[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=New Zealand white; TISSUE=Heart; Broner C.W., Eledath F.M.; "Rabbit iducible nitric oxide synthase gene-NOS II."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body.
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 (By similarity).
SUBUNIT: Homodimer. Binds SLC9A3R1 (By similarity).
SIMILARITY: Belongs to the NOS family.
SIMILARITY: Contains 1 FAD-binding FR-type 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

U85094; AAB65618.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Ocu.2556

3D structure databases

HSSP

P29476; 1F20. [HSSP ENTRY / PDB]

ModBase

O19114.

Ontologies

GO:0004517;	Molecular function: nitric-oxide synthase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR003097; FAD-binding_1.
IPR001709; FPN_cyt_redctse.
IPR004030; NO_synthase_oxygenase_reg.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Pfam

PF00667; FAD_binding_1; 1.
PF00175; NAD_binding_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00371; FPNCR.

PROSITE

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

BLOCKS

O19114.

Phylogenomic databases

HOVERGEN

O19114; -.

Other

ProtoNet

O19114.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >496`	`>496`	`Nitric oxide synthase, inducible.`	`PRO_0000170936`
`DOMAIN`	`101 341`	`241`	`FAD-binding FR-type.`
`NP_BIND`	`<1 25`	`>25`	`FMN (By similarity).`
`NP_BIND`	`138 149`	`12`	`FAD (By similarity).`
`NP_BIND`	`274 284`	`11`	`FAD (By similarity).`
`NP_BIND`	`349 367`	`19`	`NADP (By similarity).`
`NP_BIND`	`447 462`	`16`	`NADP (By similarity).`
`NON_TER`	`1 1`
`NON_TER`	`496 496`

Sequence information

Length: 496 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 56397 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: A0A1D303C57F0EEC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYPHFCAFVM TSTRNCLTWA ASQLAPTGEG DELSGQEDAF RSWAVQTFRA ACETFDVRSK 

        70         80         90        100        110        120 
HCIQIPKRYT SNATWEPEQY KLTQSPEPLD LNKALSSIHA KNLFTMRLRS LQNLHSEKSS 

       130        140        150        160        170        180 
RTTLLVQLTF EGSRGPSYLP GEHLGIFPGN QTGLVQGILE RVVDCSSPDQ TVCLEVHDES 

       190        200        210        220        230        240 
GSYWVKDKRL PPCSLRQALT YFLDITTPPT QLQLHKLARF ATEETHRQRL EALCQPSEYN 

       250        260        270        280        290        300 
DWKFSNNPTF LEVLEEFPSL RVPAAFLLSQ LPILKPRYYS ISSSQDHTPS EVHLTVAVVT 

       310        320        330        340        350        360 
YRTRDGQGPL HHGVCSTWIN NLKPEDPVPC FVRSVSGFQL PEDPSQPCIL IGPGTGIAPF 

       370        380        390        400        410        420 
RSFWQQRLHD SQHRGLKGGR MTLVFGCRHP EEDHLYQEEM QEMVRKGVLF QVHTGYSRLP 

       430        440        450        460        470        480 
GKPKVYVQDI LQKELADEVF SVLHGEQGHL YVCGDVRMAR DVATTLKKLV AAKLNLSEEQ 

       490 
VEDYFFQLKY HEDIFG

O19114 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