Nitric oxide synthase, inducible - Gallus gallus (Chicken)

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Q90703 (NOS2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Macrophage NOS
NOS type II
Peptidyl-cysteine S-nitrosylase NOS2

Gene names

Name:

NOS2

Organism

Gallus gallus (Chicken) [Reference proteome]

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.
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. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2 By similarity.
Catalytic activity	2 L-arginine + 3 NADPH + 4 O₂ = 2 L-citrulline + 2 nitric oxide + 3 NADP⁺ + 4 H₂O.
Cofactor	Heme group By similarity. Binds 1 FAD By similarity. Binds 1 FMN By similarity. Tetrahydrobiopterin (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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro peptidyl-cysteine S-nitrosylation Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding 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: EC
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

FMN By similarity

Nucleotide binding

764 – 775

FAD By similarity

Nucleotide binding

900 – 910

FAD By similarity

Nucleotide binding

975 – 993

NADP By similarity

Nucleotide binding

1073 – 1088

NADP By similarity

Region

506 – 526

Calmodulin-binding Potential

Sites

Metal binding

107

Zinc By similarity

Metal binding

112

Zinc By similarity

Metal binding

197

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

400

S → T in AAB17499. Ref.2

Sequence conflict

873

R → S in BAA12817. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q90703 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: D5CB73AC7BA94B9D
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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

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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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 646-986. Tissue: Heart.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U46504 mRNA. Translation: AAC59886.1. U34045 mRNA. Translation: AAB17499.1. D85422 mRNA. Translation: BAA12817.1.
IPI	IPI00593125.
RefSeq	NP_990292.1. NM_204961.1.
UniGene	Gga.3327.
3D structure databases
ProteinModelPortal	Q90703.
SMR	Q90703. Positions 80-499, 700-1127.
ModBase	Search...
Proteomic databases
PaxDb	Q90703.
PRIDE	Q90703.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	395807.
KEGG	gga:395807.
Organism-specific databases
CTD	4843.
Phylogenomic databases
eggNOG	COG4362.
HOGENOM	HOG000220884.
HOVERGEN	HBG000159.
KO	K13241.
Family and domain databases
Gene3D	1.20.990.10. 1 hit. 3.90.340.10. 1 hit.
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR004030. NO_synthase_oxygenase_dom. IPR026009. NOS. IPR012144. NOS_met. IPR001433. OxRdtase_FAD/NAD-bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
PANTHER	PTHR19384:SF5. PTHR19384:SF5. 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.
SUPFAM	SSF56512. NO_synthase_oxygenase_reg. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. PS60001. NOS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20815875.

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:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents