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Nitric oxide synthase, endothelial (EC 1.14.13.39) (Constitutive NOS) (cNOS) (EC-NOS) (Endothelial NOS) (eNOS) (NOS type III) (NOSIII)

 NOS3_BOVIN              Reviewed;        1205 AA.
P29473;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 190.
RecName: Full=Nitric oxide synthase, endothelial;
EC=1.14.13.39;
AltName: Full=Constitutive NOS;
Short=cNOS;
AltName: Full=EC-NOS;
AltName: Full=Endothelial NOS;
Short=eNOS;
AltName: Full=NOS type III;
Short=NOSIII;
Name=NOS3;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1378626; DOI=10.1073/pnas.89.14.6348;
Lamas S., Marsden P.A., Li G.K., Tempst P., Michel T.;
"Endothelial nitric oxide synthase: molecular cloning and
characterization of a distinct constitutive enzyme isoform.";
Proc. Natl. Acad. Sci. U.S.A. 89:6348-6352(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1385480; DOI=10.1172/JCI116092;
Nishida K., Harrison D.G., Navas J.P., Fisher A.A., Dockery S.P.,
Uematsu M., Nerem R.M., Alexander R.W., Murphy T.J.;
"Molecular cloning and characterization of the constitutive bovine
aortic endothelial cell nitric oxide synthase.";
J. Clin. Invest. 90:2092-2096(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aortic endothelium;
PubMed=1379225;
Sessa W.C., Harrison J.K., Barber C.M., Zeng D., Durieux M.E.,
D'Angelo D.D., Lynch K.R., Peach M.J.;
"Molecular cloning and expression of a cDNA encoding endothelial cell
nitric oxide synthase.";
J. Biol. Chem. 267:15274-15276(1992).
[4]
MYRISTOYLATION AT GLY-2.
PubMed=7682550;
Busconi L., Michel T.;
"Endothelial nitric oxide synthase. N-terminal myristoylation
determines subcellular localization.";
J. Biol. Chem. 268:8410-8413(1993).
[5]
PALMITOYLATION AT CYS-15 AND CYS-26.
PubMed=8524847; DOI=10.1073/pnas.92.25.11776;
Robinson L.J., Michel T.;
"Mutagenesis of palmitoylation sites in endothelial nitric oxide
synthase identifies a novel motif for dual acylation and subcellular
targeting.";
Proc. Natl. Acad. Sci. U.S.A. 92:11776-11780(1995).
[6]
PHOSPHORYLATION AT THR-497; SER-635 AND SER-1179.
PubMed=12384459; DOI=10.1152/ajpheart.00214.2002;
Boo Y.C., Hwang J., Sykes M., Michell B.J., Kemp B.E., Lum H., Jo H.;
"Shear stress stimulates phosphorylation of eNOS at Ser(635) by a
protein kinase A-dependent mechanism.";
Am. J. Physiol. 283:H1819-H1828(2002).
[7]
SUBCELLULAR LOCATION.
PubMed=17071725; DOI=10.1152/ajpheart.00990.2006;
Mukhopadhyay S., Xu F., Sehgal P.B.;
"Aberrant cytoplasmic sequestration of eNOS in endothelial cells after
monocrotaline, hypoxia, and senescence: live-cell caveolar and
cytoplasmic NO imaging.";
Am. J. Physiol. 292:H1373-H1389(2007).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 67-482.
PubMed=9875848; DOI=10.1016/S0092-8674(00)81718-3;
Raman C.S., Li H., Martasek P., Kral V., Masters B.S.S., Poulos T.L.;
"Crystal structure of constitutive endothelial nitric oxide synthase:
a paradigm for pterin function involving a novel metal center.";
Cell 95:939-950(1998).
[9]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 67-482.
PubMed=11051558; DOI=10.1016/S0162-0134(00)00099-4;
Li H., Raman C.S., Martasek P., Kral V., Masters B.S.S., Poulos T.L.;
"Mapping the active site polarity in structures of endothelial nitric
oxide synthase heme domain complexed with isothioureas.";
J. Inorg. Biochem. 81:133-139(2000).
[10]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
PubMed=11331003; DOI=10.1021/bi002658v;
Li H., Raman C.S., Martasek P., Masters B.S.S., Poulos T.L.;
"Crystallographic studies on endothelial nitric oxide synthase
complexed with nitric oxide and mechanism-based inhibitors.";
Biochemistry 40:5399-5406(2001).
[11]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
PubMed=11695891; DOI=10.1021/bi010957u;
Raman C.S., Li H., Martasek P., Southan G., Masters B.S.S.,
Poulos T.L.;
"Crystal structure of nitric oxide synthase bound to nitro indazole
reveals a novel inactivation mechanism.";
Biochemistry 40:13448-13455(2001).
[12]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
PubMed=11331290; DOI=10.1074/jbc.M102255200;
Raman C.S., Li H., Martasek P., Babu B.R., Griffith O.W., Southan G.,
Masters B.S.S., Poulos T.L.;
"Implications for isoform-selective inhibitor design derived from the
binding mode of bulky isothioureas to the heme domain of endothelial
nitric-oxide synthase.";
J. Biol. Chem. 276:26486-26491(2001).
[13]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
PubMed=11590164; DOI=10.1074/jbc.M011469200;
Kotsonis P., Frohlich L.G., Raman C.S., Li H., Berg M., Gerwig R.,
Groehn V., Kang Y., Al-Masoudi N., Taghavi-Moghadam S., Mohr D.,
Munch U., Schnabel J., Martasek P., Masters B.S.S., Strobel H.,
Poulos T., Matter H., Pfleiderer W., Schmidt H.H.H.W.;
"Structural basis for pterin antagonism in nitric-oxide synthase.
Development of novel 4-oxo-pteridine antagonists of (6R)-5,6,7,8-
tetrahydrobiopterin.";
J. Biol. Chem. 276:49133-49141(2001).
-!- 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: 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;
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Note=Binds 1 FAD.;
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Note=Binds 1 FMN.;
-!- COFACTOR:
Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
Xref=ChEBI:CHEBI:59560;
Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of
the enzyme.;
-!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by
NOSIP and NOSTRIN (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By
similarity). Interacts with HSP90AB1 (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P29474}.
-!- INTERACTION:
Q7JFY6:- (xeno); NbExp=5; IntAct=EBI-7636493, EBI-7636483;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17071725}.
Membrane, caveola {ECO:0000269|PubMed:17071725}. Cytoplasm,
cytoskeleton {ECO:0000250}. Golgi apparatus
{ECO:0000269|PubMed:17071725}. 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. {ECO:0000250}.
-!- PTM: Phosphorylation by AMPK at Ser-1179 in the presence of
Ca(2+)-calmodulin (CaM) activates activity. In absence of Ca(2+)-
calmodulin, AMPK also phosphorylates Thr-497, resulting in
inhibition of activity. Phosphorylation of Ser-116 by CDK5 reduces
activity (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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EMBL; M99057; AAA30667.1; -; mRNA.
EMBL; M89952; AAA30494.1; -; mRNA.
EMBL; M95674; AAA30669.1; -; mRNA.
PIR; A38943; A38943.
UniGene; Bt.4662; -.
PDB; 1D0C; X-ray; 1.65 A; A/B=39-482.
PDB; 1D0O; X-ray; 1.95 A; A/B=39-482.
PDB; 1D1V; X-ray; 1.93 A; A/B=39-482.
PDB; 1D1W; X-ray; 2.00 A; A/B=39-482.
PDB; 1D1X; X-ray; 2.00 A; A/B=39-482.
PDB; 1D1Y; X-ray; 2.20 A; A/B=39-482.
PDB; 1DM6; X-ray; 1.95 A; A/B=39-482.
PDB; 1DM7; X-ray; 2.10 A; A/B=39-482.
PDB; 1DM8; X-ray; 2.25 A; A/B=39-482.
PDB; 1DMI; X-ray; 2.00 A; A/B=39-482.
PDB; 1DMJ; X-ray; 2.35 A; A/B=39-482.
PDB; 1DMK; X-ray; 1.90 A; A/B=39-482.
PDB; 1ED4; X-ray; 1.86 A; A/B=39-482.
PDB; 1ED5; X-ray; 1.80 A; A/B=39-482.
PDB; 1ED6; X-ray; 2.05 A; A/B=39-482.
PDB; 1FOI; X-ray; 1.93 A; A/B=39-482.
PDB; 1FOJ; X-ray; 2.10 A; A/B=39-482.
PDB; 1FOL; X-ray; 2.20 A; A/B=39-482.
PDB; 1FOO; X-ray; 2.00 A; A/B=39-482.
PDB; 1FOP; X-ray; 2.30 A; A/B=39-482.
PDB; 1I83; X-ray; 2.00 A; A/B=39-482.
PDB; 1NSE; X-ray; 1.90 A; A/B=39-482.
PDB; 1P6L; X-ray; 2.35 A; A/B=67-483.
PDB; 1P6M; X-ray; 2.27 A; A/B=67-483.
PDB; 1P6N; X-ray; 2.50 A; A/B=67-483.
PDB; 1Q2O; X-ray; 1.74 A; A/B=67-482.
PDB; 1RS8; X-ray; 2.30 A; A/B=67-482.
PDB; 1RS9; X-ray; 2.22 A; A/B=67-482.
PDB; 1ZZS; X-ray; 1.85 A; A/B=67-482.
PDB; 1ZZT; X-ray; 2.14 A; A/B=67-482.
PDB; 2G6O; X-ray; 1.90 A; A/B=67-482.
PDB; 2HX2; X-ray; 1.95 A; A/B=67-482.
PDB; 2NSE; X-ray; 2.34 A; A/B=39-482.
PDB; 3DQS; X-ray; 2.03 A; A/B=67-482.
PDB; 3DQT; X-ray; 2.54 A; A/B=67-482.
PDB; 3E7S; X-ray; 2.50 A; A/B=57-487.
PDB; 3JWW; X-ray; 2.20 A; A/B=39-482.
PDB; 3JWX; X-ray; 2.00 A; A/B=39-482.
PDB; 3JWY; X-ray; 2.24 A; A/B=39-482.
PDB; 3JWZ; X-ray; 2.40 A; A/B=39-482.
PDB; 3N5P; X-ray; 2.39 A; A/B=39-482.
PDB; 3N5Q; X-ray; 2.90 A; A/B=39-482.
PDB; 3N5R; X-ray; 2.57 A; A/B=39-482.
PDB; 3N5S; X-ray; 2.18 A; A/B=39-482.
PDB; 3N5T; X-ray; 2.52 A; A/B=39-482.
PDB; 3NLD; X-ray; 2.28 A; A/B=39-482.
PDB; 3NLE; X-ray; 1.95 A; A/B=39-482.
PDB; 3NLF; X-ray; 2.32 A; A/B=39-482.
PDB; 3NLG; X-ray; 2.38 A; A/B=39-482.
PDB; 3NLH; X-ray; 2.10 A; A/B=39-482.
PDB; 3NLI; X-ray; 1.98 A; A/B=39-482.
PDB; 3NLT; X-ray; 2.74 A; A/B=39-482.
PDB; 3NLU; X-ray; 2.65 A; A/B=39-482.
PDB; 3NSE; X-ray; 2.10 A; A/B=39-482.
PDB; 3PNH; X-ray; 1.93 A; A/B=67-482.
PDB; 3RQO; X-ray; 2.08 A; A/B=40-482.
PDB; 3RQP; X-ray; 2.35 A; A/B=40-482.
PDB; 4C3A; X-ray; 2.20 A; A/B=40-482.
PDB; 4CAR; X-ray; 2.05 A; A/B=40-482.
PDB; 4CFT; X-ray; 1.79 A; A/B=40-482.
PDB; 4CTY; X-ray; 2.30 A; A/B=40-482.
PDB; 4CTZ; X-ray; 2.01 A; A/B=40-482.
PDB; 4CU0; X-ray; 2.08 A; A/B=40-482.
PDB; 4CU1; X-ray; 1.89 A; A/B=40-482.
PDB; 4CUL; X-ray; 2.23 A; A/B=40-482.
PDB; 4CUM; X-ray; 2.33 A; A/B=40-482.
PDB; 4CUN; X-ray; 2.48 A; A/B=40-482.
PDB; 4CVG; X-ray; 2.31 A; A/B=40-482.
PDB; 4CWV; X-ray; 2.34 A; A/B=40-482.
PDB; 4CWW; X-ray; 2.16 A; A/B=40-482.
PDB; 4CWX; X-ray; 2.15 A; A/B=40-482.
PDB; 4CWY; X-ray; 2.15 A; A/B=40-482.
PDB; 4CWZ; X-ray; 2.08 A; A/B=40-482.
PDB; 4CX0; X-ray; 2.20 A; A/B=40-482.
PDB; 4CX1; X-ray; 2.13 A; A/B=40-482.
PDB; 4CX2; X-ray; 2.04 A; A/B=40-482.
PDB; 4D33; X-ray; 2.09 A; A/B=40-482.
PDB; 4D34; X-ray; 2.25 A; A/B=40-482.
PDB; 4D35; X-ray; 2.18 A; A/B=40-482.
PDB; 4D36; X-ray; 2.05 A; A/B=40-482.
PDB; 4D37; X-ray; 2.10 A; A/B=40-482.
PDB; 4D38; X-ray; 2.30 A; A/B=40-482.
PDB; 4D39; X-ray; 2.00 A; A/B=40-482.
PDB; 4D3A; X-ray; 2.25 A; A/B=40-482.
PDB; 4IMX; X-ray; 2.25 A; A/B=40-482.
PDB; 4JSK; X-ray; 2.28 A; A/B=40-482.
PDB; 4JSL; X-ray; 2.04 A; A/B=40-482.
PDB; 4JSM; X-ray; 2.25 A; A/B=40-482.
PDB; 4K5H; X-ray; 2.25 A; A/B=40-482.
PDB; 4K5I; X-ray; 2.08 A; A/B=40-482.
PDB; 4K5J; X-ray; 2.36 A; A/B=40-482.
PDB; 4K5K; X-ray; 2.00 A; A/B=40-482.
PDB; 4KCP; X-ray; 2.07 A; A/B=40-482.
PDB; 4KCQ; X-ray; 2.03 A; A/B=40-482.
PDB; 4KCR; X-ray; 2.09 A; A/B=40-482.
PDB; 4KCS; X-ray; 2.05 A; A/B=40-482.
PDB; 4LUW; X-ray; 2.25 A; A/B=41-482.
PDB; 4NSE; X-ray; 1.95 A; A/B=39-482.
PDB; 4UH7; X-ray; 2.23 A; A/B=40-482.
PDB; 4UH8; X-ray; 2.30 A; A/B=40-482.
PDB; 4UH9; X-ray; 2.14 A; A/B=40-482.
PDB; 4UHA; X-ray; 2.20 A; A/B=40-482.
PDB; 4UPQ; X-ray; 2.03 A; A/B=40-482.
PDB; 4UPR; X-ray; 1.93 A; A/B=40-482.
PDB; 4UPS; X-ray; 1.95 A; A/B=40-482.
PDB; 4UPT; X-ray; 2.20 A; A/B=40-482.
PDB; 5ADJ; X-ray; 2.22 A; A/B=40-482.
PDB; 5ADK; X-ray; 1.80 A; A/B=40-482.
PDB; 5ADL; X-ray; 2.21 A; A/B=40-482.
PDB; 5ADM; X-ray; 2.20 A; A/B=40-482.
PDB; 5ADN; X-ray; 2.00 A; A/B=40-482.
PDB; 5FJ2; X-ray; 2.05 A; A/B=40-482.
PDB; 5FJ3; X-ray; 2.20 A; A/B=40-482.
PDB; 5FVY; X-ray; 2.10 A; A/B=40-482.
PDB; 5FVZ; X-ray; 2.05 A; A/B=40-482.
PDB; 5NSE; X-ray; 1.90 A; A/B=39-482.
PDB; 5UOD; X-ray; 2.01 A; A/B=40-482.
PDB; 6NSE; X-ray; 2.35 A; A/B=39-482.
PDB; 7NSE; X-ray; 2.35 A; A/B=39-482.
PDB; 8NSE; X-ray; 2.25 A; A/B=39-482.
PDB; 9NSE; X-ray; 2.24 A; A/B=39-482.
PDBsum; 1D0C; -.
PDBsum; 1D0O; -.
PDBsum; 1D1V; -.
PDBsum; 1D1W; -.
PDBsum; 1D1X; -.
PDBsum; 1D1Y; -.
PDBsum; 1DM6; -.
PDBsum; 1DM7; -.
PDBsum; 1DM8; -.
PDBsum; 1DMI; -.
PDBsum; 1DMJ; -.
PDBsum; 1DMK; -.
PDBsum; 1ED4; -.
PDBsum; 1ED5; -.
PDBsum; 1ED6; -.
PDBsum; 1FOI; -.
PDBsum; 1FOJ; -.
PDBsum; 1FOL; -.
PDBsum; 1FOO; -.
PDBsum; 1FOP; -.
PDBsum; 1I83; -.
PDBsum; 1NSE; -.
PDBsum; 1P6L; -.
PDBsum; 1P6M; -.
PDBsum; 1P6N; -.
PDBsum; 1Q2O; -.
PDBsum; 1RS8; -.
PDBsum; 1RS9; -.
PDBsum; 1ZZS; -.
PDBsum; 1ZZT; -.
PDBsum; 2G6O; -.
PDBsum; 2HX2; -.
PDBsum; 2NSE; -.
PDBsum; 3DQS; -.
PDBsum; 3DQT; -.
PDBsum; 3E7S; -.
PDBsum; 3JWW; -.
PDBsum; 3JWX; -.
PDBsum; 3JWY; -.
PDBsum; 3JWZ; -.
PDBsum; 3N5P; -.
PDBsum; 3N5Q; -.
PDBsum; 3N5R; -.
PDBsum; 3N5S; -.
PDBsum; 3N5T; -.
PDBsum; 3NLD; -.
PDBsum; 3NLE; -.
PDBsum; 3NLF; -.
PDBsum; 3NLG; -.
PDBsum; 3NLH; -.
PDBsum; 3NLI; -.
PDBsum; 3NLT; -.
PDBsum; 3NLU; -.
PDBsum; 3NSE; -.
PDBsum; 3PNH; -.
PDBsum; 3RQO; -.
PDBsum; 3RQP; -.
PDBsum; 4C3A; -.
PDBsum; 4CAR; -.
PDBsum; 4CFT; -.
PDBsum; 4CTY; -.
PDBsum; 4CTZ; -.
PDBsum; 4CU0; -.
PDBsum; 4CU1; -.
PDBsum; 4CUL; -.
PDBsum; 4CUM; -.
PDBsum; 4CUN; -.
PDBsum; 4CVG; -.
PDBsum; 4CWV; -.
PDBsum; 4CWW; -.
PDBsum; 4CWX; -.
PDBsum; 4CWY; -.
PDBsum; 4CWZ; -.
PDBsum; 4CX0; -.
PDBsum; 4CX1; -.
PDBsum; 4CX2; -.
PDBsum; 4D33; -.
PDBsum; 4D34; -.
PDBsum; 4D35; -.
PDBsum; 4D36; -.
PDBsum; 4D37; -.
PDBsum; 4D38; -.
PDBsum; 4D39; -.
PDBsum; 4D3A; -.
PDBsum; 4IMX; -.
PDBsum; 4JSK; -.
PDBsum; 4JSL; -.
PDBsum; 4JSM; -.
PDBsum; 4K5H; -.
PDBsum; 4K5I; -.
PDBsum; 4K5J; -.
PDBsum; 4K5K; -.
PDBsum; 4KCP; -.
PDBsum; 4KCQ; -.
PDBsum; 4KCR; -.
PDBsum; 4KCS; -.
PDBsum; 4LUW; -.
PDBsum; 4NSE; -.
PDBsum; 4UH7; -.
PDBsum; 4UH8; -.
PDBsum; 4UH9; -.
PDBsum; 4UHA; -.
PDBsum; 4UPQ; -.
PDBsum; 4UPR; -.
PDBsum; 4UPS; -.
PDBsum; 4UPT; -.
PDBsum; 5ADJ; -.
PDBsum; 5ADK; -.
PDBsum; 5ADL; -.
PDBsum; 5ADM; -.
PDBsum; 5ADN; -.
PDBsum; 5FJ2; -.
PDBsum; 5FJ3; -.
PDBsum; 5FVY; -.
PDBsum; 5FVZ; -.
PDBsum; 5NSE; -.
PDBsum; 5UOD; -.
PDBsum; 6NSE; -.
PDBsum; 7NSE; -.
PDBsum; 8NSE; -.
PDBsum; 9NSE; -.
ProteinModelPortal; P29473; -.
SMR; P29473; -.
DIP; DIP-42217N; -.
ELM; P29473; -.
IntAct; P29473; 2.
MINT; MINT-1347838; -.
STRING; 9913.ENSBTAP00000023515; -.
BindingDB; P29473; -.
ChEMBL; CHEMBL4802; -.
iPTMnet; P29473; -.
SwissPalm; P29473; -.
PaxDb; P29473; -.
PRIDE; P29473; -.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
eggNOG; COG4362; LUCA.
HOGENOM; HOG000220884; -.
HOVERGEN; HBG000159; -.
InParanoid; P29473; -.
BRENDA; 1.14.13.39; 908.
EvolutionaryTrace; P29473; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:GO_Central.
GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:0006527; P:arginine catabolic process; IDA:BHF-UCL.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; IMP:BHF-UCL.
GO; GO:0007005; P:mitochondrion organization; IMP:BHF-UCL.
GO; GO:0045776; P:negative regulation of blood pressure; IBA:GO_Central.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IMP:BHF-UCL.
GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IBA:GO_Central.
GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IMP:BHF-UCL.
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; 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.
PIRSF; PIRSF000333; NOS; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
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.
1: Evidence at protein level;
3D-structure; Blood coagulation; Calcium; Calmodulin-binding;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; FAD;
Flavoprotein; FMN; Golgi apparatus; Heme; Hemostasis; Iron;
Lipoprotein; Membrane; Metal-binding; Myristate; NADP; Oxidoreductase;
Palmitate; Phosphoprotein; Reference proteome; Zinc.
INIT_MET 1 1 Removed.
CHAIN 2 1205 Nitric oxide synthase, endothelial.
/FTId=PRO_0000170941.
DOMAIN 522 705 Flavodoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
DOMAIN 758 1004 FAD-binding FR-type.
{ECO:0000255|PROSITE-ProRule:PRU00716}.
NP_BIND 651 682 FMN. {ECO:0000255|PROSITE-
ProRule:PRU00088}.
NP_BIND 795 806 FAD. {ECO:0000250}.
NP_BIND 937 947 FAD. {ECO:0000250}.
NP_BIND 1012 1030 NADP. {ECO:0000250}.
NP_BIND 1110 1125 NADP. {ECO:0000250}.
REGION 100 488 Interaction with NOSIP. {ECO:0000250}.
REGION 492 512 Calmodulin-binding. {ECO:0000255}.
METAL 96 96 Zinc.
METAL 101 101 Zinc.
METAL 186 186 Iron (heme axial ligand).
MOD_RES 116 116 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P29474}.
MOD_RES 497 497 Phosphothreonine; by AMPK and PKA.
{ECO:0000269|PubMed:12384459}.
MOD_RES 617 617 Phosphoserine.
{ECO:0000250|UniProtKB:P70313}.
MOD_RES 635 635 Phosphoserine.
{ECO:0000269|PubMed:12384459}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000250|UniProtKB:P29474}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000250|UniProtKB:P29474}.
MOD_RES 1177 1177 Phosphothreonine.
{ECO:0000250|UniProtKB:P70313}.
MOD_RES 1179 1179 Phosphoserine; by AMPK, PDPK1 and PKA.
{ECO:0000269|PubMed:12384459}.
MOD_RES 1181 1181 Phosphoserine.
{ECO:0000250|UniProtKB:P70313}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:7682550}.
LIPID 15 15 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8524847}.
LIPID 26 26 S-palmitoyl cysteine.
{ECO:0000269|PubMed:8524847}.
CONFLICT 100 100 C -> R (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 165 165 Y -> I (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 318 328 EHPTLEWFAAL -> GAPHTGVVRGP (in Ref. 3;
AAA30669). {ECO:0000305}.
CONFLICT 455 455 S -> Y (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 459 459 T -> P (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 741 741 T -> A (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 804 805 CP -> SA (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 857 857 L -> V (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 907 908 WF -> LV (in Ref. 3; AAA30669).
{ECO:0000305}.
CONFLICT 1042 1042 A -> H (in Ref. 3; AAA30669).
{ECO:0000305}.
STRAND 67 70 {ECO:0000244|PDB:3E7S}.
STRAND 72 75 {ECO:0000244|PDB:1D0C}.
TURN 76 79 {ECO:0000244|PDB:1D0C}.
STRAND 80 83 {ECO:0000244|PDB:1D0C}.
HELIX 86 89 {ECO:0000244|PDB:1D0C}.
STRAND 98 101 {ECO:0000244|PDB:1DMK}.
TURN 109 111 {ECO:0000244|PDB:1D0C}.
STRAND 117 119 {ECO:0000244|PDB:8NSE}.
HELIX 122 139 {ECO:0000244|PDB:1D0C}.
HELIX 146 162 {ECO:0000244|PDB:1D0C}.
HELIX 169 181 {ECO:0000244|PDB:1D0C}.
HELIX 189 191 {ECO:0000244|PDB:1D0C}.
STRAND 196 199 {ECO:0000244|PDB:1D0C}.
HELIX 206 221 {ECO:0000244|PDB:1D0C}.
HELIX 222 224 {ECO:0000244|PDB:1D0C}.
STRAND 229 232 {ECO:0000244|PDB:1D0C}.
STRAND 238 240 {ECO:0000244|PDB:4CFT}.
STRAND 247 251 {ECO:0000244|PDB:1D0C}.
STRAND 255 257 {ECO:0000244|PDB:1D0C}.
STRAND 259 261 {ECO:0000244|PDB:4NSE}.
STRAND 263 265 {ECO:0000244|PDB:1D0C}.
HELIX 267 269 {ECO:0000244|PDB:1D0C}.
HELIX 270 278 {ECO:0000244|PDB:1D0C}.
STRAND 286 288 {ECO:0000244|PDB:1D0C}.
STRAND 293 296 {ECO:0000244|PDB:1D0C}.
STRAND 303 305 {ECO:0000244|PDB:1D0C}.
HELIX 309 311 {ECO:0000244|PDB:1D0C}.
STRAND 314 316 {ECO:0000244|PDB:1D0C}.
HELIX 323 328 {ECO:0000244|PDB:1D0C}.
STRAND 331 334 {ECO:0000244|PDB:1D0C}.
STRAND 342 345 {ECO:0000244|PDB:1D0C}.
STRAND 348 351 {ECO:0000244|PDB:1D0C}.
HELIX 361 365 {ECO:0000244|PDB:1D0C}.
HELIX 367 370 {ECO:0000244|PDB:1D0C}.
TURN 372 375 {ECO:0000244|PDB:1D0C}.
HELIX 378 384 {ECO:0000244|PDB:1D0C}.
HELIX 392 394 {ECO:0000244|PDB:1D0C}.
HELIX 396 414 {ECO:0000244|PDB:1D0C}.
HELIX 422 440 {ECO:0000244|PDB:1D0C}.
HELIX 447 450 {ECO:0000244|PDB:1D0C}.
STRAND 453 455 {ECO:0000244|PDB:1D0C}.
HELIX 456 458 {ECO:0000244|PDB:1D0C}.
HELIX 460 463 {ECO:0000244|PDB:1D0C}.
STRAND 468 470 {ECO:0000244|PDB:3E7S}.
STRAND 472 476 {ECO:0000244|PDB:1D0C}.
SEQUENCE 1205 AA; 133287 MW; 5DC8FF4F25870281 CRC64;
MGNLKSVGQE PGPPCGLGLG LGLGLCGKQG PASPAPEPSR APAPATPHAP DHSPAPNSPT
LTRPPEGPKF PRVKNWELGS ITYDTLCAQS QQDGPCTPRC CLGSLVLPRK LQTRPSPGPP
PAEQLLSQAR DFINQYYSSI KRSGSQAHEE RLQEVEAEVA STGTYHLRES ELVFGAKQAW
RNAPRCVGRI QWGKLQVFDA RDCSSAQEMF TYICNHIKYA TNRGNLRSAI TVFPQRAPGR
GDFRIWNSQL VRYAGYRQQD GSVRGDPANV EITELCIQHG WTPGNGRFDV LPLLLQAPDE
APELFVLPPE LVLEVPLEHP TLEWFAALGL RWYALPAVSN MLLEIGGLEF SAAPFSGWYM
STEIGTRNLC DPHRYNILED VAVCMDLDTR TTSSLWKDKA AVEINLAVLH SFQLAKVTIV
DHHAATVSFM KHLDNEQKAR GGCPADWAWI VPPISGSLTP VFHQEMVNYI LSPAFRYQPD
PWKGSATKGA GITRKKTFKE VANAVKISAS LMGTLMAKRV KATILYASET GRAQSYAQQL
GRLFRKAFDP RVLCMDEYDV VSLEHEALVL VVTSTFGNGD PPENGESFAA ALMEMSGPYN
SSPRPEQHKS YKIRFNSVSC SDPLVSSWRR KRKESSNTDS AGALGTLRFC VFGLGSRAYP
HFCAFARAVD TRLEELGGER LLQLGQGDEL CGQEEAFRGW AKAAFQASCE TFCVGEEAKA
AAQDIFSPKR SWKRQRYRLS TQAEGLQLLP GLIHVHRRKM FQATVLSVEN LQSSKSTRAT
ILVRLDTAGQ EGLQYQPGDH IGICPPNRPG LVEALLSRVE DPPPPTESVA VEQLEKGSPG
GPPPSWVRDP RLPPCTLRQA LTFFLDITSP PSPRLLRLLS TLAEEPSEQQ ELETLSQDPR
RYEEWKWFRC PTLLEVLEQF PSVALPAPLL LTQLPLLQPR YYSVSSAPNA HPGEVHLTVA
VLAYRTQDGL GPLHYGVCST WLSQLKTGDP VPCFIRGAPS FRLPPDPYVP CILVGPGTGI
APFRGFWQER LHDIESKGLQ PAPMTLVFGC RCSQLDHLYR DEVQDAQERG VFGRVLTAFS
REPDSPKTYV QDILRTELAA EVHRVLCLER GHMFVCGDVT MATSVLQTVQ RILATEGDME
LDEAGDVIGV LRDQQRYHED IFGLTLRTQE VTSRIRTQSF SLQERHLRGA VPWAFDPPGP
DTPGP


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