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Nitric oxide synthase, brain (EC 1.14.13.39) (BNOS) (Constitutive NOS) (NC-NOS) (NOS type I) (Neuronal NOS) (N-NOS) (nNOS) (Peptidyl-cysteine S-nitrosylase NOS1)

 NOS1_RAT                Reviewed;        1429 AA.
P29476; P70594;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
30-AUG-2017, entry version 200.
RecName: Full=Nitric oxide synthase, brain;
EC=1.14.13.39;
AltName: Full=BNOS;
AltName: Full=Constitutive NOS;
AltName: Full=NC-NOS;
AltName: Full=NOS type I;
AltName: Full=Neuronal NOS;
Short=N-NOS;
Short=nNOS;
AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
Name=Nos1; Synonyms=Bnos;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Brain;
PubMed=1712077; DOI=10.1038/351714a0;
Bredt D.S., Hwang P.M., Glatt C.L., Lowenstein C., Reed R.R.,
Snyder S.H.;
"Cloned and expressed nitric oxide synthase structurally resembles
cytochrome P-450 reductase.";
Nature 351:714-718(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PNNOS).
STRAIN=Fischer 344; TISSUE=Penis;
PubMed=8806605; DOI=10.1006/bbrc.1996.1324;
Magee T., Fuentes A.M., Garban H., Rajavashisth T., Marquez D.,
Rodriguez J.A., Rajfer J., Gonzalez-Cadavid N.F.;
"Cloning of a novel neuronal nitric oxide synthase expressed in penis
and lower urinary tract.";
Biochem. Biophys. Res. Commun. 226:145-151(1996).
[3]
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, AND TISSUE SPECIFICITY.
TISSUE=Colon;
PubMed=7520037;
Seo H.G., Tatsumi H., Fujii J., Nishikawa A., Suzuki K., Kangawa K.,
Taniguchi N.;
"Nitric oxide synthase from rat colorectum: purification, peptide
sequencing, partial PCR cloning, and immunohistochemistry.";
J. Biochem. 115:602-607(1994).
[4]
IDENTIFICATION OF TETRAHYDROBIOPTERIN-BINDING DOMAIN.
PubMed=7530005; DOI=10.1006/bbrc.1995.1104;
Uvarov V.Y., Lyashenko A.A.;
"The identification of the pterin-binding domain in the nitric oxide
synthase's sequence.";
Biochem. Biophys. Res. Commun. 206:736-741(1995).
[5]
MUTAGENESIS OF TYR-588.
PubMed=11237702; DOI=10.1006/bbrc.2001.4356;
Sato Y., Sagami I., Matsui T., Shimizu T.;
"Unusual role of Tyr588 of neuronal nitric oxide synthase in
controlling substrate specificity and electron transfer.";
Biochem. Biophys. Res. Commun. 281:621-626(2001).
[6]
INTERACTION WITH CAPON AND RASD1.
PubMed=11086993; DOI=10.1016/S0896-6273(00)00095-7;
Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.;
"Dexras1: a G protein specifically coupled to neuronal nitric oxide
synthase via CAPON.";
Neuron 28:183-193(2000).
[7]
INTERACTION WITH CAPON AND SYN1.
PubMed=11867766; DOI=10.1073/pnas.261705799;
Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H.;
"Neuronal nitric-oxide synthase localization mediated by a ternary
complex with synapsin and CAPON.";
Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002).
[8]
INTERACTION WITH ZDHHC23.
PubMed=15105416; DOI=10.1074/jbc.M401471200;
Saitoh F., Tian Q.B., Okano A., Sakagami H., Kondo H., Suzuki T.;
"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.";
J. Biol. Chem. 279:29461-29468(2004).
[9]
UBIQUITINATION.
PubMed=15466472; DOI=10.1074/jbc.M406926200;
Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M.,
Patterson C., Pratt W.B., Osawa Y.;
"Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a
chaperone-dependent E3 ligase.";
J. Biol. Chem. 279:52970-52977(2004).
[10]
INTERACTION WITH NOSIP, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
PubMed=15548660; DOI=10.1523/JNEUROSCI.2265-04.2004;
Dreyer J., Schleicher M., Tappe A., Schilling K., Kuner T.,
Kusumawidijaja G., Mueller-Esterl W., Oess S., Kuner R.;
"Nitric oxide synthase (NOS)-interacting protein interacts with
neuronal NOS and regulates its distribution and activity.";
J. Neurosci. 24:10454-10465(2004).
[11]
INTERACTION WITH VAC14, AND DOMAIN.
PubMed=17161399; DOI=10.1016/j.febslet.2006.11.061;
Lemaire J.F., McPherson P.S.;
"Binding of Vac14 to neuronal nitric oxide synthase: Characterisation
of a new internal PDZ-recognition motif.";
FEBS Lett. 580:6948-6954(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-847 AND SER-858, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[13]
INTERACTION WITH DLG4.
PubMed=23300088; DOI=10.1074/jbc.M112.412478;
Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.;
"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.";
J. Biol. Chem. 288:6438-6450(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 14-125.
PubMed=10221915; DOI=10.1126/science.284.5415.812;
Hillier B.J., Christopherson K.S., Prehoda K.E., Bredt D.S., Lim W.A.;
"Unexpected modes of PDZ domain scaffolding revealed by structure of
nNOS-syntrophin complex.";
Science 284:812-815(1999).
[15]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 963-1397.
PubMed=11473123; DOI=10.1074/jbc.M105503200;
Zhang J., Martasek P., Paschke R., Shea T., Masters B.S.S.,
Kim J.-J.P.;
"Crystal structure of the FAD/NADPH-binding domain of rat neuronal
nitric-oxide synthase. Comparisons with nadph-cytochrome p450
oxidoreductase.";
J. Biol. Chem. 276:37506-37513(2001).
-!- 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 O(2) = 2 L-
citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
Note=Binds 1 FAD. {ECO:0000250};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
Note=Binds 1 FMN. {ECO:0000250};
-!- COFACTOR:
Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250};
Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of
the enzyme. {ECO:0000250};
-!- 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. {ECO:0000250,
ECO:0000269|PubMed:15548660}.
-!- SUBUNIT: 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).
{ECO:0000250, ECO:0000269|PubMed:11086993,
ECO:0000269|PubMed:11867766, ECO:0000269|PubMed:15105416,
ECO:0000269|PubMed:15548660, ECO:0000269|PubMed:17161399,
ECO:0000269|PubMed:23300088}.
-!- INTERACTION:
P62157:CALM (xeno); NbExp=2; IntAct=EBI-349460, EBI-397403;
-!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Cell projection,
dendritic spine {ECO:0000250}. 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.
{ECO:0000250, ECO:0000269|PubMed:15548660}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=N-NOS-1;
IsoId=P29476-1; Sequence=Displayed;
Name=N-NOS-2;
IsoId=P29476-2; Sequence=VSP_003580;
Name=PNNOS;
IsoId=P29476-3; Sequence=VSP_003581;
-!- 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. {ECO:0000269|PubMed:7520037}.
-!- DOMAIN: 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. {ECO:0000250,
ECO:0000269|PubMed:17161399}.
-!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of
Hsp70 and Hsp40 (in vitro). {ECO:0000269|PubMed:15466472}.
-!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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EMBL; X59949; CAA42574.1; -; mRNA.
EMBL; U67309; AAC52782.1; -; mRNA.
PIR; S16233; S16233.
RefSeq; NP_434686.1; NM_052799.1.
UniGene; Rn.10573; -.
UniGene; Rn.214189; -.
UniGene; Rn.214216; -.
PDB; 1B8Q; NMR; -; A=11-133.
PDB; 1CMI; X-ray; 2.50 A; C/D=225-237.
PDB; 1F20; X-ray; 1.90 A; A=963-1397.
PDB; 1K2R; X-ray; 2.15 A; A/B=299-717.
PDB; 1K2S; X-ray; 2.55 A; A/B=299-717.
PDB; 1K2T; X-ray; 2.20 A; A/B=299-717.
PDB; 1K2U; X-ray; 2.20 A; A/B=299-717.
PDB; 1LZX; X-ray; 2.00 A; A/B=299-717.
PDB; 1LZZ; X-ray; 2.05 A; A/B=299-717.
PDB; 1M00; X-ray; 2.05 A; A/B=299-717.
PDB; 1MMV; X-ray; 2.00 A; A/B=299-717.
PDB; 1MMW; X-ray; 2.00 A; A/B=299-717.
PDB; 1OM4; X-ray; 1.75 A; A/B=297-718.
PDB; 1OM5; X-ray; 2.30 A; A/B=297-717.
PDB; 1P6H; X-ray; 1.98 A; A/B=297-717.
PDB; 1P6I; X-ray; 1.90 A; A/B=297-717.
PDB; 1P6J; X-ray; 2.00 A; A/B=297-717.
PDB; 1P6K; X-ray; 1.78 A; A/B=297-717.
PDB; 1QAU; X-ray; 1.25 A; A=14-125.
PDB; 1QAV; X-ray; 1.90 A; B=12-126.
PDB; 1QW6; X-ray; 2.10 A; A=298-716.
PDB; 1QWC; X-ray; 2.30 A; A=298-716.
PDB; 1RS6; X-ray; 1.95 A; A/B=297-717.
PDB; 1RS7; X-ray; 1.95 A; A/B=297-717.
PDB; 1TLL; X-ray; 2.30 A; A/B=742-1429.
PDB; 1VAG; X-ray; 2.00 A; A=298-716.
PDB; 1ZVI; X-ray; 2.00 A; A=298-716.
PDB; 1ZVL; X-ray; 2.50 A; A/B=298-716.
PDB; 1ZZQ; X-ray; 1.90 A; A/B=299-718.
PDB; 1ZZR; X-ray; 2.05 A; A/B=299-718.
PDB; 1ZZU; X-ray; 1.90 A; A/B=299-718.
PDB; 2G6H; X-ray; 2.00 A; A/B=299-718.
PDB; 2G6I; X-ray; 1.90 A; A/B=299-718.
PDB; 2G6J; X-ray; 2.30 A; A/B=299-718.
PDB; 2G6K; X-ray; 2.00 A; A/B=299-718.
PDB; 2G6L; X-ray; 2.05 A; A/B=299-718.
PDB; 2G6M; X-ray; 1.85 A; A/B=299-718.
PDB; 2G6N; X-ray; 1.90 A; A/B=299-718.
PDB; 2HX3; X-ray; 2.00 A; A/B=297-718.
PDB; 2HX4; X-ray; 2.15 A; A/B=297-718.
PDB; 3B3M; X-ray; 1.95 A; A/B=297-718.
PDB; 3B3N; X-ray; 1.98 A; A/B=297-718.
PDB; 3B3O; X-ray; 2.05 A; A/B=297-718.
PDB; 3B3P; X-ray; 2.45 A; A/B=297-718.
PDB; 3DQR; X-ray; 2.40 A; A/B=297-718.
PDB; 3FC5; X-ray; 2.59 A; A/B=297-718.
PDB; 3HSN; X-ray; 1.91 A; A/B=297-718.
PDB; 3HSO; X-ray; 2.02 A; A/B=297-718.
PDB; 3HSP; X-ray; 2.20 A; A/B=297-718.
PDB; 3JT3; X-ray; 2.15 A; A/B=297-718.
PDB; 3JT4; X-ray; 1.80 A; A/B=297-718.
PDB; 3JT5; X-ray; 2.10 A; A/B=297-718.
PDB; 3JT6; X-ray; 2.20 A; A/B=297-718.
PDB; 3JT7; X-ray; 2.10 A; A/B=297-718.
PDB; 3JT8; X-ray; 1.95 A; A/B=297-718.
PDB; 3JT9; X-ray; 2.10 A; A/B=297-718.
PDB; 3JTA; X-ray; 2.18 A; A/B=297-718.
PDB; 3JWS; X-ray; 1.95 A; A/B=297-718.
PDB; 3JWT; X-ray; 2.01 A; A/B=297-718.
PDB; 3JWU; X-ray; 1.93 A; A/B=297-718.
PDB; 3JWV; X-ray; 1.98 A; A/B=297-718.
PDB; 3JX0; X-ray; 2.20 A; A/B=297-718.
PDB; 3JX1; X-ray; 2.00 A; A/B=297-718.
PDB; 3JX2; X-ray; 2.10 A; A/B=297-718.
PDB; 3JX3; X-ray; 1.95 A; A/B=297-718.
PDB; 3JX4; X-ray; 2.26 A; A/B=297-718.
PDB; 3JX5; X-ray; 2.15 A; A/B=297-718.
PDB; 3JX6; X-ray; 2.35 A; A/B=297-718.
PDB; 3N2R; X-ray; 1.90 A; A/B=297-718.
PDB; 3N5V; X-ray; 2.30 A; A/B=297-718.
PDB; 3N5W; X-ray; 1.73 A; A/B=297-718.
PDB; 3N5X; X-ray; 1.80 A; A/B=297-718.
PDB; 3N5Y; X-ray; 2.05 A; A/B=297-718.
PDB; 3N5Z; X-ray; 2.18 A; A/B=297-718.
PDB; 3N60; X-ray; 1.98 A; A/B=297-718.
PDB; 3N61; X-ray; 1.95 A; A/B=297-718.
PDB; 3N62; X-ray; 1.95 A; A/B=297-718.
PDB; 3N63; X-ray; 2.00 A; A/B=297-718.
PDB; 3N64; X-ray; 1.95 A; A/B=297-718.
PDB; 3N65; X-ray; 1.80 A; A/B=297-718.
PDB; 3N66; X-ray; 1.78 A; A/B=297-718.
PDB; 3N67; X-ray; 2.09 A; A/B=298-711.
PDB; 3N68; X-ray; 2.53 A; A/B=298-711.
PDB; 3N69; X-ray; 2.65 A; A/B=298-711.
PDB; 3N6A; X-ray; 2.49 A; A/B=298-711.
PDB; 3N6B; X-ray; 3.10 A; A/B=298-711.
PDB; 3N6C; X-ray; 3.06 A; A/B=298-711.
PDB; 3N6D; X-ray; 3.05 A; A/B=298-711.
PDB; 3N6E; X-ray; 2.20 A; A/B=298-711.
PDB; 3N6F; X-ray; 2.18 A; A/B=298-711.
PDB; 3N6G; X-ray; 2.21 A; A/B=298-711.
PDB; 3NLJ; X-ray; 2.20 A; A/B=297-718.
PDB; 3NLK; X-ray; 2.02 A; A/B=297-718.
PDB; 3NLM; X-ray; 1.85 A; A/B=297-718.
PDB; 3NLN; X-ray; 2.00 A; A/B=297-718.
PDB; 3NLO; X-ray; 2.30 A; A/B=297-718.
PDB; 3NLP; X-ray; 2.02 A; A/B=297-718.
PDB; 3NLQ; X-ray; 2.15 A; A/B=297-718.
PDB; 3NLR; X-ray; 2.10 A; A/B=297-718.
PDB; 3NLV; X-ray; 2.10 A; A/B=297-718.
PDB; 3NLW; X-ray; 2.10 A; A/B=297-718.
PDB; 3NLX; X-ray; 1.87 A; A/B=297-718.
PDB; 3NLY; X-ray; 1.99 A; A/B=297-718.
PDB; 3NLZ; X-ray; 1.92 A; A/B=297-718.
PDB; 3NM0; X-ray; 1.81 A; A/B=297-718.
PDB; 3NNY; X-ray; 2.10 A; A/B=297-718.
PDB; 3NNZ; X-ray; 1.97 A; A/B=297-718.
PDB; 3PNE; X-ray; 1.97 A; A/B=297-718.
PDB; 3PNF; X-ray; 1.94 A; A/B=297-718.
PDB; 3PNG; X-ray; 1.88 A; A/B=297-718.
PDB; 3Q99; X-ray; 2.15 A; A/B=297-718.
PDB; 3Q9A; X-ray; 2.24 A; A/B=297-718.
PDB; 3RQJ; X-ray; 1.84 A; A/B=297-718.
PDB; 3RQK; X-ray; 2.21 A; A/B=297-718.
PDB; 3RQL; X-ray; 1.93 A; A/B=297-718.
PDB; 3RQM; X-ray; 1.95 A; A/B=297-718.
PDB; 3RQN; X-ray; 1.95 A; A/B=297-718.
PDB; 3SVP; X-ray; 2.05 A; A/B=297-718.
PDB; 3SVQ; X-ray; 2.18 A; A/B=297-718.
PDB; 3TYL; X-ray; 1.90 A; A/B=297-718.
PDB; 3TYM; X-ray; 2.00 A; A/B=297-718.
PDB; 3TYN; X-ray; 1.97 A; A/B=297-718.
PDB; 3TYO; X-ray; 1.93 A; A/B=297-718.
PDB; 3UFO; X-ray; 2.17 A; A/B=297-718.
PDB; 3UFP; X-ray; 2.10 A; A/B=297-718.
PDB; 3UFQ; X-ray; 2.06 A; A/B=297-718.
PDB; 3UFR; X-ray; 2.10 A; A/B=297-718.
PDB; 3UFS; X-ray; 1.97 A; A/B=297-718.
PDB; 3UFT; X-ray; 2.08 A; A/B=297-718.
PDB; 3UFU; X-ray; 1.89 A; A/B=297-718.
PDB; 3UFV; X-ray; 2.08 A; A/B=297-718.
PDB; 3UFW; X-ray; 2.00 A; A/B=297-718.
PDB; 4C39; X-ray; 1.98 A; A/B=297-718.
PDB; 4CAM; X-ray; 1.83 A; A/B=297-718.
PDB; 4CAN; X-ray; 1.91 A; A/B=297-718.
PDB; 4CAO; X-ray; 1.98 A; A/B=297-718.
PDB; 4CAP; X-ray; 2.06 A; A/B=297-718.
PDB; 4CAQ; X-ray; 1.95 A; A/B=297-718.
PDB; 4CDT; X-ray; 2.00 A; A/B=297-718.
PDB; 4CTP; X-ray; 2.05 A; A/B=297-718.
PDB; 4CTQ; X-ray; 2.00 A; A/B=297-718.
PDB; 4CTR; X-ray; 2.20 A; A/B=297-718.
PDB; 4CTT; X-ray; 2.30 A; A/B=297-718.
PDB; 4CTU; X-ray; 2.16 A; A/B=297-718.
PDB; 4CTV; X-ray; 1.78 A; A/B=297-718.
PDB; 4CTW; X-ray; 1.90 A; A/B=297-718.
PDB; 4CTX; X-ray; 1.82 A; A/B=297-718.
PDB; 4CX3; X-ray; 1.97 A; A/B=297-718.
PDB; 4CX4; X-ray; 1.98 A; A/B=297-718.
PDB; 4CX5; X-ray; 1.80 A; A/B=297-718.
PDB; 4CX6; X-ray; 1.90 A; A/B=297-718.
PDB; 4D2Y; X-ray; 1.98 A; A/B=297-718.
PDB; 4D2Z; X-ray; 1.89 A; A/B=297-718.
PDB; 4D30; X-ray; 1.96 A; A/B=297-718.
PDB; 4D31; X-ray; 1.95 A; A/B=297-718.
PDB; 4D32; X-ray; 2.10 A; A/B=297-718.
PDB; 4D3B; X-ray; 1.80 A; A/B=297-718.
PDB; 4D7O; X-ray; 1.78 A; A/B=297-718.
PDB; 4EUX; X-ray; 2.14 A; A/B=297-718.
PDB; 4FVW; X-ray; 1.81 A; A/B=297-718.
PDB; 4FVX; X-ray; 2.00 A; A/B=297-718.
PDB; 4FVY; X-ray; 1.70 A; A/B=297-718.
PDB; 4FVZ; X-ray; 1.99 A; A/B=297-718.
PDB; 4FW0; X-ray; 1.95 A; A/B=297-718.
PDB; 4GQE; X-ray; 1.80 A; A/B=297-718.
PDB; 4HOP; X-ray; 2.29 A; B/D/F=4-126.
PDB; 4IMS; X-ray; 2.15 A; A/B=297-718.
PDB; 4IMT; X-ray; 2.20 A; A/B=297-718.
PDB; 4IMU; X-ray; 2.03 A; A/B=297-718.
PDB; 4IMW; X-ray; 2.20 A; A/B=297-718.
PDB; 4JSE; X-ray; 1.97 A; A/B=297-718.
PDB; 4JSF; X-ray; 2.05 A; A/B=297-718.
PDB; 4JSG; X-ray; 1.94 A; A/B=297-718.
PDB; 4JSH; X-ray; 2.35 A; A/B=297-718.
PDB; 4JSI; X-ray; 2.09 A; A/B=297-718.
PDB; 4JSJ; X-ray; 1.92 A; A/B=297-718.
PDB; 4K5D; X-ray; 2.10 A; A/B=297-718.
PDB; 4K5E; X-ray; 1.89 A; A/B=297-718.
PDB; 4K5F; X-ray; 2.20 A; A/B=297-718.
PDB; 4K5G; X-ray; 1.85 A; A/B=297-718.
PDB; 4KCH; X-ray; 2.15 A; A/B=297-718.
PDB; 4KCI; X-ray; 2.27 A; A/B=297-718.
PDB; 4KCJ; X-ray; 2.05 A; A/B=297-718.
PDB; 4KCK; X-ray; 2.10 A; A/B=297-718.
PDB; 4KCL; X-ray; 1.93 A; A/B=297-718.
PDB; 4KCM; X-ray; 2.07 A; A/B=297-718.
PDB; 4KCN; X-ray; 1.85 A; A/B=297-718.
PDB; 4KCO; X-ray; 1.86 A; A/B=297-718.
PDB; 4LUX; X-ray; 1.86 A; A/B=297-718.
PDB; 4UGZ; X-ray; 2.08 A; A/B=297-718.
PDB; 4UH0; X-ray; 2.04 A; A/B=297-718.
PDB; 4UH1; X-ray; 1.80 A; A/B=297-718.
PDB; 4UH2; X-ray; 1.99 A; A/B=297-718.
PDB; 4UH3; X-ray; 2.03 A; A/B=297-718.
PDB; 4UH4; X-ray; 1.95 A; A/B=297-718.
PDB; 4UPM; X-ray; 1.90 A; A/B=297-718.
PDB; 4UPN; X-ray; 2.09 A; A/B=297-718.
PDB; 4UPO; X-ray; 1.95 A; A/B=297-718.
PDB; 4UPP; X-ray; 1.91 A; A/B=297-718.
PDB; 4V3V; X-ray; 2.06 A; A/B=297-718.
PDB; 4V3W; X-ray; 2.13 A; A/B=297-718.
PDB; 4V3X; X-ray; 1.99 A; A/B=297-718.
PDB; 4V3Y; X-ray; 1.96 A; A/B=297-718.
PDB; 4V3Z; X-ray; 2.05 A; A/B=297-718.
PDB; 5AD4; X-ray; 1.98 A; A/B=297-718.
PDB; 5AD5; X-ray; 1.90 A; A/B=297-718.
PDB; 5AD6; X-ray; 2.00 A; A/B=297-718.
PDB; 5AD7; X-ray; 1.95 A; A/B=297-718.
PDB; 5AD8; X-ray; 1.91 A; A/B=297-718.
PDB; 5AD9; X-ray; 2.30 A; A/B=297-718.
PDB; 5ADA; X-ray; 1.98 A; A/B=297-718.
PDB; 5ADB; X-ray; 2.05 A; A/B=297-718.
PDB; 5ADC; X-ray; 2.10 A; A/B=297-718.
PDB; 5ADD; X-ray; 2.10 A; A/B=297-718.
PDB; 5ADE; X-ray; 2.10 A; A/B=297-718.
PDB; 5AGK; X-ray; 2.00 A; A/B=297-718.
PDB; 5AGL; X-ray; 1.94 A; A/B=297-718.
PDB; 5AGM; X-ray; 1.84 A; A/B=297-718.
PDB; 5AGN; X-ray; 1.95 A; A/B=297-718.
PDB; 5AGO; X-ray; 1.90 A; A/B=297-718.
PDB; 5AGP; X-ray; 2.10 A; A/B=297-718.
PDB; 5FVO; X-ray; 2.12 A; A=297-718.
PDB; 5FVP; X-ray; 2.10 A; A/B=297-718.
PDB; 5FVQ; X-ray; 1.95 A; A/B=297-718.
PDB; 5FVR; X-ray; 1.84 A; A/B=297-718.
PDB; 5FVS; X-ray; 1.95 A; A/B=297-718.
PDB; 5FVT; X-ray; 1.83 A; A/B=297-718.
PDB; 5FW0; X-ray; 1.80 A; A/B=297-718.
PDB; 5G0N; X-ray; 1.94 A; A/B=297-718.
PDB; 5G0O; X-ray; 1.85 A; A/B=297-718.
PDB; 5G0P; X-ray; 2.10 A; A/B=297-718.
PDB; 5UNR; X-ray; 1.95 A; A/B=297-718.
PDB; 5UNS; X-ray; 1.90 A; A/B=297-718.
PDB; 5UNT; X-ray; 2.05 A; A/B=297-718.
PDB; 5UNU; X-ray; 2.05 A; A/B=297-718.
PDB; 5UNV; X-ray; 2.00 A; A/B=297-718.
PDB; 5UNW; X-ray; 2.04 A; A/B=297-718.
PDB; 5UNX; X-ray; 2.03 A; A/B=297-718.
PDB; 5UNY; X-ray; 1.82 A; A/B=297-718.
PDB; 5UNZ; X-ray; 1.95 A; A/B=297-718.
PDB; 5UO0; X-ray; 1.97 A; A/B=297-718.
PDBsum; 1B8Q; -.
PDBsum; 1CMI; -.
PDBsum; 1F20; -.
PDBsum; 1K2R; -.
PDBsum; 1K2S; -.
PDBsum; 1K2T; -.
PDBsum; 1K2U; -.
PDBsum; 1LZX; -.
PDBsum; 1LZZ; -.
PDBsum; 1M00; -.
PDBsum; 1MMV; -.
PDBsum; 1MMW; -.
PDBsum; 1OM4; -.
PDBsum; 1OM5; -.
PDBsum; 1P6H; -.
PDBsum; 1P6I; -.
PDBsum; 1P6J; -.
PDBsum; 1P6K; -.
PDBsum; 1QAU; -.
PDBsum; 1QAV; -.
PDBsum; 1QW6; -.
PDBsum; 1QWC; -.
PDBsum; 1RS6; -.
PDBsum; 1RS7; -.
PDBsum; 1TLL; -.
PDBsum; 1VAG; -.
PDBsum; 1ZVI; -.
PDBsum; 1ZVL; -.
PDBsum; 1ZZQ; -.
PDBsum; 1ZZR; -.
PDBsum; 1ZZU; -.
PDBsum; 2G6H; -.
PDBsum; 2G6I; -.
PDBsum; 2G6J; -.
PDBsum; 2G6K; -.
PDBsum; 2G6L; -.
PDBsum; 2G6M; -.
PDBsum; 2G6N; -.
PDBsum; 2HX3; -.
PDBsum; 2HX4; -.
PDBsum; 3B3M; -.
PDBsum; 3B3N; -.
PDBsum; 3B3O; -.
PDBsum; 3B3P; -.
PDBsum; 3DQR; -.
PDBsum; 3FC5; -.
PDBsum; 3HSN; -.
PDBsum; 3HSO; -.
PDBsum; 3HSP; -.
PDBsum; 3JT3; -.
PDBsum; 3JT4; -.
PDBsum; 3JT5; -.
PDBsum; 3JT6; -.
PDBsum; 3JT7; -.
PDBsum; 3JT8; -.
PDBsum; 3JT9; -.
PDBsum; 3JTA; -.
PDBsum; 3JWS; -.
PDBsum; 3JWT; -.
PDBsum; 3JWU; -.
PDBsum; 3JWV; -.
PDBsum; 3JX0; -.
PDBsum; 3JX1; -.
PDBsum; 3JX2; -.
PDBsum; 3JX3; -.
PDBsum; 3JX4; -.
PDBsum; 3JX5; -.
PDBsum; 3JX6; -.
PDBsum; 3N2R; -.
PDBsum; 3N5V; -.
PDBsum; 3N5W; -.
PDBsum; 3N5X; -.
PDBsum; 3N5Y; -.
PDBsum; 3N5Z; -.
PDBsum; 3N60; -.
PDBsum; 3N61; -.
PDBsum; 3N62; -.
PDBsum; 3N63; -.
PDBsum; 3N64; -.
PDBsum; 3N65; -.
PDBsum; 3N66; -.
PDBsum; 3N67; -.
PDBsum; 3N68; -.
PDBsum; 3N69; -.
PDBsum; 3N6A; -.
PDBsum; 3N6B; -.
PDBsum; 3N6C; -.
PDBsum; 3N6D; -.
PDBsum; 3N6E; -.
PDBsum; 3N6F; -.
PDBsum; 3N6G; -.
PDBsum; 3NLJ; -.
PDBsum; 3NLK; -.
PDBsum; 3NLM; -.
PDBsum; 3NLN; -.
PDBsum; 3NLO; -.
PDBsum; 3NLP; -.
PDBsum; 3NLQ; -.
PDBsum; 3NLR; -.
PDBsum; 3NLV; -.
PDBsum; 3NLW; -.
PDBsum; 3NLX; -.
PDBsum; 3NLY; -.
PDBsum; 3NLZ; -.
PDBsum; 3NM0; -.
PDBsum; 3NNY; -.
PDBsum; 3NNZ; -.
PDBsum; 3PNE; -.
PDBsum; 3PNF; -.
PDBsum; 3PNG; -.
PDBsum; 3Q99; -.
PDBsum; 3Q9A; -.
PDBsum; 3RQJ; -.
PDBsum; 3RQK; -.
PDBsum; 3RQL; -.
PDBsum; 3RQM; -.
PDBsum; 3RQN; -.
PDBsum; 3SVP; -.
PDBsum; 3SVQ; -.
PDBsum; 3TYL; -.
PDBsum; 3TYM; -.
PDBsum; 3TYN; -.
PDBsum; 3TYO; -.
PDBsum; 3UFO; -.
PDBsum; 3UFP; -.
PDBsum; 3UFQ; -.
PDBsum; 3UFR; -.
PDBsum; 3UFS; -.
PDBsum; 3UFT; -.
PDBsum; 3UFU; -.
PDBsum; 3UFV; -.
PDBsum; 3UFW; -.
PDBsum; 4C39; -.
PDBsum; 4CAM; -.
PDBsum; 4CAN; -.
PDBsum; 4CAO; -.
PDBsum; 4CAP; -.
PDBsum; 4CAQ; -.
PDBsum; 4CDT; -.
PDBsum; 4CTP; -.
PDBsum; 4CTQ; -.
PDBsum; 4CTR; -.
PDBsum; 4CTT; -.
PDBsum; 4CTU; -.
PDBsum; 4CTV; -.
PDBsum; 4CTW; -.
PDBsum; 4CTX; -.
PDBsum; 4CX3; -.
PDBsum; 4CX4; -.
PDBsum; 4CX5; -.
PDBsum; 4CX6; -.
PDBsum; 4D2Y; -.
PDBsum; 4D2Z; -.
PDBsum; 4D30; -.
PDBsum; 4D31; -.
PDBsum; 4D32; -.
PDBsum; 4D3B; -.
PDBsum; 4D7O; -.
PDBsum; 4EUX; -.
PDBsum; 4FVW; -.
PDBsum; 4FVX; -.
PDBsum; 4FVY; -.
PDBsum; 4FVZ; -.
PDBsum; 4FW0; -.
PDBsum; 4GQE; -.
PDBsum; 4HOP; -.
PDBsum; 4IMS; -.
PDBsum; 4IMT; -.
PDBsum; 4IMU; -.
PDBsum; 4IMW; -.
PDBsum; 4JSE; -.
PDBsum; 4JSF; -.
PDBsum; 4JSG; -.
PDBsum; 4JSH; -.
PDBsum; 4JSI; -.
PDBsum; 4JSJ; -.
PDBsum; 4K5D; -.
PDBsum; 4K5E; -.
PDBsum; 4K5F; -.
PDBsum; 4K5G; -.
PDBsum; 4KCH; -.
PDBsum; 4KCI; -.
PDBsum; 4KCJ; -.
PDBsum; 4KCK; -.
PDBsum; 4KCL; -.
PDBsum; 4KCM; -.
PDBsum; 4KCN; -.
PDBsum; 4KCO; -.
PDBsum; 4LUX; -.
PDBsum; 4UGZ; -.
PDBsum; 4UH0; -.
PDBsum; 4UH1; -.
PDBsum; 4UH2; -.
PDBsum; 4UH3; -.
PDBsum; 4UH4; -.
PDBsum; 4UPM; -.
PDBsum; 4UPN; -.
PDBsum; 4UPO; -.
PDBsum; 4UPP; -.
PDBsum; 4V3V; -.
PDBsum; 4V3W; -.
PDBsum; 4V3X; -.
PDBsum; 4V3Y; -.
PDBsum; 4V3Z; -.
PDBsum; 5AD4; -.
PDBsum; 5AD5; -.
PDBsum; 5AD6; -.
PDBsum; 5AD7; -.
PDBsum; 5AD8; -.
PDBsum; 5AD9; -.
PDBsum; 5ADA; -.
PDBsum; 5ADB; -.
PDBsum; 5ADC; -.
PDBsum; 5ADD; -.
PDBsum; 5ADE; -.
PDBsum; 5AGK; -.
PDBsum; 5AGL; -.
PDBsum; 5AGM; -.
PDBsum; 5AGN; -.
PDBsum; 5AGO; -.
PDBsum; 5AGP; -.
PDBsum; 5FVO; -.
PDBsum; 5FVP; -.
PDBsum; 5FVQ; -.
PDBsum; 5FVR; -.
PDBsum; 5FVS; -.
PDBsum; 5FVT; -.
PDBsum; 5FW0; -.
PDBsum; 5G0N; -.
PDBsum; 5G0O; -.
PDBsum; 5G0P; -.
PDBsum; 5UNR; -.
PDBsum; 5UNS; -.
PDBsum; 5UNT; -.
PDBsum; 5UNU; -.
PDBsum; 5UNV; -.
PDBsum; 5UNW; -.
PDBsum; 5UNX; -.
PDBsum; 5UNY; -.
PDBsum; 5UNZ; -.
PDBsum; 5UO0; -.
ProteinModelPortal; P29476; -.
SMR; P29476; -.
BioGrid; 246738; 12.
DIP; DIP-33272N; -.
ELM; P29476; -.
IntAct; P29476; 7.
MINT; MINT-89230; -.
STRING; 10116.ENSRNOP00000062735; -.
BindingDB; P29476; -.
ChEMBL; CHEMBL3048; -.
GuidetoPHARMACOLOGY; 1251; -.
iPTMnet; P29476; -.
PhosphoSitePlus; P29476; -.
PaxDb; P29476; -.
PRIDE; P29476; -.
GeneID; 24598; -.
KEGG; rno:24598; -.
UCSC; RGD:3184; rat. [P29476-1]
CTD; 4842; -.
RGD; 3184; Nos1.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
eggNOG; COG4362; LUCA.
HOGENOM; HOG000220884; -.
HOVERGEN; HBG000159; -.
InParanoid; P29476; -.
KO; K13240; -.
PhylomeDB; P29476; -.
BRENDA; 1.14.13.39; 5301.
SABIO-RK; P29476; -.
EvolutionaryTrace; P29476; -.
PRO; PR:P29476; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0042582; C:azurophil granule; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0031965; C:nuclear membrane; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0001917; C:photoreceptor inner segment; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
GO; GO:0043234; C:protein complex; IDA:BHF-UCL.
GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0012506; C:vesicle membrane; IDA:RGD.
GO; GO:0016597; F:amino acid binding; TAS:RGD.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0046870; F:cadmium ion binding; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:BHF-UCL.
GO; GO:0010181; F:FMN binding; IDA:BHF-UCL.
GO; GO:0020037; F:heme binding; IDA:BHF-UCL.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IDA:BHF-UCL.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:0051219; F:phosphoprotein binding; IPI:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006527; P:arginine catabolic process; IDA:BHF-UCL.
GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:BHF-UCL.
GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:RGD.
GO; GO:0045184; P:establishment of protein localization; IDA:CAFA.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
GO; GO:0045822; P:negative regulation of heart contraction; IMP:RGD.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:RGD.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:RGD.
GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IMP:BHF-UCL.
GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA:BHF-UCL.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IMP:RGD.
GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:GO_Central.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; IMP:BHF-UCL.
GO; GO:0008016; P:regulation of heart contraction; IMP:RGD.
GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IDA:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:BHF-UCL.
GO; GO:0010288; P:response to lead ion; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0071731; P:response to nitric oxide; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IMP:RGD.
GO; GO:0033197; P:response to vitamin E; IEP:RGD.
Gene3D; 3.40.50.360; -; 1.
InterPro; IPR003097; FAD-binding_1.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_dom.
InterPro; IPR012144; NOS_euk.
InterPro; IPR004030; NOS_N.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR001478; PDZ.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
Pfam; PF02898; NO_synthase; 1.
Pfam; PF00595; PDZ; 1.
PIRSF; PIRSF000333; NOS; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF56512; SSF56512; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PROSITE; PS60001; NOS; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane;
Cell projection; Complete proteome; Direct protein sequencing; FAD;
Flavoprotein; FMN; Heme; Iron; Membrane; Metal-binding; NADP;
Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 1429 Nitric oxide synthase, brain.
/FTId=PRO_0000170924.
DOMAIN 17 99 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 755 935 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 990 1237 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 881 912 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 1027 1038 FAD. {ECO:0000250}.
NP_BIND 1170 1180 FAD. {ECO:0000250}.
NP_BIND 1245 1263 NADP. {ECO:0000250}.
NP_BIND 1343 1358 NADP. {ECO:0000250}.
REGION 1 200 Interaction with NOSIP.
{ECO:0000269|PubMed:15548660}.
REGION 163 240 PIN (nNOS-inhibiting protein) binding.
{ECO:0000250}.
REGION 725 745 Calmodulin-binding. {ECO:0000255}.
REGION 750 769 Tetrahydrobiopterin-binding.
METAL 415 415 Iron (heme axial ligand). {ECO:0000250}.
BINDING 588 588 Substrate.
MOD_RES 280 280 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0J4}.
MOD_RES 847 847 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 857 857 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z0J4}.
MOD_RES 858 858 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 504 608 Missing (in isoform N-NOS-2).
{ECO:0000305}.
/FTId=VSP_003580.
VAR_SEQ 839 839 K -> KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR
(in isoform PNNOS).
{ECO:0000303|PubMed:8806605}.
/FTId=VSP_003581.
MUTAGEN 588 588 Y->F: No decrease in activity.
{ECO:0000269|PubMed:11237702}.
MUTAGEN 588 588 Y->H: 50% decrease of activity.
{ECO:0000269|PubMed:11237702}.
MUTAGEN 588 588 Y->S: 30% decrease of activity.
{ECO:0000269|PubMed:11237702}.
CONFLICT 269 269 I -> V (in Ref. 2; AAC52782 and 3; AA
sequence). {ECO:0000305}.
CONFLICT 953 953 P -> A (in Ref. 2; AAC52782 and 3; AA
sequence). {ECO:0000305}.
CONFLICT 1008 1008 F -> S (in Ref. 2; AAC52782).
{ECO:0000305}.
CONFLICT 1311 1311 A -> V (in Ref. 2; AAC52782).
{ECO:0000305}.
STRAND 9 12 {ECO:0000244|PDB:4HOP}.
STRAND 15 21 {ECO:0000244|PDB:1QAU}.
TURN 24 26 {ECO:0000244|PDB:1QAU}.
STRAND 29 34 {ECO:0000244|PDB:1QAU}.
STRAND 36 39 {ECO:0000244|PDB:1QAU}.
STRAND 41 46 {ECO:0000244|PDB:1QAU}.
HELIX 51 55 {ECO:0000244|PDB:1QAU}.
TURN 60 62 {ECO:0000244|PDB:1B8Q}.
STRAND 63 67 {ECO:0000244|PDB:1QAU}.
STRAND 73 75 {ECO:0000244|PDB:1B8Q}.
HELIX 77 86 {ECO:0000244|PDB:1QAU}.
STRAND 89 98 {ECO:0000244|PDB:1QAU}.
STRAND 103 111 {ECO:0000244|PDB:1QAU}.
STRAND 113 115 {ECO:0000244|PDB:1QAV}.
STRAND 117 124 {ECO:0000244|PDB:1QAU}.
STRAND 228 236 {ECO:0000244|PDB:1CMI}.
STRAND 301 305 {ECO:0000244|PDB:4FVY}.
TURN 306 308 {ECO:0000244|PDB:4FVY}.
STRAND 311 314 {ECO:0000244|PDB:4FVY}.
HELIX 316 319 {ECO:0000244|PDB:4FVY}.
STRAND 328 331 {ECO:0000244|PDB:3N5V}.
STRAND 340 342 {ECO:0000244|PDB:1VAG}.
STRAND 345 347 {ECO:0000244|PDB:1VAG}.
HELIX 351 368 {ECO:0000244|PDB:4FVY}.
STRAND 372 374 {ECO:0000244|PDB:1K2U}.
HELIX 375 391 {ECO:0000244|PDB:4FVY}.
HELIX 398 410 {ECO:0000244|PDB:4FVY}.
HELIX 418 420 {ECO:0000244|PDB:4FVY}.
STRAND 425 428 {ECO:0000244|PDB:4FVY}.
HELIX 435 450 {ECO:0000244|PDB:4FVY}.
HELIX 451 453 {ECO:0000244|PDB:4FVY}.
STRAND 458 461 {ECO:0000244|PDB:4FVY}.
STRAND 466 470 {ECO:0000244|PDB:4FVY}.
STRAND 476 480 {ECO:0000244|PDB:4FVY}.
STRAND 484 486 {ECO:0000244|PDB:4FVY}.
STRAND 490 494 {ECO:0000244|PDB:4FVY}.
HELIX 496 498 {ECO:0000244|PDB:4FVY}.
HELIX 499 507 {ECO:0000244|PDB:4FVY}.
STRAND 515 517 {ECO:0000244|PDB:3N5W}.
STRAND 522 525 {ECO:0000244|PDB:4FVY}.
STRAND 527 529 {ECO:0000244|PDB:3N6D}.
STRAND 532 534 {ECO:0000244|PDB:4FVY}.
HELIX 538 540 {ECO:0000244|PDB:4FVY}.
STRAND 543 545 {ECO:0000244|PDB:4FVY}.
HELIX 554 557 {ECO:0000244|PDB:4FVY}.
STRAND 560 563 {ECO:0000244|PDB:4FVY}.
STRAND 571 574 {ECO:0000244|PDB:4FVY}.
STRAND 577 580 {ECO:0000244|PDB:4FVY}.
HELIX 590 594 {ECO:0000244|PDB:4FVY}.
HELIX 596 599 {ECO:0000244|PDB:4FVY}.
TURN 601 604 {ECO:0000244|PDB:4FVY}.
HELIX 607 613 {ECO:0000244|PDB:4FVY}.
HELIX 621 623 {ECO:0000244|PDB:4FVY}.
HELIX 625 643 {ECO:0000244|PDB:4FVY}.
HELIX 651 669 {ECO:0000244|PDB:4FVY}.
HELIX 676 679 {ECO:0000244|PDB:4FVY}.
STRAND 682 684 {ECO:0000244|PDB:4FVY}.
HELIX 685 687 {ECO:0000244|PDB:4FVY}.
HELIX 689 692 {ECO:0000244|PDB:4FVY}.
STRAND 696 698 {ECO:0000244|PDB:3N6D}.
STRAND 701 705 {ECO:0000244|PDB:4FVY}.
HELIX 710 713 {ECO:0000244|PDB:4FVY}.
STRAND 754 760 {ECO:0000244|PDB:1TLL}.
STRAND 762 764 {ECO:0000244|PDB:1TLL}.
HELIX 765 777 {ECO:0000244|PDB:1TLL}.
TURN 778 780 {ECO:0000244|PDB:1TLL}.
STRAND 781 787 {ECO:0000244|PDB:1TLL}.
TURN 788 790 {ECO:0000244|PDB:1TLL}.
HELIX 796 798 {ECO:0000244|PDB:1TLL}.
STRAND 800 806 {ECO:0000244|PDB:1TLL}.
TURN 810 812 {ECO:0000244|PDB:1TLL}.
HELIX 816 818 {ECO:0000244|PDB:1TLL}.
HELIX 819 828 {ECO:0000244|PDB:1TLL}.
HELIX 841 844 {ECO:0000244|PDB:1TLL}.
TURN 873 876 {ECO:0000244|PDB:1TLL}.
STRAND 878 885 {ECO:0000244|PDB:1TLL}.
STRAND 889 891 {ECO:0000244|PDB:1TLL}.
HELIX 894 905 {ECO:0000244|PDB:1TLL}.
STRAND 909 912 {ECO:0000244|PDB:1TLL}.
STRAND 915 918 {ECO:0000244|PDB:1TLL}.
TURN 919 922 {ECO:0000244|PDB:1TLL}.
HELIX 923 942 {ECO:0000244|PDB:1TLL}.
STRAND 946 948 {ECO:0000244|PDB:1TLL}.
STRAND 961 963 {ECO:0000244|PDB:1TLL}.
STRAND 968 973 {ECO:0000244|PDB:1F20}.
HELIX 980 988 {ECO:0000244|PDB:1F20}.
STRAND 993 1002 {ECO:0000244|PDB:1F20}.
STRAND 1012 1018 {ECO:0000244|PDB:1F20}.
HELIX 1023 1025 {ECO:0000244|PDB:1F20}.
STRAND 1032 1035 {ECO:0000244|PDB:1F20}.
HELIX 1041 1048 {ECO:0000244|PDB:1F20}.
STRAND 1051 1053 {ECO:0000244|PDB:1F20}.
STRAND 1061 1072 {ECO:0000244|PDB:1F20}.
STRAND 1076 1081 {ECO:0000244|PDB:1F20}.
HELIX 1090 1096 {ECO:0000244|PDB:1F20}.
HELIX 1106 1113 {ECO:0000244|PDB:1F20}.
HELIX 1119 1128 {ECO:0000244|PDB:1F20}.
HELIX 1133 1142 {ECO:0000244|PDB:1F20}.
HELIX 1146 1152 {ECO:0000244|PDB:1F20}.
HELIX 1160 1166 {ECO:0000244|PDB:1F20}.
STRAND 1173 1176 {ECO:0000244|PDB:1F20}.
TURN 1181 1183 {ECO:0000244|PDB:1F20}.
STRAND 1187 1193 {ECO:0000244|PDB:1F20}.
STRAND 1196 1198 {ECO:0000244|PDB:1F20}.
HELIX 1200 1202 {ECO:0000244|PDB:1F20}.
STRAND 1206 1208 {ECO:0000244|PDB:1F20}.
HELIX 1210 1215 {ECO:0000244|PDB:1F20}.
STRAND 1223 1229 {ECO:0000244|PDB:1F20}.
HELIX 1232 1234 {ECO:0000244|PDB:1TLL}.
STRAND 1244 1247 {ECO:0000244|PDB:1F20}.
HELIX 1250 1253 {ECO:0000244|PDB:1F20}.
HELIX 1254 1270 {ECO:0000244|PDB:1F20}.
STRAND 1277 1284 {ECO:0000244|PDB:1F20}.
TURN 1286 1288 {ECO:0000244|PDB:1F20}.
HELIX 1293 1301 {ECO:0000244|PDB:1F20}.
STRAND 1304 1314 {ECO:0000244|PDB:1F20}.
HELIX 1323 1330 {ECO:0000244|PDB:1F20}.
HELIX 1332 1340 {ECO:0000244|PDB:1F20}.
STRAND 1345 1350 {ECO:0000244|PDB:1F20}.
HELIX 1352 1369 {ECO:0000244|PDB:1F20}.
HELIX 1374 1386 {ECO:0000244|PDB:1F20}.
STRAND 1390 1394 {ECO:0000244|PDB:1F20}.
HELIX 1401 1411 {ECO:0000244|PDB:1TLL}.
SEQUENCE 1429 AA; 160559 MW; 7255C5AE165200F5 CRC64;
MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA
GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI
RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI
DPTMKSTKAN LQDIGEHDEL LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD
GKSHKAPPLG GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF
LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT KDQLFPLAKE
FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ
WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI
RYAGYKQPDG STLGDPANVQ FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL
VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD
NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK
HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN
GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA
FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS
YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD
TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKPNNSLISN
DRSWKRNKFR LTYVAEAPDL TQGLSNVHKK RVSAARLLSR QNLQSPKFSR STIFVRLHTN
GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK
DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW
GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR
DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW
QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK
KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF
ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDADEVFSS


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