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 11-JUL-2012, entry version 76. 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). CC -!- CATALYTIC ACTIVITY: L-arginine + n NADPH + n H(+) + m O(2) = CC citrulline + nitric oxide + n NADP(+). CC -!- COFACTOR: Heme group (By similarity). CC -!- COFACTOR: Binds 1 FAD (By similarity). CC -!- COFACTOR: Binds 1 FMN (By similarity). CC -!- COFACTOR: Tetrahydrobiopterin (BH4). May stabilize the dimeric CC form of the enzyme (By similarity). CC -!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by CC NOSIP and NOSTRIN (By similarity). CC -!- SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By CC similarity). CC -!- SUBCELLULAR LOCATION: Membrane, caveola (By similarity). CC Cytoplasm, cytoskeleton (By similarity). Golgi apparatus (By CC similarity). Cell membrane (By similarity). Note=Specifically CC associates with actin cytoskeleton in the G2 phase of the cell CC cycle, which is favored by interaction with NOSIP and results in a CC reduced enzymatic activity (By similarity). CC -!- SIMILARITY: Belongs to the NOS family. 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 ProteinModelPortal; P79209; -. DR SMR; P79209; 1-99. 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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004517; F:nitric-oxide synthase activity; IEA:EC. DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro. DR InterPro; IPR012144; Nitric-oxide_synthase. DR InterPro; IPR004030; NO_synthase_oxygenase_dom. DR PANTHER; PTHR19384:SF5; PTHR19384:SF5; 1. DR Pfam; PF02898; NO_synthase; 1. DR SUPFAM; SSF56512; NO_synthase_oxygenase_reg; 1. DR PROSITE; PS60001; NOS; PARTIAL. PE 3: Inferred from homology; KW Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; KW FAD; FMN; Golgi apparatus; Heme; Iron; Membrane; Metal-binding; NADP; KW Oxidoreductase. 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 //