Reviewed, UniProtKB/Swiss-Prot Q90703 (NOS2_CHICK)

Names and origin

Protein names

Recommended name:
    Nitric oxide synthase, inducible
    EC=1.14.13.39
Alternative name(s):
    Inducible NO synthase
      Short name=Inducible NOS
      Short name=iNOS
    NOS type II
    Macrophage NOS

Gene names

Name:

NOS2

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	1136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (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 O(2) = citrulline + nitric oxide + n NADP(+).
Cofactor	Heme group By similarity. Binds 1 FAD By similarity. Binds 1 FMN By similarity. Metrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme By similarity.
Enzyme regulation	Not stimulated by calcium/calmodulin.
Subunit structure	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).
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP Zinc
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro FMN binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro calmodulin binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1136	1136	Nitric oxide synthase, inducible		PRO_0000170938
Regions
	Domain	536 – 674	139	Flavodoxin-like
	Domain	727 – 967	241	FAD-binding FR-type
	Nucleotide binding	620 – 651	32	FMN By similarity
	Nucleotide binding	764 – 775	12	FAD By similarity
	Nucleotide binding	900 – 910	11	FAD By similarity
	Nucleotide binding	975 – 993	19	NADP By similarity
	Nucleotide binding	1073 – 1088	16	NADP By similarity
	Region	506 – 526	21	Calmodulin-binding Potential
Sites
	Metal binding	107	1	Zinc By similarity
	Metal binding	112	1	Zinc By similarity
	Metal binding	197	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	400	1	S → T in AAB17499. Ref.2
	Sequence conflict	873	1	R → S in BAA12817. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q90703-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: D5CB73AC7BA94B9D	FASTA	1,136	129,649
	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

References

[1]	"Molecular cloning and expression of an avian macrophage nitric-oxide synthase cDNA and the analysis of the genomic 5'-flanking region." Lin A.W., Chang C.C., McCormick C.C. J. Biol. Chem. 271:11911-11919(1996) [PubMed: 8662618] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Proinflammatory agents, IL-8 and IL-10, upregulate inducible nitric oxide synthase expression and nitric oxide production in avian osteoclast-like cells." Sunyer T., Rothe L., Jiang X., Osdoby P., Collin-Osdoby P. J. Cell. Biochem. 60:469-483(1996) [PubMed: 8707887] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 171-472. Tissue: Osteoclast.
[3]	"Molecular cloning and expression of inducible nitric oxide synthase in chick embryonic ventricular myocytes." Shimizu T., Kinugawa K., Sugishita Y., Sugishita K., Harada K., Matsui H., Kohmoto O., Serizawa T., Takahashi T. Cardiovasc. Res. 38:405-413(1998) [PubMed: 9709401] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 646-986. Tissue: Heart.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U46504 mRNA. Translation: AAC59886.1. U34045 mRNA. Translation: AAB17499.1. D85422 mRNA. Translation: BAA12817.1.
RefSeq	NP_990292.1.
UniGene	Gga.3327
3D structure databases
HSSP	HSSP built from PDB template 1NOS based on UniProtKB P29477.
SMR	Q90703. Positions 80-499.
ModBase	Search...
Genome annotation databases
Ensembl	ENSGALG00000005693. Gallus gallus. [Contig view]
GeneID	395807.
KEGG	gga:395807.
Phylogenomic databases
HOVERGEN	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]
Gene3D	G3DSA:3.90.340.10. NO_synthase_oxygenase_reg. 1 hit.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. PF02898. NO_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF000333. NOS. 1 hit.
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. PS60001. NOS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NOS2_CHICK

Accession

Primary (citable) accession number: Q90703
Secondary accession number(s): Q90677, Q90934

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)