Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nitric oxide synthase, inducible

Gene

NOS2

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (By similarity).By similarity

Catalytic activityi

2 L-arginine + 3 NADPH + 4 O2 = 2 L-citrulline + 2 nitric oxide + 3 NADP+ + 4 H2O.

Cofactori

Protein has several cofactor binding sites:
  • hemeBy similarity
  • FADBy similarityNote: Binds 1 FAD.By similarity
  • FMNBy similarityNote: Binds 1 FMN.By similarity
  • 5,6,7,8-tetrahydrobiopterinBy similarityNote: Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.By similarity

Enzyme regulationi

Not stimulated by calcium/calmodulin.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi‹1 – 25›25FMNBy similarityAdd
BLAST
Nucleotide bindingi138 – 14912FADBy similarityAdd
BLAST
Nucleotide bindingi274 – 28411FADBy similarityAdd
BLAST
Nucleotide bindingi349 – 36719NADPBy similarityAdd
BLAST
Nucleotide bindingi447 – 46216NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. nitric-oxide synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. peptidyl-cysteine S-nitrosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calmodulin-binding, FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

Names & Taxonomyi

Protein namesi
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 namesi
Name:NOS2
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›496›496Nitric oxide synthase, induciblePRO_0000170936Add
BLAST

Interactioni

Subunit structurei

Homodimer. Binds SLC9A3R1 (By similarity). Interacts with GAPDH. Interacts with S100A8 and S100A9 to form the iNOS-S100A8/9 transnitrosylase complex (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO19114.
SMRiO19114. Positions 74-496.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 341241FAD-binding FR-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the NOS family.Curated
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiO19114.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

O19114-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYPHFCAFVM TSTRNCLTWA ASQLAPTGEG DELSGQEDAF RSWAVQTFRA
60 70 80 90 100
ACETFDVRSK HCIQIPKRYT SNATWEPEQY KLTQSPEPLD LNKALSSIHA
110 120 130 140 150
KNLFTMRLRS LQNLHSEKSS RTTLLVQLTF EGSRGPSYLP GEHLGIFPGN
160 170 180 190 200
QTGLVQGILE RVVDCSSPDQ TVCLEVHDES GSYWVKDKRL PPCSLRQALT
210 220 230 240 250
YFLDITTPPT QLQLHKLARF ATEETHRQRL EALCQPSEYN DWKFSNNPTF
260 270 280 290 300
LEVLEEFPSL RVPAAFLLSQ LPILKPRYYS ISSSQDHTPS EVHLTVAVVT
310 320 330 340 350
YRTRDGQGPL HHGVCSTWIN NLKPEDPVPC FVRSVSGFQL PEDPSQPCIL
360 370 380 390 400
IGPGTGIAPF RSFWQQRLHD SQHRGLKGGR MTLVFGCRHP EEDHLYQEEM
410 420 430 440 450
QEMVRKGVLF QVHTGYSRLP GKPKVYVQDI LQKELADEVF SVLHGEQGHL
460 470 480 490
YVCGDVRMAR DVATTLKKLV AAKLNLSEEQ VEDYFFQLKY HEDIFG
Length:496
Mass (Da):56,397
Last modified:January 1, 1998 - v1
Checksum:iA0A1D303C57F0EEC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei496 – 4961

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85094 mRNA. Translation: AAB65618.1.
UniGeneiOcu.2556.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85094 mRNA. Translation: AAB65618.1.
UniGeneiOcu.2556.

3D structure databases

ProteinModelPortaliO19114.
SMRiO19114. Positions 74-496.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiO19114.

Family and domain databases

Gene3Di1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
SUPFAMiSSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

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

Entry informationi

Entry nameiNOS2_RABIT
AccessioniPrimary (citable) accession number: O19114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.