2G6IX-ray1.90A/B299-718[»]
    2G6JX-ray2.30A/B299-718[»]
    2G6KX-ray2.00A/B299-718[»]
    2G6LX-ray2.05A/B299-718[»]
    2G6MX-ray1.85A/B299-718[»]
    2G6NX-ray1.90A/B299-718[»]
    2HX3X-ray2.00A/B297-718[»]
    2HX4X-ray2.15A/B297-718[»]
    3B3MX-ray1.95A/B297-718[»]
    3B3NX-ray1.98A/B297-718[»]
    3B3OX-ray2.05A/B297-718[»]
    3B3PX-ray2.45A/B297-718[»]
    3DQRX-ray2.40A/B297-718[»]
    3FC5X-ray2.59A/B297-718[»]
    3HSNX-ray1.91A/B297-718[»]
    3HSOX-ray2.02A/B297-718[»]
    3HSPX-ray2.20A/B297-718[»]
    3JT3X-ray2.15A/B297-718[»]
    3JT4X-ray1.80A/B297-718[»]
    3JT5X-ray2.10A/B297-718[»]
    3JT6X-ray2.20A/B297-718[»]
    3JT7X-ray2.10A/B297-718[»]
    3JT8X-ray1.95A/B297-718[»]
    3JT9X-ray2.10A/B297-718[»]
    3JTAX-ray2.18A/B297-718[»]
    3JWSX-ray1.95A/B297-718[»]
    3JWTX-ray2.01A/B297-718[»]
    3JWUX-ray1.93A/B297-718[»]
    3JWVX-ray1.98A/B297-718[»]
    3JX0X-ray2.20A/B297-718[»]
    3JX1X-ray2.00A/B297-718[»]
    3JX2X-ray2.10A/B297-718[»]
    3JX3X-ray1.95A/B297-718[»]
    3JX4X-ray2.26A/B297-718[»]
    3JX5X-ray2.15A/B297-718[»]
    3JX6X-ray2.35A/B297-718[»]
    3N2RX-ray1.90A/B297-718[»]
    3N5VX-ray2.30A/B297-718[»]
    3N5WX-ray1.73A/B297-718[»]
    3N5XX-ray1.80A/B297-718[»]
    3N5YX-ray2.05A/B297-718[»]
    3N5ZX-ray2.18A/B297-718[»]
    3N60X-ray1.98A/B297-718[»]
    3N61X-ray1.95A/B297-718[»]
    3N62X-ray1.95A/B297-718[»]
    3N63X-ray2.00A/B297-718[»]
    3N64X-ray1.95A/B297-718[»]
    3N65X-ray1.80A/B297-718[»]
    3N66X-ray1.78A/B297-718[»]
    3N67X-ray2.09A/B298-711[»]
    3N68X-ray2.53A/B298-711[»]
    3N69X-ray2.65A/B298-711[»]
    3N6AX-ray2.49A/B298-711[»]
    3N6BX-ray3.10A/B298-711[»]
    3N6CX-ray3.06A/B298-711[»]
    3N6DX-ray3.05A/B298-711[»]
    3N6EX-ray2.20A/B298-711[»]
    3N6FX-ray2.18A/B298-711[»]
    3N6GX-ray2.21A/B298-711[»]
    3NLJX-ray2.20A/B297-718[»]
    3NLKX-ray2.02A/B297-718[»]
    3NLMX-ray1.85A/B297-718[»]
    3NLNX-ray2.00A/B297-718[»]
    3NLOX-ray2.30A/B297-718[»]
    3NLPX-ray2.02A/B297-718[»]
    3NLQX-ray2.15A/B297-718[»]
    3NLRX-ray2.10A/B297-718[»]
    3NLVX-ray2.10A/B297-718[»]
    3NLWX-ray2.10A/B297-718[»]
    3NLXX-ray1.87A/B297-718[»]
    3NLYX-ray1.99A/B297-718[»]
    3NLZX-ray1.92A/B297-718[»]
    3NM0X-ray1.81A/B297-718[»]
    3NNYX-ray2.10A/B297-718[»]
    3NNZX-ray1.97A/B297-718[»]
    3PNEX-ray1.97A/B297-718[»]
    3PNFX-ray1.94A/B297-718[»]
    3PNGX-ray1.88A/B297-718[»]
    3Q99X-ray2.15A/B297-718[»]
    3Q9AX-ray2.24A/B297-718[»]
    3RQJX-ray1.84A/B297-718[»]
    3RQKX-ray2.21A/B297-718[»]
    3RQLX-ray1.93A/B297-718[»]
    3RQMX-ray1.95A/B297-718[»]
    3RQNX-ray1.95A/B297-718[»]
    3SVPX-ray2.05A/B297-718[»]
    3SVQX-ray2.18A/B297-718[»]
    3TYLX-ray1.90A/B297-718[»]
    3TYMX-ray2.00A/B297-718[»]
    3TYNX-ray1.97A/B297-718[»]
    3TYOX-ray1.93A/B297-718[»]
    3UFOX-ray2.17A/B297-718[»]
    3UFPX-ray2.10A/B297-718[»]
    3UFQX-ray2.06A/B297-718[»]
    3UFRX-ray2.10A/B297-718[»]
    3UFSX-ray1.97A/B297-718[»]
    3UFTX-ray2.08A/B297-718[»]
    3UFUX-ray1.89A/B297-718[»]
    3UFVX-ray2.08A/B297-718[»]
    3UFWX-ray2.00A/B297-718[»]
    4C39X-ray1.98A/B297-718[»]
    4CAMX-ray1.83A/B297-718[»]
    4CANX-ray1.91A/B297-718[»]
    4CAOX-ray1.98A/B297-718[»]
    4CAPX-ray2.06A/B297-718[»]
    4CAQX-ray1.95A/B297-718[»]
    4CDTX-ray2.00A/B297-718[»]
    4CTPX-ray2.05A/B297-718[»]
    4CTQX-ray2.00A/B297-718[»]
    4CTRX-ray2.20A/B297-718[»]
    4CTTX-ray2.30A/B297-718[»]
    4CTUX-ray2.16A/B297-718[»]
    4CTVX-ray1.78A/B297-718[»]
    4CTWX-ray1.90A/B297-718[»]
    4CTXX-ray1.82A/B297-718[»]
    4EUXX-ray2.14A/B297-718[»]
    4FVWX-ray1.81A/B297-718[»]
    4FVXX-ray2.00A/B297-718[»]
    4FVYX-ray1.70A/B297-718[»]
    4FVZX-ray1.99A/B297-718[»]
    4FW0X-ray1.95A/B297-718[»]
    4GQEX-ray1.80A/B297-718[»]
    4HOPX-ray2.29B/D/F4-126[»]
    4IMSX-ray2.15A/B297-718[»]
    4IMTX-ray2.20A/B297-718[»]
    4IMUX-ray2.03A/B297-718[»]
    4IMWX-ray2.20A/B297-718[»]
    4JSEX-ray1.97A/B297-718[»]
    4JSFX-ray2.05A/B297-718[»]
    4JSGX-ray1.94A/B297-718[»]
    4JSHX-ray2.35A/B297-718[»]
    4JSIX-ray2.09A/B297-718[»]
    4JSJX-ray1.92A/B297-718[»]
    4K5DX-ray2.10A/B297-718[»]
    4K5EX-ray1.89A/B297-718[»]
    4K5FX-ray2.20A/B297-718[»]
    4K5GX-ray1.85A/B297-718[»]
    4KCHX-ray2.15A/B297-718[»]
    4KCIX-ray2.27A/B297-718[»]
    4KCJX-ray2.05A/B297-718[»]
    4KCKX-ray2.10A/B297-718[»]
    4KCLX-ray1.93A/B297-718[»]
    4KCMX-ray2.07A/B297-718[»]
    4KCNX-ray1.85A/B297-718[»]
    4KCOX-ray1.86A/B297-718[»]
    4LUXX-ray1.86A/B297-718[»]
    ProteinModelPortaliP29476.
    SMRiP29476. Positions 12-126, 298-716, 750-1413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29476.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 9983PDZPROSITE-ProRule annotationAdd
    BLAST
    Domaini755 – 935181Flavodoxin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini990 – 1237248FAD-binding FR-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 200200Interaction with NOSIPAdd
    BLAST
    Regioni163 – 24078PIN (nNOS-inhibiting protein) bindingBy similarityAdd
    BLAST
    Regioni725 – 74521Calmodulin-bindingSequence AnalysisAdd
    BLAST
    Regioni750 – 76920Tetrahydrobiopterin-bindingAdd
    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 By similarity. Mediates interaction with VAC14.By similarity1 Publication

    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.
    InParanoidiP29476.
    KOiK13240.
    PhylomeDBiP29476.

    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform N-NOS-1 (identifier: P29476-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG     50
    AAEQSGLIQA GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP 100
    EGFTTHLETT FTGDGTPKTI RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD 150
    RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI DPTMKSTKAN LQDIGEHDEL 200
    LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD GKSHKAPPLG 250
    GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF 300
    LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT 350
    KDQLFPLAKE FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE 400
    LIYGAKHAWR NASRCVGRIQ WSKLQVFDAR DCTTAHGMFN YICNHVKYAT 450
    NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI RYAGYKQPDG STLGDPANVQ 500
    FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL VLEVPIRHPK 550
    FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD 600
    NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD 650
    HHSATESFIK HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL 700
    TPSFEYQPDP WNTHVWKGTN GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA 750
    KRVKATILYA TETGKSQAYA KTLCEIFKHA FDAKAMSMEE YDIVHLEHEA 800
    LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS YKVRFNSVSS 850
    YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD 900
    TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI 950
    EKPNNSLISN DRSWKRNKFR LTYVAEAPDL TQGLSNVHKK RVSAARLLSR 1000
    QNLQSPKFSR STIFVRLHTN GNQELQYQPG DHLGVFPGNH EDLVNALIER 1050
    LEDAPPANHV VKVEMLEERN TALGVISNWK DESRLPPCTI FQAFKYYLDI 1100
    TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW GKNPTMVEVL 1150
    EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR 1200
    DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG 1250
    TGIAPFRSFW QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK 1300
    NKGVFRELYT AYSREPDRPK KYVQDVLQEQ LAESVYRALK EQGGHIYVCG 1350
    DVTMAADVLK AIQRIMTQQG KLSEEDAGVF ISRLRDDNRY HEDIFGVTLR 1400
    TYEVTNRLRS ESIAFIEESK KDADEVFSS 1429
    Length:1,429
    Mass (Da):160,559
    Last modified:April 1, 1993 - v1
    Checksum:i7255C5AE165200F5
    GO
    Isoform N-NOS-2 (identifier: P29476-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         504-608: Missing.

    Show »
    Length:1,324
    Mass (Da):148,548
    Checksum:i2B527386DF5B4160
    GO
    Isoform PNNOS (identifier: P29476-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         839-839: K → KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR

    Show »
    Length:1,463
    Mass (Da):164,430
    Checksum:iA0522B26817B6705
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691I → V in AAC52782. (PubMed:8806605)Curated
    Sequence conflicti269 – 2691I → V AA sequence (PubMed:7520037)Curated
    Sequence conflicti953 – 9531P → A in AAC52782. (PubMed:8806605)Curated
    Sequence conflicti953 – 9531P → A AA sequence (PubMed:7520037)Curated
    Sequence conflicti1008 – 10081F → S in AAC52782. (PubMed:8806605)Curated
    Sequence conflicti1311 – 13111A → V in AAC52782. (PubMed:8806605)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei504 – 608105Missing in isoform N-NOS-2. CuratedVSP_003580Add
    BLAST
    Alternative sequencei839 – 8391K → KYPEPLRFFPRKGPSLSHVD SEAHSLVAARDSQHR in isoform PNNOS. 1 PublicationVSP_003581

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59949 mRNA. Translation: CAA42574.1.
    U67309 mRNA. Translation: AAC52782.1.
    PIRiS16233.
    RefSeqiNP_434686.1. NM_052799.1.
    UniGeneiRn.10573.

    Genome annotation databases

    GeneIDi24598.
    KEGGirno:24598.
    UCSCiRGD:3184. rat. [P29476-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59949 mRNA. Translation: CAA42574.1 .
    U67309 mRNA. Translation: AAC52782.1 .
    PIRi S16233.
    RefSeqi NP_434686.1. NM_052799.1.
    UniGenei Rn.10573.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B8Q NMR - A 11-133 [» ]
    1CMI X-ray 2.50 C/D 225-237 [» ]
    1F20 X-ray 1.90 A 963-1397 [» ]
    1K2R X-ray 2.15 A/B 299-717 [» ]
    1K2S X-ray 2.55 A/B 299-717 [» ]
    1K2T X-ray 2.20 A/B 299-717 [» ]
    1K2U X-ray 2.20 A/B 299-717 [» ]
    1LZX X-ray 2.00 A/B 299-717 [» ]
    1LZZ X-ray 2.05 A/B 299-717 [» ]
    1M00 X-ray 2.05 A/B 299-717 [» ]
    1MMV X-ray 2.00 A/B 299-717 [» ]
    1MMW X-ray 2.00 A/B 299-717 [» ]
    1OM4 X-ray 1.75 A/B 297-718 [» ]
    1OM5 X-ray 2.30 A/B 297-717 [» ]
    1P6H X-ray 1.98 A/B 297-717 [» ]
    1P6I X-ray 1.90 A/B 297-717 [» ]
    1P6J X-ray 2.00 A/B 297-717 [» ]
    1P6K X-ray 1.78 A/B 297-717 [» ]
    1QAU X-ray 1.25 A 14-125 [» ]
    1QAV X-ray 1.90 B 12-126 [» ]
    1QW6 X-ray 2.10 A 298-716 [» ]
    1QWC X-ray 2.30 A 298-716 [» ]
    1RS6 X-ray 1.95 A/B 297-717 [» ]
    1RS7 X-ray 1.95 A/B 297-717 [» ]
    1TLL X-ray 2.30 A/B 742-1429 [» ]
    1VAG X-ray 2.00 A 298-716 [» ]
    1ZVI X-ray 2.00 A 298-716 [» ]
    1ZVL X-ray 2.50 A/B 298-716 [» ]
    1ZZQ X-ray 1.90 A/B 299-718 [» ]
    1ZZR X-ray 2.05 A/B 299-718 [» ]
    1ZZU X-ray 1.90 A/B 299-718 [» ]
    2G6H X-ray 2.00 A/B 299-718 [» ]
    2G6I X-ray 1.90 A/B 299-718 [» ]
    2G6J X-ray 2.30 A/B 299-718 [» ]
    2G6K X-ray 2.00 A/B 299-718 [» ]
    2G6L X-ray 2.05 A/B 299-718 [» ]
    2G6M X-ray 1.85 A/B 299-718 [» ]
    2G6N X-ray 1.90 A/B 299-718 [» ]
    2HX3 X-ray 2.00 A/B 297-718 [» ]
    2HX4 X-ray 2.15 A/B 297-718 [» ]
    3B3M X-ray 1.95 A/B 297-718 [» ]
    3B3N X-ray 1.98 A/B 297-718 [» ]
    3B3O X-ray 2.05 A/B 297-718 [» ]
    3B3P X-ray 2.45 A/B 297-718 [» ]
    3DQR X-ray 2.40 A/B 297-718 [» ]
    3FC5 X-ray 2.59 A/B 297-718 [» ]
    3HSN X-ray 1.91 A/B 297-718 [» ]
    3HSO X-ray 2.02 A/B 297-718 [» ]
    3HSP X-ray 2.20 A/B 297-718 [» ]
    3JT3 X-ray 2.15 A/B 297-718 [» ]
    3JT4 X-ray 1.80 A/B 297-718 [» ]
    3JT5 X-ray 2.10 A/B 297-718 [» ]
    3JT6 X-ray 2.20 A/B 297-718 [» ]
    3JT7 X-ray 2.10 A/B 297-718 [» ]
    3JT8 X-ray 1.95 A/B 297-718 [» ]
    3JT9 X-ray 2.10 A/B 297-718 [» ]
    3JTA X-ray 2.18 A/B 297-718 [» ]
    3JWS X-ray 1.95 A/B 297-718 [» ]
    3JWT X-ray 2.01 A/B 297-718 [» ]
    3JWU X-ray 1.93 A/B 297-718 [» ]
    3JWV X-ray 1.98 A/B 297-718 [» ]
    3JX0 X-ray 2.20 A/B 297-718 [» ]
    3JX1 X-ray 2.00 A/B 297-718 [» ]
    3JX2 X-ray 2.10 A/B 297-718 [» ]
    3JX3 X-ray 1.95 A/B 297-718 [» ]
    3JX4 X-ray 2.26 A/B 297-718 [» ]
    3JX5 X-ray 2.15 A/B 297-718 [» ]
    3JX6 X-ray 2.35 A/B 297-718 [» ]
    3N2R X-ray 1.90 A/B 297-718 [» ]
    3N5V X-ray 2.30 A/B 297-718 [» ]
    3N5W X-ray 1.73 A/B 297-718 [» ]
    3N5X X-ray 1.80 A/B 297-718 [» ]
    3N5Y X-ray 2.05 A/B 297-718 [» ]
    3N5Z X-ray 2.18 A/B 297-718 [» ]
    3N60 X-ray 1.98 A/B 297-718 [» ]
    3N61 X-ray 1.95 A/B 297-718 [» ]
    3N62 X-ray 1.95 A/B 297-718 [» ]
    3N63 X-ray 2.00 A/B 297-718 [» ]
    3N64 X-ray 1.95 A/B 297-718 [» ]
    3N65 X-ray 1.80 A/B 297-718 [» ]
    3N66 X-ray 1.78 A/B 297-718 [» ]
    3N67 X-ray 2.09 A/B 298-711 [» ]
    3N68 X-ray 2.53 A/B 298-711 [» ]
    3N69 X-ray 2.65 A/B 298-711 [» ]
    3N6A X-ray 2.49 A/B 298-711 [» ]
    3N6B X-ray 3.10 A/B 298-711 [» ]
    3N6C X-ray 3.06 A/B 298-711 [» ]
    3N6D X-ray 3.05 A/B 298-711 [» ]
    3N6E X-ray 2.20 A/B 298-711 [» ]
    3N6F X-ray 2.18 A/B 298-711 [» ]
    3N6G X-ray 2.21 A/B 298-711 [» ]
    3NLJ X-ray 2.20 A/B 297-718 [» ]
    3NLK X-ray 2.02 A/B 297-718 [» ]
    3NLM X-ray 1.85 A/B 297-718 [» ]
    3NLN X-ray 2.00 A/B 297-718 [» ]
    3NLO X-ray 2.30 A/B 297-718 [» ]
    3NLP X-ray 2.02 A/B 297-718 [» ]
    3NLQ X-ray 2.15 A/B 297-718 [» ]
    3NLR X-ray 2.10 A/B 297-718 [» ]
    3NLV X-ray 2.10 A/B 297-718 [» ]
    3NLW X-ray 2.10 A/B 297-718 [» ]
    3NLX X-ray 1.87 A/B 297-718 [» ]
    3NLY X-ray 1.99 A/B 297-718 [» ]
    3NLZ X-ray 1.92 A/B 297-718 [» ]
    3NM0 X-ray 1.81 A/B 297-718 [» ]
    3NNY X-ray 2.10 A/B 297-718 [» ]
    3NNZ X-ray 1.97 A/B 297-718 [» ]
    3PNE X-ray 1.97 A/B 297-718 [» ]
    3PNF X-ray 1.94 A/B 297-718 [» ]
    3PNG X-ray 1.88 A/B 297-718 [» ]
    3Q99 X-ray 2.15 A/B 297-718 [» ]
    3Q9A X-ray 2.24 A/B 297-718 [» ]
    3RQJ X-ray 1.84 A/B 297-718 [» ]
    3RQK X-ray 2.21 A/B 297-718 [» ]
    3RQL X-ray 1.93 A/B 297-718 [» ]
    3RQM X-ray 1.95 A/B 297-718 [» ]
    3RQN X-ray 1.95 A/B 297-718 [» ]
    3SVP X-ray 2.05 A/B 297-718 [» ]
    3SVQ X-ray 2.18 A/B 297-718 [» ]
    3TYL X-ray 1.90 A/B 297-718 [» ]
    3TYM X-ray 2.00 A/B 297-718 [» ]
    3TYN X-ray 1.97 A/B 297-718 [» ]
    3TYO X-ray 1.93 A/B 297-718 [» ]
    3UFO X-ray 2.17 A/B 297-718 [» ]
    3UFP X-ray 2.10 A/B 297-718 [» ]
    3UFQ X-ray 2.06 A/B 297-718 [» ]
    3UFR X-ray 2.10 A/B 297-718 [» ]
    3UFS X-ray 1.97 A/B 297-718 [» ]
    3UFT X-ray 2.08 A/B 297-718 [» ]
    3UFU X-ray 1.89 A/B 297-718 [» ]
    3UFV X-ray 2.08 A/B 297-718 [» ]
    3UFW X-ray 2.00 A/B 297-718 [» ]
    4C39 X-ray 1.98 A/B 297-718 [» ]
    4CAM X-ray 1.83 A/B 297-718 [» ]
    4CAN X-ray 1.91 A/B 297-718 [» ]
    4CAO X-ray 1.98 A/B 297-718 [» ]
    4CAP X-ray 2.06 A/B 297-718 [» ]
    4CAQ X-ray 1.95 A/B 297-718 [» ]
    4CDT X-ray 2.00 A/B 297-718 [» ]
    4CTP X-ray 2.05 A/B 297-718 [» ]
    4CTQ X-ray 2.00 A/B 297-718 [» ]
    4CTR X-ray 2.20 A/B 297-718 [» ]
    4CTT X-ray 2.30 A/B 297-718 [» ]
    4CTU X-ray 2.16 A/B 297-718 [» ]
    4CTV X-ray 1.78 A/B 297-718 [» ]
    4CTW X-ray 1.90 A/B 297-718 [» ]
    4CTX X-ray 1.82 A/B 297-718 [» ]
    4EUX X-ray 2.14 A/B 297-718 [» ]
    4FVW X-ray 1.81 A/B 297-718 [» ]
    4FVX X-ray 2.00 A/B 297-718 [» ]
    4FVY X-ray 1.70 A/B 297-718 [» ]
    4FVZ X-ray 1.99 A/B 297-718 [» ]
    4FW0 X-ray 1.95 A/B 297-718 [» ]
    4GQE X-ray 1.80 A/B 297-718 [» ]
    4HOP X-ray 2.29 B/D/F 4-126 [» ]
    4IMS X-ray 2.15 A/B 297-718 [» ]
    4IMT X-ray 2.20 A/B 297-718 [» ]
    4IMU X-ray 2.03 A/B 297-718 [» ]
    4IMW X-ray 2.20 A/B 297-718 [» ]
    4JSE X-ray 1.97 A/B 297-718 [» ]
    4JSF X-ray 2.05 A/B 297-718 [» ]
    4JSG X-ray 1.94 A/B 297-718 [» ]
    4JSH X-ray 2.35 A/B 297-718 [» ]
    4JSI X-ray 2.09 A/B 297-718 [» ]
    4JSJ X-ray 1.92 A/B 297-718 [» ]
    4K5D X-ray 2.10 A/B 297-718 [» ]
    4K5E X-ray 1.89 A/B 297-718 [» ]
    4K5F X-ray 2.20 A/B 297-718 [» ]
    4K5G X-ray 1.85 A/B 297-718 [» ]
    4KCH X-ray 2.15 A/B 297-718 [» ]
    4KCI X-ray 2.27 A/B 297-718 [» ]
    4KCJ X-ray 2.05 A/B 297-718 [» ]
    4KCK X-ray 2.10 A/B 297-718 [» ]
    4KCL X-ray 1.93 A/B 297-718 [» ]
    4KCM X-ray 2.07 A/B 297-718 [» ]
    4KCN X-ray 1.85 A/B 297-718 [» ]
    4KCO X-ray 1.86 A/B 297-718 [» ]
    4LUX X-ray 1.86 A/B 297-718 [» ]
    ProteinModelPortali P29476.
    SMRi P29476. Positions 12-126, 298-716, 750-1413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246738. 10 interactions.
    IntActi P29476. 6 interactions.
    MINTi MINT-89230.
    STRINGi 10116.ENSRNOP00000062735.

    Chemistry

    BindingDBi P29476.
    ChEMBLi CHEMBL3048.
    GuidetoPHARMACOLOGYi 1251.

    PTM databases

    PhosphoSitei P29476.

    Proteomic databases

    PaxDbi P29476.
    PRIDEi P29476.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24598.
    KEGGi rno:24598.
    UCSCi RGD:3184. rat. [P29476-1 ]

    Organism-specific databases

    CTDi 4842.
    RGDi 3184. Nos1.

    Phylogenomic databases

    eggNOGi COG4362.
    HOGENOMi HOG000220884.
    HOVERGENi HBG000159.
    InParanoidi P29476.
    KOi K13240.
    PhylomeDBi P29476.

    Enzyme and pathway databases

    SABIO-RK P29476.

    Miscellaneous databases

    EvolutionaryTracei P29476.
    NextBioi 603800.

    Gene expression databases

    Genevestigatori P29476.

    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. "Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase."
      Bredt D.S., Hwang P.M., Glatt C.L., Lowenstein C., Reed R.R., Snyder S.H.
      Nature 351:714-718(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Brain.
    2. "Cloning of a novel neuronal nitric oxide synthase expressed in penis and lower urinary tract."
      Magee T., Fuentes A.M., Garban H., Rajavashisth T., Marquez D., Rodriguez J.A., Rajfer J., Gonzalez-Cadavid N.F.
      Biochem. Biophys. Res. Commun. 226:145-151(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PNNOS).
      Strain: Fischer 344.
      Tissue: Penis.
    3. "Nitric oxide synthase from rat colorectum: purification, peptide sequencing, partial PCR cloning, and immunohistochemistry."
      Seo H.G., Tatsumi H., Fujii J., Nishikawa A., Suzuki K., Kangawa K., Taniguchi N.
      J. Biochem. 115:602-607(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 119-129; 132-142; 144-156; 189-200; 264-276; 305-310; 360-369; 376-379; 381-385; 387-396; 779-785; 953-963 AND 1131-1139, TISSUE SPECIFICITY.
      Tissue: Colon.
    4. "The identification of the pterin-binding domain in the nitric oxide synthase's sequence."
      Uvarov V.Y., Lyashenko A.A.
      Biochem. Biophys. Res. Commun. 206:736-741(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF TETRAHYDROBIOPTERIN-BINDING DOMAIN.
    5. "Unusual role of Tyr588 of neuronal nitric oxide synthase in controlling substrate specificity and electron transfer."
      Sato Y., Sagami I., Matsui T., Shimizu T.
      Biochem. Biophys. Res. Commun. 281:621-626(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-588.
    6. "Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON."
      Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.
      Neuron 28:183-193(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAPON AND RASD1.
    7. "Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON."
      Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H.
      Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAPON AND SYN1.
    8. "NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity."
      Saitoh F., Tian Q.B., Okano A., Sakagami H., Kondo H., Suzuki T.
      J. Biol. Chem. 279:29461-29468(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZDHHC23.
    9. "Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase."
      Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M., Patterson C., Pratt W.B., Osawa Y.
      J. Biol. Chem. 279:52970-52977(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    10. "Nitric oxide synthase (NOS)-interacting protein interacts with neuronal NOS and regulates its distribution and activity."
      Dreyer J., Schleicher M., Tappe A., Schilling K., Kuner T., Kusumawidijaja G., Mueller-Esterl W., Oess S., Kuner R.
      J. Neurosci. 24:10454-10465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOSIP, ENZYME REGULATION, SUBCELLULAR LOCATION.
    11. "Binding of Vac14 to neuronal nitric oxide synthase: Characterisation of a new internal PDZ-recognition motif."
      Lemaire J.F., McPherson P.S.
      FEBS Lett. 580:6948-6954(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VAC14, DOMAIN.
    12. "Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled receptor 30 (GPR30), an estrogen receptor that can be identified in hippocampal dendritic spines."
      Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.
      J. Biol. Chem. 288:6438-6450(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG4.
    13. "Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex."
      Hillier B.J., Christopherson K.S., Prehoda K.E., Bredt D.S., Lim W.A.
      Science 284:812-815(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 14-125.
    14. "Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with nadph-cytochrome p450 oxidoreductase."
      Zhang J., Martasek P., Paschke R., Shea T., Masters B.S.S., Kim J.-J.P.
      J. Biol. Chem. 276:37506-37513(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 963-1397.

    Entry informationi

    Entry nameiNOS1_RAT
    AccessioniPrimary (citable) accession number: P29476
    Secondary accession number(s): P70594
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 171 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3