NOS3_CAVPO
ID NOS3_CAVPO Reviewed; 100 AA.
AC P97270;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endothelial cell;
RX PubMed=9838160; DOI=10.1016/s0165-3806(98)00145-x;
RA Aguan K., Murotsuki J., Gagnon R., Thompson L.P., Weiner C.P.;
RT "Effect of chronic hypoxemia on the regulation of nitric-oxide synthase in
RT the fetal sheep brain.";
RL Brain Res. Dev. Brain Res. 111:271-277(1998).
CC -!- FUNCTION: Produces nitric oxide (NO) which is implicated in vascular
CC smooth muscle relaxation through a cGMP-mediated signal transduction
CC pathway. NO mediates vascular endothelial growth factor (VEGF)-induced
CC angiogenesis in coronary vessels and promotes blood clotting through
CC the activation of platelets (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; 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=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250};
CC Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC enzyme. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin. Inhibited by
CC NOSIP and NOSTRIN (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with NOSIP and NOSTRIN (By similarity).
CC Interacts with HSP90AB1 (By similarity). Forms a complex with ASL, ASS1
CC and SLC7A1; the complex regulates cell-autonomous L-arginine synthesis
CC and citrulline recycling while channeling extracellular L-arginine to
CC nitric oxide synthesis pathway (By similarity).
CC {ECO:0000250|UniProtKB:P29474, ECO:0000250|UniProtKB:P70313}.
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 by
CC interaction with NOSIP and results in a reduced enzymatic activity.
CC {ECO:0000250}.
CC -!- INDUCTION: Repressed by hypoxemia in fetal brain.
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; U76736; AAB40703.1; -; mRNA.
DR AlphaFoldDB; P97270; -.
DR SMR; P97270; -.
DR STRING; 10141.ENSCPOP00000003945; -.
DR InParanoid; P97270; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
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 Gene3D; 3.90.1230.10; -; 1.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR Pfam; PF02898; NO_synthase; 1.
DR SUPFAM; SSF56512; SSF56512; 1.
PE 2: Evidence at transcript level;
KW Calcium; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton; FAD;
KW Flavoprotein; FMN; Golgi apparatus; Heme; Iron; Membrane; Metal-binding;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN <1..>100
FT /note="Nitric oxide synthase, endothelial"
FT /id="PRO_0000170942"
FT REGION 81..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 2
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 6
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 11
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 92
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT NON_TER 1
FT NON_TER 100
SQ SEQUENCE 100 AA; 11271 MW; 867D7F89F4B132A8 CRC64;
WYMSTEIGTR NLCDPHRYNI LEDVAVCMDL DTRTTSSLWK DKAAVEINVA VLHSYQLAKV
TIVDHHAATV SFMKHLENEQ KGRGGCPADW GWDPCPPSRA
