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Protein

Nitric oxide synthase, inducible

Gene

NOS2

Organism
Capra hircus (Goat)
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).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

Regulated by calcium/calmodulin.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi35 – 351Iron (heme axial ligand)By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. nitric oxide biosynthetic process Source: InterPro
  2. peptidyl-cysteine S-nitrosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Calcium, 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
OrganismiCapra hircus (Goat)
Taxonomic identifieri9925 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeCapra

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›110›110Nitric oxide synthase, induciblePRO_0000170928Add
BLAST

Expressioni

Inductioni

By lipopolysaccharide (LPS).

Interactioni

Subunit structurei

Homodimer. Binds SLC9A3R1 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ28314.
SMRiQ28314. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NOS family.Curated

Family and domain databases

Gene3Di3.90.340.10. 1 hit.
InterProiIPR004030. NOS_N.
[Graphical view]
PfamiPF02898. NO_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF56512. SSF56512. 1 hit.
PROSITEiPS60001. NOS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q28314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VEAVTKEIET TGTYQLTGDE LIFATKQAWR NAPRCIGRIQ WSNLQVFDAR
60 70 80 90 100
SCSTAQEMFE HICRHVRYAT NNGNIRSAIT VFPQRSDGKH DFRVWNAQLI
110
RYAGYQMPDG
Length:110
Mass (Da):12,654
Last modified:October 31, 1996 - v1
Checksum:iD72188FB257EC518
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei110 – 1101

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29085 mRNA. Translation: AAB02338.1.
UniGeneiChi.38774.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29085 mRNA. Translation: AAB02338.1.
UniGeneiChi.38774.

3D structure databases

ProteinModelPortaliQ28314.
SMRiQ28314. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.90.340.10. 1 hit.
InterProiIPR004030. NOS_N.
[Graphical view]
PfamiPF02898. NO_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF56512. SSF56512. 1 hit.
PROSITEiPS60001. NOS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Differential regulation of inducible nitric oxide synthase production in bovine and caprine macrophages."
    Adler H., Adler B., Peveri P., Werner E.R., Wachter H., Peterhans E., Jungi T.W.
    J. Infect. Dis. 173:971-978(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peripheral blood monocyte.

Entry informationi

Entry nameiNOS2_CAPHI
AccessioniPrimary (citable) accession number: Q28314
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2000
Last sequence update: October 31, 1996
Last modified: November 25, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.