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P29476 (NOS1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Nos1
Synonyms:Bnos
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1429 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

Cofactor

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 regulation

Stimulated by calcium/calmodulin. Inhibited by n-Nos-inhibiting protein (PIN) which may prevent the dimerization of the protein By similarity. Inhibited by NOSIP. Ref.10

Subunit structure

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). Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12

Subcellular location

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. Ref.10

Tissue specificity

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. Ref.3

Domain

The PDZ domain in the N-terminal part of the neuronal isoform participatesin protein-protein interaction, and is responsible for targeting nNos to synaptic membranes in muscles By similarity. Mediates interaction with VAC14. Ref.4 Ref.11

Post-translational modification

Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro). Ref.9

Sequence similarities

Belongs to the NOS family.

Contains 1 FAD-binding FR-type domain.

Contains 1 flavodoxin-like domain.

Contains 1 PDZ (DHR) domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
   LigandCalmodulin-binding
FAD
Flavoprotein
FMN
Heme
Iron
Metal-binding
NADP
   Molecular functionOxidoreductase
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from expression pattern PubMed 17683464. Source: RGD

arginine catabolic process

Inferred from direct assay PubMed 1383204. Source: BHF-UCL

behavioral response to cocaine

Inferred from mutant phenotype PubMed 23579428. Source: RGD

cellular response to mechanical stimulus

Inferred from mutant phenotype PubMed 23619128. Source: RGD

female pregnancy

Inferred from expression pattern PubMed 20630934PubMed 23283939. Source: RGD

muscle contraction

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 20596694. Source: RGD

negative regulation of blood pressure

Inferred from mutant phenotype PubMed 15331368. Source: RGD

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 20338922. Source: RGD

negative regulation of cytosolic calcium ion concentration

Inferred from mutant phenotype PubMed 23172925. Source: RGD

negative regulation of heart contraction

Inferred from mutant phenotype PubMed 15331368. Source: RGD

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 17130471. Source: RGD

negative regulation of vasoconstriction

Inferred from mutant phenotype PubMed 23640592. Source: RGD

nitric oxide biosynthetic process

Inferred from direct assay PubMed 1383204. Source: BHF-UCL

nitric oxide mediated signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

peptidyl-cysteine S-nitrosylation

Inferred from direct assay PubMed 18591664. Source: BHF-UCL

positive regulation of guanylate cyclase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of long-term synaptic potentiation

Inferred from mutant phenotype PubMed 23579428. Source: RGD

positive regulation of neuron death

Inferred from mutant phenotype PubMed 23062100. Source: RGD

positive regulation of sodium ion transmembrane transport

Inferred from mutant phenotype PubMed 18591664. Source: BHF-UCL

positive regulation of vasodilation

Inferred from mutant phenotype PubMed 17291465. Source: RGD

regulation of heart contraction

Inferred from mutant phenotype PubMed 16537391. Source: RGD

regulation of sensory perception of pain

Inferred from mutant phenotype PubMed 17101217. Source: RGD

response to activity

Inferred from expression pattern PubMed 19793134. Source: RGD

response to estrogen

Inferred from direct assay PubMed 17553983. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 16737454. Source: RGD

response to heat

Inferred from expression pattern PubMed 16950411. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16276418. Source: BHF-UCL

response to lead ion

Inferred from expression pattern PubMed 19524414. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 20724006. Source: RGD

response to nicotine

Inferred from expression pattern PubMed 21050840. Source: RGD

response to nitric oxide

Inferred from expression pattern PubMed 20473255. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 20079408. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 17611313. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 17310378. Source: RGD

response to peptide hormone

Inferred from mutant phenotype PubMed 20181617. Source: RGD

response to vitamin E

Inferred from expression pattern PubMed 17200156. Source: RGD

   Cellular_componentazurophil granule

Inferred from direct assay PubMed 16387842. Source: RGD

cytoplasm

Inferred from direct assay PubMed 12526033PubMed 16387842. Source: RGD

cytosol

Inferred from direct assay PubMed 16361261. Source: RGD

dendrite

Inferred from direct assay PubMed 12526033. Source: RGD

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 21490139. Source: RGD

mitochondrial outer membrane

Inferred from direct assay PubMed 12526033. Source: RGD

mitochondrion

Inferred from direct assay PubMed 16537391. Source: MGI

nuclear membrane

Inferred from direct assay PubMed 16387842. Source: RGD

nucleus

Inferred from direct assay PubMed 16387842. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17027776. Source: BHF-UCL

photoreceptor inner segment

Inferred from direct assay PubMed 17027776. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 16387842. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 11226670. Source: RGD

protein complex

Inferred from direct assay PubMed 18591664. Source: BHF-UCL

sarcolemma

Inferred from direct assay PubMed 7527495. Source: BHF-UCL

synapse

Inferred from direct assay PubMed 12526033. Source: RGD

vesicle membrane

Inferred from direct assay PubMed 21448354. Source: RGD

   Molecular_functionFMN binding

Inferred from direct assay PubMed 1383204PubMed 17029414. Source: BHF-UCL

NADP binding

Inferred from direct assay PubMed 17029414. Source: BHF-UCL

NADPH-hemoprotein reductase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

amino acid binding

Traceable author statement PubMed 14966111. Source: RGD

cadmium ion binding

Inferred from direct assay PubMed 17029414. Source: BHF-UCL

calmodulin binding

Inferred from direct assay PubMed 14966111PubMed 20529840. Source: RGD

enzyme binding

Inferred from physical interaction PubMed 16537391. Source: RGD

flavin adenine dinucleotide binding

Inferred from direct assay PubMed 1383204PubMed 17029414. Source: BHF-UCL

heme binding

Inferred from direct assay PubMed 1383204. Source: BHF-UCL

ion channel binding

Inferred from physical interaction PubMed 18591664. Source: BHF-UCL

iron ion binding

Inferred from electronic annotation. Source: InterPro

nitric-oxide synthase activity

Inferred from direct assay PubMed 1383204PubMed 17029414PubMed 18591664. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.6Ref.7PubMed 9459447. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 17347455PubMed 23832698. Source: RGD

scaffold protein binding

Inferred from physical interaction PubMed 18591664. Source: BHF-UCL

sodium channel regulator activity

Inferred from mutant phenotype PubMed 18591664. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CALMP621572EBI-349460,EBI-397403From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform N-NOS-1 (identifier: P29476-1)

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.
Isoform N-NOS-2 (identifier: P29476-2)

The sequence of this isoform differs from the canonical sequence as follows:
     504-608: Missing.
Isoform PNNOS (identifier: P29476-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14291429Nitric oxide synthase, brain
PRO_0000170924

Regions

Domain17 – 9983PDZ
Domain755 – 935181Flavodoxin-like
Domain990 – 1237248FAD-binding FR-type
Nucleotide binding881 – 91232FMN By similarity
Nucleotide binding1027 – 103812FAD By similarity
Nucleotide binding1170 – 118011FAD By similarity
Nucleotide binding1245 – 126319NADP By similarity
Nucleotide binding1343 – 135816NADP By similarity
Region1 – 200200Interaction with NOSIP
Region163 – 24078PIN (nNOS-inhibiting protein) binding By similarity
Region725 – 74521Calmodulin-binding Potential
Region750 – 76920Tetrahydrobiopterin-binding

Sites

Metal binding4151Iron (heme axial ligand) By similarity
Binding site5881Substrate

Natural variations

Alternative sequence504 – 608105Missing in isoform N-NOS-2.
VSP_003580
Alternative sequence8391K → KYPEPLRFFPRKGPSLSHVD SEAHSLVAARDSQHR in isoform PNNOS.
VSP_003581

Experimental info

Mutagenesis5881Y → F: No decrease in activity. Ref.5
Mutagenesis5881Y → H: 50% decrease of activity. Ref.5
Mutagenesis5881Y → S: 30% decrease of activity. Ref.5
Sequence conflict2691I → V in AAC52782. Ref.2
Sequence conflict2691I → V AA sequence Ref.3
Sequence conflict9531P → A in AAC52782. Ref.2
Sequence conflict9531P → A AA sequence Ref.3
Sequence conflict10081F → S in AAC52782. Ref.2
Sequence conflict13111A → V in AAC52782. Ref.2

Secondary structure

....................................................................................................................................................................................................................................... 1429
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform N-NOS-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 7255C5AE165200F5

FASTA1,429160,559
        10         20         30         40         50         60 
MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA 

        70         80         90        100        110        120 
GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI 

       130        140        150        160        170        180 
RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI 

       190        200        210        220        230        240 
DPTMKSTKAN LQDIGEHDEL LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD 

       250        260        270        280        290        300 
GKSHKAPPLG GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF 

       310        320        330        340        350        360 
LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT KDQLFPLAKE 

       370        380        390        400        410        420 
FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ 

       430        440        450        460        470        480 
WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI 

       490        500        510        520        530        540 
RYAGYKQPDG STLGDPANVQ FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL 

       550        560        570        580        590        600 
VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD 

       610        620        630        640        650        660 
NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK 

       670        680        690        700        710        720 
HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN 

       730        740        750        760        770        780 
GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA 

       790        800        810        820        830        840 
FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS 

       850        860        870        880        890        900 
YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD 

       910        920        930        940        950        960 
TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKPNNSLISN 

       970        980        990       1000       1010       1020 
DRSWKRNKFR LTYVAEAPDL TQGLSNVHKK RVSAARLLSR QNLQSPKFSR STIFVRLHTN 

      1030       1040       1050       1060       1070       1080 
GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK 

      1090       1100       1110       1120       1130       1140 
DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW 

      1150       1160       1170       1180       1190       1200 
GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR 

      1210       1220       1230       1240       1250       1260 
DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW 

      1270       1280       1290       1300       1310       1320 
QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK 

      1330       1340       1350       1360       1370       1380 
KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF 

      1390       1400       1410       1420 
ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDADEVFSS 

« Hide

Isoform N-NOS-2 [UniParc].

Checksum: 2B527386DF5B4160
Show »

FASTA1,324148,548
Isoform PNNOS [UniParc].

Checksum: A0522B26817B6705
Show »

FASTA1,463164,430

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59949 mRNA. Translation: CAA42574.1.
U67309 mRNA. Translation: AAC52782.1.
PIRS16233.
RefSeqNP_434686.1. NM_052799.1.
UniGeneRn.10573.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP29476.
SMRP29476. Positions 12-126, 298-716, 750-1413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246738. 10 interactions.
IntActP29476. 6 interactions.
MINTMINT-89230.
STRING10116.ENSRNOP00000062735.

Chemistry

BindingDBP29476.
ChEMBLCHEMBL3048.
GuidetoPHARMACOLOGY1251.

PTM databases

PhosphoSiteP29476.

Proteomic databases

PaxDbP29476.
PRIDEP29476.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24598.
KEGGrno:24598.
UCSCRGD:3184. rat. [P29476-1]

Organism-specific databases

CTD4842.
RGD3184. Nos1.

Phylogenomic databases

eggNOGCOG4362.
HOGENOMHOG000220884.
HOVERGENHBG000159.
InParanoidP29476.
KOK13240.
PhylomeDBP29476.

Enzyme and pathway databases

SABIO-RKP29476.

Gene expression databases

GenevestigatorP29476.

Family and domain databases

Gene3D1.20.990.10. 1 hit.
2.30.42.10. 1 hit.
3.40.50.360. 2 hits.
3.90.340.10. 1 hit.
InterProIPR003097. 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.
IPR004030. NO_synthase_oxygenase_dom.
IPR012144. NOS_euk.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001478. PDZ.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamPF00667. 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]
PIRSFPIRSF000333. NOS. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SMARTSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMSSF50156. SSF50156. 1 hit.
SSF52218. SSF52218. 1 hit.
SSF56512. SSF56512. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
PS60001. NOS. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29476.
NextBio603800.

Entry information

Entry nameNOS1_RAT
AccessionPrimary (citable) accession number: P29476
Secondary accession number(s): P70594
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references