P79209 · NOS3_SHEEP

  • Protein
    Nitric oxide synthase 3
  • Gene
    NOS3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

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 (By similarity).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
heme b (UniProtKB | Rhea| CHEBI:60344 )

FAD (UniProtKB | Rhea| CHEBI:57692 )

Note: Binds 1 FAD.
FMN (UniProtKB | Rhea| CHEBI:58210 )

Note: Binds 1 FMN.
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | Rhea| CHEBI:59560 )

Note: Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.

Activity regulation

Stimulated by calcium/calmodulin. Inhibited by NOSIP and NOSTRIN (By similarity).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site96Zn2+ (UniProtKB | ChEBI); ligand shared between homodimeric partners
Binding site101Zn2+ (UniProtKB | ChEBI); ligand shared between homodimeric partners
Binding site104(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI)
Binding site186Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue
Binding site250L-arginine (UniProtKB | ChEBI)
Binding site359L-arginine (UniProtKB | ChEBI)
Binding site360L-arginine (UniProtKB | ChEBI)
Binding site364L-arginine (UniProtKB | ChEBI)
Binding site368(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI)
Binding site369L-arginine (UniProtKB | ChEBI)
Binding site449(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI)
Binding site450(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI)
Binding site463(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI)
Binding site478heme b (UniProtKB | ChEBI)
Binding site529FMN (UniProtKB | ChEBI)
Binding site530FMN (UniProtKB | ChEBI)
Binding site531FMN (UniProtKB | ChEBI)
Binding site533FMN (UniProtKB | ChEBI)
Binding site575FMN (UniProtKB | ChEBI)
Binding site576FMN (UniProtKB | ChEBI)
Binding site657FMN (UniProtKB | ChEBI)
Binding site664FMN (UniProtKB | ChEBI)
Binding site690FMN (UniProtKB | ChEBI)
Binding site694FMN (UniProtKB | ChEBI)
Binding site781NADP+ (UniProtKB | ChEBI)
Binding site803FAD (UniProtKB | ChEBI)
Binding site939FAD (UniProtKB | ChEBI)
Binding site941FAD (UniProtKB | ChEBI)
Binding site942FAD (UniProtKB | ChEBI)
Binding site957FAD (UniProtKB | ChEBI)
Binding site959FAD (UniProtKB | ChEBI)
Binding site1018NADP+ (UniProtKB | ChEBI)
Binding site1051NADP+ (UniProtKB | ChEBI)
Binding site1080NADP+ (UniProtKB | ChEBI)
Binding site1081NADP+ (UniProtKB | ChEBI)
Binding site1087NADP+ (UniProtKB | ChEBI)
Binding site1089NADP+ (UniProtKB | ChEBI)
Binding site1091NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcaveola
Cellular Componentcytoskeleton
Cellular ComponentGolgi apparatus
Molecular Functioncalmodulin binding
Molecular Functionflavin adenine dinucleotide binding
Molecular FunctionFMN binding
Molecular Functionheme binding
Molecular Functionmetal ion binding
Molecular FunctionNADP binding
Molecular Functionnitric-oxide synthase activity
Biological Processnitric oxide biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nitric oxide synthase 3
  • EC number
  • Alternative names
    • Constitutive NOS (cNOS)
    • EC-NOS
    • NOS type III (NOSIII)
    • Nitric oxide synthase, endothelial
      (Endothelial NOS
      ; eNOS
      )

Gene names

    • Name
      NOS3
    • Synonyms
      ENOS

Organism names

  • Taxonomic identifier
  • Strain
    • Texel
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Caprinae > Ovis

Accessions

  • Primary accession
    P79209
  • Secondary accessions
    • W5NV95

Proteomes

Subcellular Location

Membrane, caveola
Golgi apparatus
Cell membrane
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.

Keywords

PTM/Processing

Features

Showing features for initiator methionine, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed
ChainPRO_00001709472-1205Nitric oxide synthase 3
Modified residue116Phosphoserine
Modified residue498Phosphothreonine
Modified residue618Phosphoserine
Modified residue636Phosphoserine
Modified residue641Phosphoserine
Modified residue1177Phosphothreonine
Modified residue1179Phosphoserine
Modified residue1181Phosphoserine

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer. Interacts with NOSIP and NOSTRIN (By similarity).
Interacts with HSP90AB1 (By similarity).
Forms a complex with ASL, ASS1 and SLC7A1; the complex regulates cell-autonomous L-arginine synthesis and citrulline recycling while channeling extracellular L-arginine to nitric oxide synthesis pathway (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-20Disordered
Region26-73Disordered
Compositional bias35-66Pro residues
Region100-489Interaction with NOSIP
Region796-850Disordered
Compositional bias830-849Pro residues

Sequence similarities

Belongs to the NOS family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,205
  • Mass (Da)
    132,978
  • Last updated
    2023-11-08 v2
  • Checksum
    CE5FDDE325A3A07F
MGNLKSVGQEPGPPCGLGLGLGFGLCGKQGPASPAPEPSWAPAPATPQAPDHSPAPSSPTLTRPPEGPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPSQGPPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRLSAITVFPQRTPGRGDFRIWNTQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWSPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSMWKDKAAVEINLAVLHSFQPPKVTIVDHHAATVSFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYVLSPAFRYQPDPWKGSAAKGAGITRKKTFKEVANAVKISASLMGTLMAKRVKATILYASETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHEALVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHRSYKIRFNSVSCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLGQLGQGGELRGQGEGFRGWGEGASRNAASCETFCVGEEAKAAAQDIFSPKRSWKRQRYRLSTQAEGLQLLPGLIHVHRRKMFQATVLSVENLQSSKSTRATILVRLDTAGQEGLQYQPGDHISPHPPPRSSHRPGQGGPRVAPFSERPLMPRTPPPGGPPPSWVRDPRLPPCTLRQALTFFLDITSPPSPRLLRLLSTLAEEPSEQQELETLSQDPRRYEEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSAHPGEVHLTVAVLALDTSRLCSPLHPAEVVKSGGVWGDKGGLTEGVLARAPSFRLPPDPYVPCILVGPGTGIAPFRGFWQERLHDIESKGLQRAAPTLVFGCRCSQLDHLYRDEVQDAQERGVFGRVLTAFSREPDSPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATSVLQTVPRILATEGGMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERHLRGAVPWAFDPPGPDTPGP

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias35-66Pro residues
Sequence conflict396in Ref. 2; AAB40705
Sequence conflict415-416in Ref. 2; AAB40705
Compositional bias830-849Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AMGL01089902
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AMGL01089903
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AMGL01089904
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AMGL01089905
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
U76738
EMBL· GenBank· DDBJ
AAB40705.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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