NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
PubMed=8872189 [NCBI, ExPASy, EBI, Israel, Japan]
Laing K.J., Grawbowski P.S., Belosevic M., Secombes C.J.;
"A partial sequence for nitric oxide synthase from a goldfish (Carassius auratus) macrophage cell line.";
Immunol. Cell Biol. 74:374-379(1996).

Comments

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions.
CATALYTIC ACTIVITY: L-arginine + n NADPH + m O₂ = citrulline + nitric oxide + n NADP⁺.
COFACTOR: Heme group (By similarity).
COFACTOR: Binds 1 FAD (By similarity).
COFACTOR: Binds 1 FMN (By similarity).
COFACTOR: Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme (By similarity).
ENZYME REGULATION: Not stimulated by calcium/calmodulin (By similarity).
SUBUNIT: Homodimer (By similarity).
INDUCTION: By lipopolysaccharide (LPS).
SIMILARITY: Belongs to the NOS family.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X97603; CAA66203.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P29473; 1D0C. [HSSP ENTRY / PDB]

ModBase

Q92037.

Family and domain databases

InterPro

IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR004030; NO_synthase_oxygenase_reg.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.

Pfam

PF00258; Flavodoxin_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00369; FLAVODOXIN.

PROSITE

PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; PARTIAL.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q92037.

Phylogenomic databases

HOVERGEN

Q92037; -.

Other

ProtoNet

Q92037.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Calmodulin-binding; FAD; FMN; Heme; Iron; Metal-binding; NADP; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >164`	`>164`	`Nitric oxide synthase, inducible.`	`PRO_0000170940`
`DOMAIN`	`66 >164`	`>99`	`Flavodoxin-like.`
`NP_BIND`	`150 >164`	`>15`	`FMN (By similarity).`
`REGION`	`36 56`	`21`	`Calmodulin-binding (Potential).`
`NON_TER`	`1 1`
`NON_TER`	`164 164`

Sequence information

Length: 164 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 19045 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: CD584B9D47A285F4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
FGFHQQMLNY ILSPFFYYQP DPWLTHKWKD EKRNMRKHSI SFKGLIRAVL FSQTLIKSAL 

        70         80         90        100        110        120 
AKRVRCTVLY ATETGKSKTL AKKLNTMMNY AFSSKVVCME DYNFSELEKE SLLFVVTSTF 

       130        140        150        160 
GNGDCPGNGE SFKKQLLSLN NLRNQVRYSV FGLGSRMYPH FCAF

Q92037 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools