[1]
|
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Brain;
DOI=10.1038/351714a0; PubMed=1712077 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1006/bbrc.1996.1324; PubMed=8806605 [NCBI, ExPASy, EBI, Israel, Japan]
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; 264-268; 270-276; 305-310; 360-369; 376-379; 381-385; 387-396; 779-785; 954-963 AND 1131-1139, AND TISSUE SPECIFICITY.
TISSUE=Colon;
PubMed=7520037 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1006/bbrc.1995.1104; PubMed=7530005 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1006/bbrc.2001.4356; PubMed=11237702 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/S0896-6273(00)00095-7; PubMed=11086993 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1073/pnas.261705799; PubMed=11867766 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1074/jbc.M401471200; PubMed=15105416 [NCBI, ExPASy, EBI, Israel, Japan]
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]
|
INTERACTION WITH NOSIP, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
DOI=10.1523/JNEUROSCI.2265-04.2004; PubMed=15548660 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[10]
|
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 14-125.
DOI=10.1126/science.284.5415.812; PubMed=10221915 [NCBI, ExPASy, EBI, Israel, Japan]
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).
|
[11]
|
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 963-1397.
DOI=10.1074/jbc.M105503200; PubMed=11473123 [NCBI, ExPASy, EBI, Israel, Japan]
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.
- CATALYTIC ACTIVITY: L-arginine + n NADPH + m O2 = citrulline + nitric oxide + n NADP+.
- COFACTOR: Heme group (By similarity).
- COFACTOR: Binds 1 FAD (By similarity).
- COFACTOR: Binds 1 FMN (By similarity).
- COFACTOR: Metrahydrobiopterin (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.
- 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).
- INTERACTION:
P31016:Dlg4; NbExp=1; IntAct=EBI-349460, EBI-375655;
Q61234:Snta1 (xeno); NbExp=1; IntAct=EBI-349460, EBI-295952;
- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral membrane protein (By similarity). Cell projection, dendritic 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.
- ALTERNATIVE PRODUCTS:
3 named isoforms [FASTA] produced by alternative splicing.
|
| Name | N-NOS-2 |
| Isoform ID | P29476-2 |
| Features which should be applied to build the isoform sequence: VSP_003580. |
|
|
| Name | PNNOS |
| Isoform ID | P29476-3 |
| Features which should be applied to build the isoform 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.
- 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).
- SIMILARITY: Belongs to the NOS family.
- SIMILARITY: Contains 1 FAD-binding FR-type domain.
- SIMILARITY: Contains 1 flavodoxin-like domain.
- SIMILARITY: Contains 1 PDZ (DHR) domain.
|
ExPASy Home page
