Q26240 · NOS_RHOPR
- ProteinNitric oxide synthase, salivary gland
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1174 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. The production of NO in the salivary gland is used as a vasodilator for blood sucking.
Catalytic activity
- 2 L-arginine + 3 NADPH + 4 O2 + H+ = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O
2 CHEBI:32682 + 3 CHEBI:57783 + 4 CHEBI:15379 + CHEBI:15378 = 2 CHEBI:57743 + 2 CHEBI:16480 + 3 CHEBI:58349 + 4 CHEBI:15377
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD.
Note: Binds 1 FMN.
Activity regulation
Stimulated by calcium/calmodulin.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 83 | (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI) | |||
Binding site | 162 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); axial binding residue | |||
Binding site | 225 | L-arginine (UniProtKB | ChEBI) | |||
Binding site | 334 | L-arginine (UniProtKB | ChEBI) | |||
Binding site | 335 | L-arginine (UniProtKB | ChEBI) | |||
Binding site | 339 | L-arginine (UniProtKB | ChEBI) | |||
Binding site | 344 | L-arginine (UniProtKB | ChEBI) | |||
Binding site | 425 | (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI) | |||
Binding site | 438 | (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin (UniProtKB | ChEBI) | |||
Binding site | 453 | heme b (UniProtKB | ChEBI) | |||
Binding site | 639-670 | FMN (UniProtKB | ChEBI) | |||
Binding site | 780-791 | FAD (UniProtKB | ChEBI) | |||
Binding site | 923-933 | FAD (UniProtKB | ChEBI) | |||
Binding site | 998-1016 | NADP+ (UniProtKB | ChEBI) | |||
Binding site | 1095-1110 | NADP+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | calmodulin binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | NADP binding | |
Molecular Function | nitric-oxide synthase activity | |
Biological Process | nitric oxide biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNitric oxide synthase, salivary gland
- EC number
- Short namesNOS
Organism names
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Reduviidae > Triatominae > Rhodnius
Accessions
- Primary accessionQ26240
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000170952 | 1-1174 | Nitric oxide synthase, salivary gland | ||
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 475-495 | Calmodulin-binding | |||
Domain | 505-693 | Flavodoxin-like | |||
Domain | 745-990 | FAD-binding FR-type | |||
Sequence similarities
Belongs to the NOS family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,174
- Mass (Da)132,393
- Last updated1996-11-01 v1
- ChecksumC32F664EE51409CF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U59389 EMBL· GenBank· DDBJ | AAB03810.1 EMBL· GenBank· DDBJ | mRNA |