Reviewed, UniProtKB/Swiss-Prot Q92091 (NOS2_ONCMY)

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

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.
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. In macrophages, NO mediates tumoricidal and bactericidal actions.
Catalytic activity	L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+.
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: InterPro calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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	1
	Non-terminal residue	470	1

Sequences

	Sequence		Length	Mass (Da)
	Q92091-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 40B6717EE500B64D	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

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
EMBLGenBankDDBJ	X97013 mRNA. Translation: CAA65736.1.
UniGene	Omy.30
3D structure databases
HSSP	HSSP built from PDB template 1NOS based on UniProtKB P29477.
SMR	Q92091. Positions 1-132.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q92091.
Enzyme and pathway databases
BRENDA	1.14.13.39. 3435.
Family and domain databases
InterPro	IPR003097. FAD-binding_1. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR004030. NO_synthase_oxygenase_reg. [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. PF02898. NO_synthase. 1 hit. [Graphical view]
PRINTS	PR00369. FLAVODOXIN.
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:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)