[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1074/jbc.271.20.11911; PubMed=8662618 [NCBI, ExPASy, EBI, Israel, Japan] Lin A.W., Chang C.C., McCormick C.C.; "Molecular cloning and expression of an avian macrophage nitric-oxide synthase cDNA and the analysis of the genomic 5'-flanking region."; J. Biol. Chem. 271:11911-11919(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 171-472. TISSUE=Osteoclast; DOI=10.1002/(SICI)1097-4644(19960315)60:4<469::AID-JCB4>3.0.CO;2-Q; PubMed=8707887 [NCBI, ExPASy, EBI, Israel, Japan] Sunyer T., Rothe L., Jiang X., Osdoby P., Collin-Osdoby P.; "Proinflammatory agents, IL-8 and IL-10, upregulate inducible nitric oxide synthase expression and nitric oxide production in avian osteoclast-like cells."; J. Cell. Biochem. 60:469-483(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 646-986. TISSUE=Heart; DOI=10.1016/S0008-6363(98)00005-4; PubMed=9709401 [NCBI, ExPASy, EBI, Israel, Japan] Shimizu T., Kinugawa K., Sugishita Y., Sugishita K., Harada K., Matsui H., Kohmoto O., Serizawa T., Takahashi T.; "Molecular cloning and expression of inducible nitric oxide synthase in chick embryonic ventricular myocytes."; Cardiovasc. Res. 38:405-413(1998).

Comments

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. NO may serve as both a paracrine and autocrine signal for modulating osteoclast bone resorption.
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.
SUBUNIT: Homodimer (By similarity).
INDUCTION: By treatment with lipopolysaccharides (LPS) or cytokines, but not in osteoclasts where they are induced by calcium and PMA (phorbol 12-myristate 13-acetate).
SIMILARITY: Belongs to the NOS family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
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

U46504; AAC59886.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U34045; AAB17499.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D85422; BAA12817.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_990292.1; -.

UniGene

Gga.3327

3D structure databases

HSSP

P29477; 1NOS. [HSSP ENTRY / PDB]

SMR

Q90703; 80-499.

ModBase

Q90703.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR004030; NO_synthase_oxygenase_reg.
IPR012144; NOS.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF02898; NO_synthase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000333; NOS; 1.

PRINTS

PR00369; FLAVODOXIN.
PR00371; FPNCR.

PROSITE

PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PS60001; NOS; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q90703.

Genome annotation databases

Ensembl

ENSGALG00000005693; Gallus gallus. [Contig view]

GeneID

395807; -.

KEGG

gga:395807; -.

Phylogenomic databases

HOVERGEN

Q90703; -.

Other

ProtoNet

Q90703.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1136`	`1136`	`Nitric oxide synthase, inducible.`	`PRO_0000170938`
`DOMAIN`	`536 674`	`139`	`Flavodoxin-like.`
`DOMAIN`	`727 967`	`241`	`FAD-binding FR-type.`
`NP_BIND`	`620 651`	`32`	`FMN (By similarity).`
`NP_BIND`	`764 775`	`12`	`FAD (By similarity).`
`NP_BIND`	`900 910`	`11`	`FAD (By similarity).`
`NP_BIND`	`975 993`	`19`	`NADP (By similarity).`
`NP_BIND`	`1073 1088`	`16`	`NADP (By similarity).`
`REGION`	`506 526`	`21`	`Calmodulin-binding (Potential).`
`METAL`	`107 107`		`Zinc (By similarity).`
`METAL`	`112 112`		`Zinc (By similarity).`
`METAL`	`197 197`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`400 400`		`S -> T (in Ref. 2; AAB17499).`
`CONFLICT`	`873 873`		`R -> S (in Ref. 3; BAA12817).`

Sequence information

Length: 1136 AA [This is the length of the unprocessed precursor]

Molecular weight: 129649 Da [This is the MW of the unprocessed precursor]

CRC64: D5CB73AC7BA94B9D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLCPWQFAFK PHAVKNQSSE EKDINNNVEK DVKVHSFVKD DAKLHSLSKK QMKMSPIITS 

        70         80         90        100        110        120 
AEKHPQNGIK ASNQISRCPR HVKVRNMENG SSLLDTLHLT AKEVINCRTR ACQGALMTPK 

       130        140        150        160        170        180 
GLVRSTRDGP VPPAELLPQA VDFVKQYYSS FKELKIEEHL ARLETVTKEI ETTGTYHLTK 

       190        200        210        220        230        240 
DELIFAAKQA WRNAPRCIGR IQWSNLQVFD ARDCKTAKEM FEYICRHIQY ATNNGNIRSA 

       250        260        270        280        290        300 
ITIFPQRTDG KHDFRVWNSQ LIRYAGYQMP DGSVIGDPAS VEFTKLCIEL GWKPKYGRFD 

       310        320        330        340        350        360 
VVPLILQANG QDPEIFEYPP EIILEVPMEH PKYEWFKELD LKWYALPAVA NMLLEVGGLE 

       370        380        390        400        410        420 
FTACPFNGWY MGTEIGVRDF CDVQRYNILK EVGRRMGLES NKLASLWKDR AVVEINVAVL 

       430        440        450        460        470        480 
HSFQKQNVTI MDHHSAAESF MKYMQNEYRV RGGCPADWVW IVPPMSGSIT PVFHQEMLNY 

       490        500        510        520        530        540 
VLTPFFYYQV DAWKTHIWHD ETRRPKKREI KLSILAKAVL LASLLLQKTM AARPKVTVIY 

       550        560        570        580        590        600 
ATETGKSETL ANSLCSLFSC AFNTKILCMD EYNISDLEKE TLLLVVTSTF GNGDSPNNGK 

       610        620        630        640        650        660 
TLKNSLLTLK LLRKNIRYAV FGLGSTMYPE FCAFAHAIDQ KLSQLGALQL TPVGEGDELN 

       670        680        690        700        710        720 
GQEEAFRTWA VTAFKTACDI FDIRGKNSIQ LPEIYTSDDS WNPKKHRIVY DSQTMDLTKA 

       730        740        750        760        770        780 
LSDIHGKNVI PMKLKFRQNL QSLKSSRVTI LVKLSCETNQ EVHYLPGEHI GISPGNQPEL 

       790        800        810        820        830        840 
VHGLIARVKD APPADQTIRL ETCTEGGYWA SEKKIPACTL SQALTYLLDI TTPPTQQLLK 

       850        860        870        880        890        900 
KLSQLVTAEG DKQRLEVLCH STEEYNKWKF YNRPNILEVL EEFPSAEVST AFLLTQLPLL 

       910        920        930        940        950        960 
KPRYYSVSSS CDMTPREIHL TVAVVNYRTR DGQGPLHHGV CSTWLNKIAL NETVPCFVRS 

       970        980        990       1000       1010       1020 
ADGFRLPKEP AKPCILIGPG TGIAPFRSFW QQRLYDLEKK GIKGGDMILL FGCRHPDMDH 

      1030       1040       1050       1060       1070       1080 
IYKEEVEEMK RKGVLKEVFT AYSRQPGQPK VYVQDILQNE LETKVCNILH KEEGHLYVCG 

      1090       1100       1110       1120       1130 
DVRMARDVAQ TLKRMLVKKL NHTEQQAEEY FFQLKSQKRY HEDIFGAVFP HEVKRI

Q90703 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