[1]	NUCLEOTIDE SEQUENCE [MRNA]. 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).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-288. STRAIN=Sprague-Dawley; Toporsian M., Govindaraju K., Nagi M., Eidelman D., Thibault G., Ward M.E.; "Downregulation of endothelial nitric oxide synthase (NOS III) in rat aorta following in-vivo hypoxia."; Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 14-1202. STRAIN=SS/JrHsdMcwi; TISSUE=Heart; DOI=10.1016/j.yjmcc.2005.02.005; PubMed=15808839 [NCBI, ExPASy, EBI, Israel, Japan] Shi Y., Hutchins W., Ogawa H., Chang C.-C., Pritchard K.A. Jr., Zhang C., Khampang P., Lazar J., Jacob H.J., Rafiee P., Baker J.E.; "Increased resistance to myocardial ischemia in the Brown Norway vs. Dahl S rat: role of nitric oxide synthase and Hsp90."; J. Mol. Cell. Cardiol. 38:625-635(2005).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 473-672 AND 951-1192. TISSUE=Brain; Seidel B., Jiang L., Wolf G.; "Cloning and expression of the rat endothelial nitric oxide synthase."; Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 633-862. STRAIN=Sprague-Dawley; PubMed=7527874 [NCBI, ExPASy, EBI, Israel, Japan] Mohaupt M.G., Elzie J.L., Ahn K.Y., Clapp W.L., Wilcox C.S., Kone B.C.; "Differential expression and induction of mRNAs encoding two inducible nitric oxide synthases in rat kidney."; Kidney Int. 46:653-665(1994).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 1015-1132. STRAIN=Sprague-Dawley; TISSUE=Lung; Minchenko A.G., Armstead V.E., Opentanova I.L., Lefer A.M.; "Endothelin-1, endothelin receptors and ecNOS mRNA expression in vital organs during traumatic shock in rats."; Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 1018-1080. STRAIN=Sprague-Dawley; TISSUE=Lung; PubMed=7537461 [NCBI, ExPASy, EBI, Israel, Japan] Kawai N., Bloch D.B., Filippov G., Rabkina D., Suen H.C., Losty P.D., Janssens S.P., Zapol W.M., de la Monte S., Bloch K.D.; "Constitutive endothelial nitric oxide synthase gene expression is regulated during lung development."; Am. J. Physiol. 268:L589-L595(1995).

Comments

FUNCTION: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. No mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets.
CATALYTIC ACTIVITY: L-arginine + n NADPH + m O₂ = citrulline + nitric oxide + n NADP⁺.
COFACTOR: Heme group.
COFACTOR: Binds 1 FAD.
COFACTOR: Binds 1 FMN.
COFACTOR: Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.
ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by NOSIP and NOSTRIN (By similarity).
SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By similarity).
SUBCELLULAR LOCATION: Cell membrane, caveola (By similarity). Cytoplasm, cytoskeleton (By similarity). Golgi apparatus (By similarity). Note=Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle; which is favored by interaction with NOSIP and results in a reduced enzymatic activity (By similarity).
TISSUE SPECIFICITY: Expressed constitutively by vascular endothelium. Detected in alveolar and serosal epithelial cells as well as in endothelial cells in one day old rat. In adult lung, detected in rare endothelial cells.
DEVELOPMENTAL STAGE: Detected at high levels in lung during the late fetal and postnatal period and at lower levels in adult.
SIMILARITY: Belongs to the NOS family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB176831; BAD15356.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF085195; AAC34677.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY695391; AAT99567.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ011115; CAA09493.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ011116; CAA09494.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U02534; AAA96141.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF093837; AAC64178.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U18336; AAC52188.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I51917; I51917.
I56979; I56979.

RefSeq

NP_068610.1; -.

UniGene

Rn.44265

3D structure databases

HSSP

P29474; 3NOS. [HSSP ENTRY / PDB]

Q62600; 64-479.

PTM databases

Q62600; -.

Organism-specific databases

RGD

3186; Nos3.

Gene expression databases

ArrayExpress

Q62600; -.

GermOnline

ENSRNOG00000009348; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR008254; Flavodoxin/NO_synth.
IPR004030; NO_synthase_oxygenase_reg.
IPR012144; NOS.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000333; NOS; 1.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q62600.

Genome annotation databases

Ensembl

ENSRNOG00000009348; Rattus norvegicus. [Contig view]

GeneID

24600; -.

KEGG

rno:24600; -.

Phylogenomic databases

HOVERGEN

Q62600; -.

Other

ProtoNet

Q62600.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; FAD; FMN; Golgi apparatus; Heme; Iron; Lipoprotein; Membrane; Metal-binding; Myristate; NADP; Oxidoreductase; Palmitate; Phosphoprotein; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 1202`	`1201`	`Nitric oxide synthase, endothelial.`	`PRO_0000170946`
`DOMAIN`	`519 702`	`184`	`Flavodoxin-like.`
`DOMAIN`	`755 1001`	`247`	`FAD-binding FR-type.`
`NP_BIND`	`648 679`	`32`	`FMN (By similarity).`
`NP_BIND`	`792 803`	`12`	`FAD (By similarity).`
`NP_BIND`	`1009 1027`	`19`	`NADP (By similarity).`
`NP_BIND`	`1107 1122`	`16`	`NADP (By similarity).`
`REGION`	`97 485`	`389`	`Interaction with NOSIP (By similarity).`
`REGION`	`489 509`	`21`	`Calmodulin-binding (Potential).`
`COMPBIAS`	`31 68`	`38`	`Pro-rich.`
`METAL`	`93 93`		`Zinc (By similarity).`
`METAL`	`98 98`		`Zinc (By similarity).`
`METAL`	`183 183`		`Iron (heme axial ligand) (By similarity).`
`MOD_RES`	`80 80`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`494 494`		`Phosphothreonine (By similarity).`
`MOD_RES`	`632 632`		`Phosphoserine (By similarity).`
`MOD_RES`	`1174 1174`		`Phosphothreonine (By similarity).`
`MOD_RES`	`1176 1176`		`Phosphoserine (By similarity).`
`LIPID`	`2 2`		`N-myristoyl glycine (By similarity).`
`LIPID`	`15 15`		`S-palmitoyl cysteine (By similarity).`
`LIPID`	`26 26`		`S-palmitoyl cysteine (By similarity).`
`CONFLICT`	`232 233`		`QR -> PS (in Ref. 2; AAC34677).`
`CONFLICT`	`249 249`		`R -> S (in Ref. 2; AAC34677).`
`CONFLICT`	`298 304`		`Missing (in Ref. 3; AAT99567).`
`CONFLICT`	`600 600`		`P -> L (in Ref. 4; CAA09493).`
`CONFLICT`	`735 735`		`R -> G (in Ref. 3; AAT99567).`
`CONFLICT`	`739 739`		`Q -> P (in Ref. 3; AAT99567).`
`CONFLICT`	`748 748`		`R -> G (in Ref. 1; BAD15356).`
`CONFLICT`	`771 771`		`S -> T (in Ref. 3; AAT99567).`
`CONFLICT`	`852 854`		`CTL -> GTV (in Ref. 5; AAA96141).`
`CONFLICT`	`966 966`		`G -> V (in Ref. 1; BAD15356).`
`CONFLICT`	`997 998`		`SF -> FL (in Ref. 3; AAT99567).`

Sequence information

Length: 1202 AA [This is the length of the unprocessed precursor]

Molecular weight: 133290 Da [This is the MW of the unprocessed precursor]

CRC64: 52E905C3134E244D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSQ APVPPSPTRP APDHSPPLTR 

        70         80         90        100        110        120 
PPDGPKFPRV KNWEVGSITY DTLSAQAQQD GPCTPRRCLG SLVFPRKLQS RPTQGPSPTE 

       130        140        150        160        170        180 
QLLGQARDFI NQYYNSIKRS GSQAHEQRLQ EVEAEVVATG TYQLRESELV FGAKQAWRNA 

       190        200        210        220        230        240 
PRCVGRIQWG KLQVFDARDC RTAQEMFTYI CNHIKYATNR GNLRSAITVF PQRYAGRGDF 

       250        260        270        280        290        300 
RIWNSQLVRY AGYRQQDGSV RGDPANVEIT ELCIQHGWTP GNGRFDVLPL LLQAPDEPPE 

       310        320        330        340        350        360 
LFTLPPELVL EVPLEHPTLE WFAALGLRWY ALPAVSNMLL EIGGLEFPAA PFSGWYMSSE 

       370        380        390        400        410        420 
IGMRDLCDPH RYNILEDVAV CMDLDTRTTS SLWKDKAAVE INVAVLYSYQ LAKVTIVDHH 

       430        440        450        460        470        480 
AATASFMKHL ENEQKARGGC PADWAWIVPP ISGSLTPVFH QEMVNYFLSP AFRYQPDPWK 

       490        500        510        520        530        540 
GSAAKGTGIT RKKTFKEVAN AVKISASLMG TVMAKRVKAT ILYGSETGRA QSYAQQLGRL 

       550        560        570        580        590        600 
FRKAFDPRVL CMDEYDVVSL EHEALVLVVT STFGNGDPPE NGESFAAALM EMSGPYNSSP 

       610        620        630        640        650        660 
RPEQHKSYKI RFNSVSCSDP LVSSWRRKRK ESSNTDSAGA LGTLRFCVFG LGSRAYPHFC 

       670        680        690        700        710        720 
AFARAVDTRL EELGGERLLQ LGQGDELCGQ EEAFRGWAQA AFQAACETFC VGEDAKAAAR 

       730        740        750        760        770        780 
DIFSPKRSWK RQRYRLSTQA ESLQLLPRLT HVHRRKMFQA TILSVENLQS SKSTRATILV 

       790        800        810        820        830        840 
RLDTGSQEGL QYQPGDHIGV CPPNRPGLVE ALLSRVEDPP PSTEPVAVEQ LEKGSPGGPP 

       850        860        870        880        890        900 
PGWVRDPRLP PCTLRQALTY FLDITSPPSP RLLRLLSTLA EESSEQQELE ALSQDPRRYE 

       910        920        930        940        950        960 
EWKWFRCPTL LEVLEQFPSV ALPAPLILTQ LPLLQPRYYS VSSAPSAHPG EIHLTVAVLA 

       970        980        990       1000       1010       1020 
YRTQDGLGPL HYGVCSTWMS QLKAGDPVPC FIRGAPSFRL PPDPNLPCIL VGPGTGIAPF 

      1030       1040       1050       1060       1070       1080 
RGFWQDRLHD IEIKGLQPAP MTLVFGCRCS QLDHLYRDEV LDAQQRGVFG QVLTAFSRDP 

      1090       1100       1110       1120       1130       1140 
GSPKTYVQDL LRTELAAEVH RVLCLEQGHM FVCGDVTMAT SVLQTVQRIL ATEGSMELDE 

      1150       1160       1170       1180       1190       1200 
AGDVIGVLRD QQRYHEDIFG LTLRTQEVTS RIRTQSFSLQ ERQLRGAVPW SFDPPTQETP 


GS

Q62600 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools