NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
DOI=10.1016/S0165-2427(97)00139-6; PubMed=9613441 [NCBI, ExPASy, EBI, Israel, Japan]
Pampusch M.S., Bennaars A.M., Harsch S., Murtaugh M.P.;
"Inducible nitric oxide synthase expression in porcine immune cells.";
Vet. Immunol. Immunopathol. 61:279-289(1998).

Comments

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body.
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. Binds SLC9A3R1 (By similarity).
TISSUE SPECIFICITY: Detected in both stimulated and unstimulated immune cells and macrophages with little or no up-regulation following cellular stimulation with lipopolysaccharides (LPS) or concanavalin A (ConA).
INDUCTION: Little by LPS or ConA in spleen cells.
SIMILARITY: Belongs to the NOS family.

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

U59390; AAB40614.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Ssc.16188

3D structure databases

HSSP

P35228; 4NOS. [HSSP ENTRY / PDB]

SMR

P79290; 1-215.

ModBase

P79290.

Ontologies

GO:0005516;	Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004517;	Molecular function: nitric-oxide synthase activity (inferred from electronic annotation from InterPro).
GO:0006809;	Biological process: nitric oxide biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR004030; NO_synthase_oxygenase_reg.
Graphical view of domain structure.

Pfam

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

PROSITE

PS60001; NOS; PARTIAL.

ProtoNet

P79290.

Phylogenomic databases

HOVERGEN

P79290; -.

Other

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

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >215`	`>215`	`Nitric oxide synthase, inducible.`	`PRO_0000170935`
`NON_TER`	`1 1`
`NON_TER`	`215 215`

Sequence information

Length: 215 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 24716 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: FECFF5BD85B65808 [This is a checksum on the sequence]

        10         20         30         40         50         60 
DARSCSTAQE MFEHICRHLR YATNNGNIRS AITVFPQRSD GKHDFRVWNA QLIRYAGYQM 

        70         80         90        100        110        120 
PDGTIIGDPA SVEFTQLCID LGWKPKYGRF DVVPLVLHAD GRDPELFEIP PDLVLEVPME 

       130        140        150        160        170        180 
HPKYEWFQEL ELKWYALPAV ANMLLEVGGL EFPGCPFNGW YMGTEIGVRD FCDVQRYNIL 

       190        200        210 
EEVGRRMGLE THKLASLWKD RAVVEINVAV LHSFQ

P79290 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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