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Protein

Nitric oxide synthase, brain

Gene

Nos1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • hemeBy similarity
  • FADBy similarityNote: Binds 1 FAD.By similarity
  • FMNBy similarityNote: Binds 1 FMN.By similarity
  • 5,6,7,8-tetrahydrobiopterinBy similarityNote: 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.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi415Iron (heme axial ligand)By similarity1
Binding sitei588Substrate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi881 – 912FMNPROSITE-ProRule annotationAdd BLAST32
Nucleotide bindingi1027 – 1038FADBy similarityAdd BLAST12
Nucleotide bindingi1170 – 1180FADBy similarityAdd BLAST11
Nucleotide bindingi1245 – 1263NADPBy similarityAdd BLAST19
Nucleotide bindingi1343 – 1358NADPBy similarityAdd BLAST16

GO - Molecular functioni

  • amino acid binding Source: RGD
  • ATPase binding Source: BHF-UCL
  • cadmium ion binding Source: BHF-UCL
  • calmodulin binding Source: RGD
  • enzyme binding Source: RGD
  • flavin adenine dinucleotide binding Source: BHF-UCL
  • FMN binding Source: BHF-UCL
  • heme binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • iron ion binding Source: InterPro
  • NADP binding Source: BHF-UCL
  • nitric-oxide synthase activity Source: BHF-UCL
  • protein homodimerization activity Source: RGD
  • scaffold protein binding Source: BHF-UCL
  • sodium channel regulator activity Source: BHF-UCL

GO - Biological processi

  • aging Source: RGD
  • arginine catabolic process Source: BHF-UCL
  • behavioral response to cocaine Source: RGD
  • cellular response to epinephrine stimulus Source: BHF-UCL
  • cellular response to mechanical stimulus Source: RGD
  • female pregnancy Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of blood pressure Source: RGD
  • negative regulation of cell proliferation Source: RGD
  • negative regulation of cytosolic calcium ion concentration Source: RGD
  • negative regulation of heart contraction Source: RGD
  • negative regulation of insulin secretion Source: RGD
  • negative regulation of peptidyl-serine phosphorylation Source: BHF-UCL
  • negative regulation of vasoconstriction Source: RGD
  • nitric oxide biosynthetic process Source: BHF-UCL
  • nitric oxide mediated signal transduction Source: BHF-UCL
  • peptidyl-cysteine S-nitrosylation Source: BHF-UCL
  • positive regulation of guanylate cyclase activity Source: GO_Central
  • positive regulation of long-term synaptic potentiation Source: RGD
  • positive regulation of neuron death Source: RGD
  • positive regulation of sodium ion transmembrane transport Source: BHF-UCL
  • positive regulation of vasodilation Source: RGD
  • regulation of heart contraction Source: RGD
  • regulation of sensory perception of pain Source: RGD
  • response to activity Source: RGD
  • response to estrogen Source: RGD
  • response to ethanol Source: RGD
  • response to heat Source: RGD
  • response to hypoxia Source: BHF-UCL
  • response to lead ion Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to nicotine Source: RGD
  • response to nitric oxide Source: RGD
  • response to nutrient levels Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD
  • response to peptide hormone Source: RGD
  • 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

BRENDAi1.14.13.39. 5301.
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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3184. Nos1.

Subcellular locationi

GO - Cellular componenti

  • azurophil granule Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • dendrite Source: RGD
  • dendritic spine Source: UniProtKB-SubCell
  • membrane Source: RGD
  • mitochondrial outer membrane Source: RGD
  • mitochondrion Source: RGD
  • nuclear membrane Source: RGD
  • nucleus Source: RGD
  • perinuclear region of cytoplasm Source: BHF-UCL
  • photoreceptor inner segment Source: BHF-UCL
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • protein complex Source: BHF-UCL
  • sarcolemma Source: BHF-UCL
  • synapse Source: RGD
  • vesicle membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi588Y → F: No decrease in activity. 1 Publication1
Mutagenesisi588Y → H: 50% decrease of activity. 1 Publication1
Mutagenesisi588Y → S: 30% decrease of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3048.
GuidetoPHARMACOLOGYi1251.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709241 – 1429Nitric oxide synthase, brainAdd BLAST1429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei280PhosphoserineBy similarity1
Modified residuei847PhosphoserineCombined sources1
Modified residuei857PhosphoserineBy similarity1
Modified residuei858PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP29476.
PRIDEiP29476.

PTM databases

iPTMnetiP29476.
PhosphoSitePlusiP29476.

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

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.

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • calmodulin binding Source: RGD
  • enzyme binding Source: RGD
  • ion channel binding Source: BHF-UCL
  • protein homodimerization activity Source: RGD
  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi246738. 11 interactors.
DIPiDIP-33272N.
IntActiP29476. 7 interactors.
MINTiMINT-89230.
STRINGi10116.ENSRNOP00000062735.

Chemistry databases

BindingDBiP29476.

Structurei

Secondary structure

11429
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 12Combined sources4
Beta strandi15 – 21Combined sources7
Turni24 – 26Combined sources3
Beta strandi29 – 34Combined sources6
Beta strandi36 – 39Combined sources4
Beta strandi41 – 46Combined sources6
Helixi51 – 55Combined sources5
Turni60 – 62Combined sources3
Beta strandi63 – 67Combined sources5
Beta strandi73 – 75Combined sources3
Helixi77 – 86Combined sources10
Beta strandi89 – 98Combined sources10
Beta strandi103 – 111Combined sources9
Beta strandi113 – 115Combined sources3
Beta strandi117 – 124Combined sources8
Beta strandi228 – 236Combined sources9
Beta strandi301 – 305Combined sources5
Turni306 – 308Combined sources3
Beta strandi311 – 314Combined sources4
Helixi316 – 319Combined sources4
Beta strandi328 – 331Combined sources4
Beta strandi340 – 342Combined sources3
Beta strandi345 – 347Combined sources3
Helixi351 – 368Combined sources18
Beta strandi372 – 374Combined sources3
Helixi375 – 391Combined sources17
Helixi398 – 410Combined sources13
Helixi418 – 420Combined sources3
Beta strandi425 – 428Combined sources4
Helixi435 – 450Combined sources16
Helixi451 – 453Combined sources3
Beta strandi458 – 461Combined sources4
Beta strandi466 – 470Combined sources5
Beta strandi476 – 480Combined sources5
Beta strandi484 – 486Combined sources3
Beta strandi490 – 494Combined sources5
Helixi496 – 498Combined sources3
Helixi499 – 507Combined sources9
Beta strandi515 – 517Combined sources3
Beta strandi522 – 525Combined sources4
Beta strandi527 – 529Combined sources3
Beta strandi532 – 534Combined sources3
Helixi538 – 540Combined sources3
Beta strandi543 – 545Combined sources3
Helixi554 – 557Combined sources4
Beta strandi560 – 563Combined sources4
Beta strandi571 – 574Combined sources4
Beta strandi577 – 580Combined sources4
Helixi590 – 594Combined sources5
Helixi596 – 599Combined sources4
Turni601 – 604Combined sources4
Helixi607 – 613Combined sources7
Helixi621 – 623Combined sources3
Helixi625 – 643Combined sources19
Helixi651 – 669Combined sources19
Helixi676 – 679Combined sources4
Beta strandi682 – 684Combined sources3
Helixi685 – 687Combined sources3
Helixi689 – 692Combined sources4
Beta strandi696 – 698Combined sources3
Beta strandi701 – 705Combined sources5
Helixi710 – 713Combined sources4
Beta strandi754 – 760Combined sources7
Beta strandi762 – 764Combined sources3
Helixi765 – 777Combined sources13
Turni778 – 780Combined sources3
Beta strandi781 – 787Combined sources7
Turni788 – 790Combined sources3
Helixi796 – 798Combined sources3
Beta strandi800 – 806Combined sources7
Turni810 – 812Combined sources3
Helixi816 – 818Combined sources3
Helixi819 – 828Combined sources10
Helixi841 – 844Combined sources4
Turni873 – 876Combined sources4
Beta strandi878 – 885Combined sources8
Beta strandi889 – 891Combined sources3
Helixi894 – 905Combined sources12
Beta strandi909 – 912Combined sources4
Beta strandi915 – 918Combined sources4
Turni919 – 922Combined sources4
Helixi923 – 942Combined sources20
Beta strandi946 – 948Combined sources3
Beta strandi961 – 963Combined sources3
Beta strandi968 – 973Combined sources6
Helixi980 – 988Combined sources9
Beta strandi993 – 1002Combined sources10
Beta strandi1012 – 1018Combined sources7
Helixi1023 – 1025Combined sources3
Beta strandi1032 – 1035Combined sources4
Helixi1041 – 1048Combined sources8
Beta strandi1051 – 1053Combined sources3
Beta strandi1061 – 1072Combined sources12
Beta strandi1076 – 1081Combined sources6
Helixi1090 – 1096Combined sources7
Helixi1106 – 1113Combined sources8
Helixi1119 – 1128Combined sources10
Helixi1133 – 1142Combined sources10
Helixi1146 – 1152Combined sources7
Helixi1160 – 1166Combined sources7
Beta strandi1173 – 1176Combined sources4
Turni1181 – 1183Combined sources3
Beta strandi1187 – 1193Combined sources7
Beta strandi1196 – 1198Combined sources3
Helixi1200 – 1202Combined sources3
Beta strandi1206 – 1208Combined sources3
Helixi1210 – 1215Combined sources6
Beta strandi1223 – 1229Combined sources7
Helixi1232 – 1234Combined sources3
Beta strandi1244 – 1247Combined sources4
Helixi1250 – 1253Combined sources4
Helixi1254 – 1270Combined sources17
Beta strandi1277 – 1284Combined sources8
Turni1286 – 1288Combined sources3
Helixi1293 – 1301Combined sources9
Beta strandi1304 – 1314Combined sources11
Helixi1323 – 1330Combined sources8
Helixi1332 – 1340Combined sources9
Beta strandi1345 – 1350Combined sources6
Helixi1352 – 1369Combined sources18
Helixi1374 – 1386Combined sources13
Beta strandi1390 – 1394Combined sources5
Helixi1401 – 1411Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4CX3X-ray1.97A/B297-718[»]
4CX4X-ray1.98A/B297-718[»]
4CX5X-ray1.80A/B297-718[»]
4CX6X-ray1.90A/B297-718[»]
4D2YX-ray1.98A/B297-718[»]
4D2ZX-ray1.89A/B297-718[»]
4D30X-ray1.96A/B297-718[»]
4D31X-ray1.95A/B297-718[»]
4D32X-ray2.10A/B297-718[»]
4D3BX-ray1.80A/B297-718[»]
4D7OX-ray1.78A/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[»]
4UGZX-ray2.08A/B297-718[»]
4UH0X-ray2.04A/B297-718[»]
4UH1X-ray1.80A/B297-718[»]
4UH2X-ray1.99A/B297-718[»]
4UH3X-ray2.03A/B297-718[»]
4UH4X-ray1.95A/B297-718[»]
4UPMX-ray1.90A/B297-718[»]
4UPNX-ray2.09A/B297-718[»]
4UPOX-ray1.95A/B297-718[»]
4UPPX-ray1.91A/B297-718[»]
4V3VX-ray2.06A/B297-718[»]
4V3WX-ray2.13A/B297-718[»]
4V3XX-ray1.99A/B297-718[»]
4V3YX-ray1.96A/B297-718[»]
4V3ZX-ray2.05A/B297-718[»]
5AD4X-ray1.98A/B297-718[»]
5AD5X-ray1.90A/B297-718[»]
5AD6X-ray2.00A/B297-718[»]
5AD7X-ray1.95A/B297-718[»]
5AD8X-ray1.91A/B297-718[»]
5AD9X-ray2.30A/B297-718[»]
5ADAX-ray1.98A/B297-718[»]
5ADBX-ray2.05A/B297-718[»]
5ADCX-ray2.10A/B297-718[»]
5ADDX-ray2.10A/B297-718[»]
5ADEX-ray2.10A/B297-718[»]
5AGKX-ray2.00A/B297-718[»]
5AGLX-ray1.94A/B297-718[»]
5AGMX-ray1.84A/B297-718[»]
5AGNX-ray1.95A/B297-718[»]
5AGOX-ray1.90A/B297-718[»]
5AGPX-ray2.10A/B297-718[»]
5FVOX-ray2.12A297-718[»]
5FVPX-ray2.10A/B297-718[»]
5FVQX-ray1.95A/B297-718[»]
5FVRX-ray1.84A/B297-718[»]
5FVSX-ray1.95A/B297-718[»]
5FVTX-ray1.83A/B297-718[»]
5FW0X-ray1.80A/B297-718[»]
5G0NX-ray1.94A/B297-718[»]
5G0OX-ray1.85A/B297-718[»]
5G0PX-ray2.10A/B297-718[»]
ProteinModelPortaliP29476.
SMRiP29476.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29476.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 99PDZPROSITE-ProRule annotationAdd BLAST83
Domaini755 – 935Flavodoxin-likePROSITE-ProRule annotationAdd BLAST181
Domaini990 – 1237FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST248

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 200Interaction with NOSIP1 PublicationAdd BLAST200
Regioni163 – 240PIN (nNOS-inhibiting protein) bindingBy similarityAdd BLAST78
Regioni725 – 745Calmodulin-bindingSequence analysisAdd BLAST21
Regioni750 – 769Tetrahydrobiopterin-bindingAdd BLAST20

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

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
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-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG
60 70 80 90 100
AAEQSGLIQA GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP
110 120 130 140 150
EGFTTHLETT FTGDGTPKTI RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD
160 170 180 190 200
RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI DPTMKSTKAN LQDIGEHDEL
210 220 230 240 250
LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD GKSHKAPPLG
260 270 280 290 300
GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF
310 320 330 340 350
LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT
360 370 380 390 400
KDQLFPLAKE FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE
410 420 430 440 450
LIYGAKHAWR NASRCVGRIQ WSKLQVFDAR DCTTAHGMFN YICNHVKYAT
460 470 480 490 500
NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI RYAGYKQPDG STLGDPANVQ
510 520 530 540 550
FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL VLEVPIRHPK
560 570 580 590 600
FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD
610 620 630 640 650
NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD
660 670 680 690 700
HHSATESFIK HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL
710 720 730 740 750
TPSFEYQPDP WNTHVWKGTN GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA
760 770 780 790 800
KRVKATILYA TETGKSQAYA KTLCEIFKHA FDAKAMSMEE YDIVHLEHEA
810 820 830 840 850
LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS YKVRFNSVSS
860 870 880 890 900
YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD
910 920 930 940 950
TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI
960 970 980 990 1000
EKPNNSLISN DRSWKRNKFR LTYVAEAPDL TQGLSNVHKK RVSAARLLSR
1010 1020 1030 1040 1050
QNLQSPKFSR STIFVRLHTN GNQELQYQPG DHLGVFPGNH EDLVNALIER
1060 1070 1080 1090 1100
LEDAPPANHV VKVEMLEERN TALGVISNWK DESRLPPCTI FQAFKYYLDI
1110 1120 1130 1140 1150
TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW GKNPTMVEVL
1160 1170 1180 1190 1200
EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR
1210 1220 1230 1240 1250
DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG
1260 1270 1280 1290 1300
TGIAPFRSFW QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK
1310 1320 1330 1340 1350
NKGVFRELYT AYSREPDRPK KYVQDVLQEQ LAESVYRALK EQGGHIYVCG
1360 1370 1380 1390 1400
DVTMAADVLK AIQRIMTQQG KLSEEDAGVF ISRLRDDNRY HEDIFGVTLR
1410 1420
TYEVTNRLRS ESIAFIEESK KDADEVFSS
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)DescriptionActionsGraphical viewLength
Sequence conflicti269I → V in AAC52782 (PubMed:8806605).Curated1
Sequence conflicti269I → V AA sequence (PubMed:7520037).Curated1
Sequence conflicti953P → A in AAC52782 (PubMed:8806605).Curated1
Sequence conflicti953P → A AA sequence (PubMed:7520037).Curated1
Sequence conflicti1008F → S in AAC52782 (PubMed:8806605).Curated1
Sequence conflicti1311A → V in AAC52782 (PubMed:8806605).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003580504 – 608Missing in isoform N-NOS-2. CuratedAdd BLAST105
Alternative sequenceiVSP_003581839K → KYPEPLRFFPRKGPSLSHVD SEAHSLVAARDSQHR in isoform PNNOS. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59949 mRNA. Translation: CAA42574.1.
U67309 mRNA. Translation: AAC52782.1.
PIRiS16233.
RefSeqiNP_434686.1. NM_052799.1.
UniGeneiRn.10573.
Rn.214189.
Rn.214216.

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:
EMBLi
GenBanki
DDBJi
Links Updated
X59949 mRNA. Translation: CAA42574.1.
U67309 mRNA. Translation: AAC52782.1.
PIRiS16233.
RefSeqiNP_434686.1. NM_052799.1.
UniGeneiRn.10573.
Rn.214189.
Rn.214216.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4CX3X-ray1.97A/B297-718[»]
4CX4X-ray1.98A/B297-718[»]
4CX5X-ray1.80A/B297-718[»]
4CX6X-ray1.90A/B297-718[»]
4D2YX-ray1.98A/B297-718[»]
4D2ZX-ray1.89A/B297-718[»]
4D30X-ray1.96A/B297-718[»]
4D31X-ray1.95A/B297-718[»]
4D32X-ray2.10A/B297-718[»]
4D3BX-ray1.80A/B297-718[»]
4D7OX-ray1.78A/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[»]
4UGZX-ray2.08A/B297-718[»]
4UH0X-ray2.04A/B297-718[»]
4UH1X-ray1.80A/B297-718[»]
4UH2X-ray1.99A/B297-718[»]
4UH3X-ray2.03A/B297-718[»]
4UH4X-ray1.95A/B297-718[»]
4UPMX-ray1.90A/B297-718[»]
4UPNX-ray2.09A/B297-718[»]
4UPOX-ray1.95A/B297-718[»]
4UPPX-ray1.91A/B297-718[»]
4V3VX-ray2.06A/B297-718[»]
4V3WX-ray2.13A/B297-718[»]
4V3XX-ray1.99A/B297-718[»]
4V3YX-ray1.96A/B297-718[»]
4V3ZX-ray2.05A/B297-718[»]
5AD4X-ray1.98A/B297-718[»]
5AD5X-ray1.90A/B297-718[»]
5AD6X-ray2.00A/B297-718[»]
5AD7X-ray1.95A/B297-718[»]
5AD8X-ray1.91A/B297-718[»]
5AD9X-ray2.30A/B297-718[»]
5ADAX-ray1.98A/B297-718[»]
5ADBX-ray2.05A/B297-718[»]
5ADCX-ray2.10A/B297-718[»]
5ADDX-ray2.10A/B297-718[»]
5ADEX-ray2.10A/B297-718[»]
5AGKX-ray2.00A/B297-718[»]
5AGLX-ray1.94A/B297-718[»]
5AGMX-ray1.84A/B297-718[»]
5AGNX-ray1.95A/B297-718[»]
5AGOX-ray1.90A/B297-718[»]
5AGPX-ray2.10A/B297-718[»]
5FVOX-ray2.12A297-718[»]
5FVPX-ray2.10A/B297-718[»]
5FVQX-ray1.95A/B297-718[»]
5FVRX-ray1.84A/B297-718[»]
5FVSX-ray1.95A/B297-718[»]
5FVTX-ray1.83A/B297-718[»]
5FW0X-ray1.80A/B297-718[»]
5G0NX-ray1.94A/B297-718[»]
5G0OX-ray1.85A/B297-718[»]
5G0PX-ray2.10A/B297-718[»]
ProteinModelPortaliP29476.
SMRiP29476.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246738. 11 interactors.
DIPiDIP-33272N.
IntActiP29476. 7 interactors.
MINTiMINT-89230.
STRINGi10116.ENSRNOP00000062735.

Chemistry databases

BindingDBiP29476.
ChEMBLiCHEMBL3048.
GuidetoPHARMACOLOGYi1251.

PTM databases

iPTMnetiP29476.
PhosphoSitePlusiP29476.

Proteomic databases

PaxDbiP29476.
PRIDEiP29476.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4842.
RGDi3184. Nos1.

Phylogenomic databases

eggNOGiKOG1158. Eukaryota.
COG0369. LUCA.
COG4362. LUCA.
HOGENOMiHOG000220884.
HOVERGENiHBG000159.
InParanoidiP29476.
KOiK13240.
PhylomeDBiP29476.

Enzyme and pathway databases

BRENDAi1.14.13.39. 5301.
SABIO-RKP29476.

Miscellaneous databases

EvolutionaryTraceiP29476.
PROiP29476.

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-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like_dom.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.