Nitric oxide synthase, inducible - Oncorhynchus mykiss (Rainbow trout)

Preferred order of sections

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
Peptidyl-cysteine S-nitrosylase NOS2

Gene names

Name:

nos2

Organism

Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)

Taxonomic identifier

8022 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Protacanthopterygii › Salmoniformes › Salmonidae › Salmoninae › Oncorhynchus

Protein attributes

Sequence length	470 AA.
Sequence status	Fragment.
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. In macrophages, NO mediates tumoricidal and bactericidal actions. 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 By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the NOS family. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase
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 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 – ›470

›470

Nitric oxide synthase, inducible

PRO_0000170939

Regions

Domain

169 – 307

139

Flavodoxin-like

Nucleotide binding

253 – 284

32

FMN By similarity

Nucleotide binding

398 – 409

12

FAD By similarity

Region

139 – 159

21

Calmodulin-binding Potential

Experimental info

Non-terminal residue

1

Non-terminal residue

470

1

Sequences

Sequence

Length

Mass (Da)

Tools

Q92091 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 40B6717EE500B64D
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FASTA

470

53,329

        10         20         30         40         50         60 
GWYMGTEIGV RDFCDYQRYN ILEEVGRRMG LETHKLSSLW KDQALVTINV AVTYSFQKNK 

        70         80         90        100        110        120 
VIITDHHSAA ESFMKHLETE FPPARRLPAD WDWLVPPMSG SLTPIFHQEM VNYILSPFFY 

       130        140        150        160        170        180 
YQPDPWMTHV WRNGEMCLKK QQISFKAVAR AALFSSTLMS RVLANRVRCT VLYATETGKS 

       190        200        210        220        230        240 
QTLAQRLNSM LNCAFNSRLL CMEDYNFSDM EQESLLVVVM STFGNGGSPG NGESFKKQLF 

       250        260        270        280        290        300 
SLQYLRNKSR YCVFGLGSRM YPQFCAFAHA VDAKLEELGA ERVTPTGEGD ELNGQEEAFS 

       310        320        330        340        350        360 
AWALTALKDA YKEFKIQGQL SLQLPGAERF CEAWDPLRHR VAVESCPQDR ITALSAIHSK 

       370        380        390        400        410        420 
AVLPMKLKSK HNLQSPQSSR STILVELERE RSPEVMDFAP GDHVGVFPGN LPQLVAGILK 

       430        440        450        460        470 
FLPQTPPTNQ CLRLGYRSDT FRVMRKTGRL LDASQHSLCL RHSPTSWTLP

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References

[1]

"Detection of mRNA for a nitric oxide synthase in macrophages and gill of rainbow trout challenged with an attenuated bacterial pathogen."
Grabowski P.S., Laing K.J., Hardie L., Macguigan F., Ralston S., Secombes C.J.
(In) Moncada S., Stamler J., Gross S., Higgs E.A. (eds.); 4th International meeting on the biology of nitric oxide, Amelia Island, Florida, Sep. 1995, pp.10:48-48, Portland Press, Brookfield (1996)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X97013 mRNA. Translation: CAA65736.1.
UniGene	Omy.30.
3D structure databases
ProteinModelPortal	Q92091.
SMR	Q92091. Positions 1-132.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG104152.
Family and domain databases
Gene3D	1.20.990.10. 1 hit.
InterPro	IPR003097. FAD-binding_1. IPR001094. Flavdoxin. IPR008254. Flavodoxin/NO_synth. IPR023173. NADPH_Cyt_P450_Rdtase_dom3. IPR004030. NO_synthase_oxygenase_dom. IPR026009. NOS. 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. PF02898. NO_synthase. 1 hit. [Graphical view]
PRINTS	PR00369. FLAVODOXIN.
SUPFAM	SSF56512. NO_synthase_oxygenase_reg. 1 hit. SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITE	PS50902. FLAVODOXIN_LIKE. 1 hit. PS60001. NOS. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NOS2_ONCMY

Accession

Primary (citable) accession number: Q92091

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1996
Last modified:	March 6, 2013
This is version 89 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