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P29476

- NOS1_RAT

UniProt

P29476 - NOS1_RAT

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Protein
Nitric oxide synthase, brain
Gene
Nos1, Bnos
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.

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.1 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 – 91232FMN By similarity
Add
BLAST
Nucleotide bindingi1027 – 103812FAD By similarity
Add
BLAST
Nucleotide bindingi1170 – 118011FAD By similarity
Add
BLAST
Nucleotide bindingi1245 – 126319NADP By similarity
Add
BLAST
Nucleotide bindingi1343 – 135816NADP By similarity
Add
BLAST

GO - Molecular functioni

  1. FMN binding Source: BHF-UCL
  2. NADP binding Source: BHF-UCL
  3. NADPH-hemoprotein reductase activity Source: RefGenome
  4. amino acid binding Source: RGD
  5. cadmium ion binding Source: BHF-UCL
  6. calmodulin binding Source: RGD
  7. enzyme binding Source: RGD
  8. flavin adenine dinucleotide binding Source: BHF-UCL
  9. heme binding Source: BHF-UCL
  10. ion channel binding Source: BHF-UCL
  11. iron ion binding Source: InterPro
  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
Complete GO annotation...

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; 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.1 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
Complete GO annotation...

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, brain
PRO_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).6 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

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.

Miscellaneous databases

EvolutionaryTraceiP29476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9983PDZ
Add
BLAST
Domaini755 – 935181Flavodoxin-like
Add
BLAST
Domaini990 – 1237248FAD-binding FR-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 200200Interaction with NOSIP
Add
BLAST
Regioni163 – 24078PIN (nNOS-inhibiting protein) binding By similarity
Add
BLAST
Regioni725 – 74521Calmodulin-binding Reviewed prediction
Add
BLAST
Regioni750 – 76920Tetrahydrobiopterin-binding
Add
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 VAC14.2 Publications

Sequence similaritiesi

Belongs to the NOS family.
Contains 1 PDZ (DHR) domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei504 – 608105Missing in isoform N-NOS-2.
VSP_003580Add
BLAST
Alternative sequencei839 – 8391K → KYPEPLRFFPRKGPSLSHVD SEAHSLVAARDSQHR in isoform PNNOS.
VSP_003581

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691I → V in AAC52782. 1 Publication
Sequence conflicti269 – 2691I → V AA sequence 1 Publication
Sequence conflicti953 – 9531P → A in AAC52782. 1 Publication
Sequence conflicti953 – 9531P → A AA sequence 1 Publication
Sequence conflicti1008 – 10081F → S in AAC52782. 1 Publication
Sequence conflicti1311 – 13111A → V in AAC52782. 1 Publication

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: September 3, 2014
This is version 170 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

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