ID NOS3_SHEEP Reviewed; 99 AA. AC P79209; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 16-SEP-2015, entry version 91. DE RecName: Full=Nitric oxide synthase, endothelial; DE EC=1.14.13.39; DE AltName: Full=Constitutive NOS; DE Short=cNOS; DE AltName: Full=EC-NOS; DE AltName: Full=Endothelial NOS; DE Short=eNOS; DE AltName: Full=NOS type III; DE Short=NOSIII; DE Flags: Fragment; GN Name=NOS3; Synonyms=ENOS; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Endothelial cell; RA Aguan K., Weiner C.P.; RT "Effect of hypoxia on the microvasculature of developing fetal brain RT of sheep: a studies on the expression pattern of constitutive forms of RT nitric oxide synthase."; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Produces nitric oxide (NO) which is implicated in CC vascular smooth muscle relaxation through a cGMP-mediated signal CC transduction pathway. NO mediates vascular endothelial growth CC factor (VEGF)-induced angiogenesis in coronary vessels and CC promotes blood clotting through the activation of platelets (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 L-arginine + 3 NADPH + 4 O(2) = 2 L- CC citrulline + 2 nitric oxide + 3 NADP(+) + 4 H(2)O. CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD. {ECO:0000250}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN. {ECO:0000250}; CC -!- COFACTOR: CC Name=5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:15372; CC Evidence={ECO:0000250}; CC Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of CC the enzyme. {ECO:0000250}; CC -!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by CC NOSIP and NOSTRIN (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane, caveola {ECO:0000250}. Cytoplasm, CC cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell CC membrane {ECO:0000250}. Note=Specifically associates with actin CC cytoskeleton in the G2 phase of the cell cycle, which is favored CC by interaction with NOSIP and results in a reduced enzymatic CC activity. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U76738; AAB40705.1; -; mRNA. DR UniGene; Oar.521; -. DR UniGene; Oar.6941; -. DR ProteinModelPortal; P79209; -. DR Proteomes; UP000002356; Unplaced. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro. DR InterPro; IPR004030; NOS_N. DR Pfam; PF02898; NO_synthase; 1. DR SUPFAM; SSF56512; SSF56512; 1. PE 2: Evidence at transcript level; KW Calcium; Calmodulin-binding; Cell membrane; Complete proteome; KW Cytoplasm; Cytoskeleton; FAD; Flavoprotein; FMN; Golgi apparatus; KW Heme; Iron; Membrane; Metal-binding; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN <1 >99 Nitric oxide synthase, endothelial. FT /FTId=PRO_0000170947. FT NON_TER 1 1 FT NON_TER 99 99 SQ SEQUENCE 99 AA; 11034 MW; 82C3C765557031DA CRC64; VAVCMDLDTR TTSSLWKDKA AVEINLAVLH SFQLAKVTIV DHHAATVSFM KHLENEQKAR GGCPADWAWI VPPISGSLTP VFHQEMVNYV LSPAFRYQP //