LipidDB ID

LipidDB-9606-00256

Entry Name

UniProt Accession

P35228; A1L3U5; B7ZLY2; O60757; O94994; Q16263; Q16692; Q4TTS5; Q9UD42;

Theoretical PI

8.2

Molecular Weight

131117.23

Genbank Protein ID

AAA36375.1; AAA59171.1; CAA51512.1; AAA56666.1; AAB49041.1; BAA05531.1; AAB60366.1; AAC19133.1; BAA37123.1; AAY43131.1; ABY87543.1; AAI30284.1; AAI44127.1; AAD14179.1;

Genbank Nucleotide ID

L24553; L09210; X73029; U05810; U31511; D26525; U20141; AF068236; AB022318; DQ060518; EU332854; BC130283; BC144126; S75615;

Protein Name

Nitric oxide synthase, inducible

Protein Synonyms/Alias

1.14.13.39; Hepatocyte NOS; HEP-NOS; Inducible NO synthase; Inducible NOS; iNOS; NOS type II; Peptidyl-cysteine S-nitrosylase NOS2;

Gene Name

NOS2

Gene Synonyms/Alias

NOS2A;

Created Date

01-FEB-1994

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Navarro-Lérida I, Corvi MM, Barrientos AA, Gavilanes F, Berthiaume LG,Rodríguez-Crespo I. Palmitoylation of inducible nitric-oxide synthase at Cys-3 isrequired for proper intracellular traffic and nitric oxide synthesis. J BiolChem. 2004 Dec 31;279(53):55682-9. Epub 2004 Oct 13.[PMID:15485846]
[2] Navarro-Lérida I, Alvarez-Barrientos A, Rodríguez-Crespo I. N-terminalpalmitoylation within the appropriate amino acid environment conveys on NOS2 the ability to progress along the intracellular sorting pathways. J Cell Sci. 2006Apr 15;119(Pt 8):1558-69. Epub 2006 Mar 28. Erratum in: J Cell Sci. 2006 May1;119(Pt 9):1974.[PMID:16569659]

Functional Description

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.

Sequence Annotation

Domain: 539 677 Flavodoxin-like.
Domain: 730 970 FAD-binding FR-type.
Nucleotide-binding: 623 654 FMN.
Nucleotide-binding: 767 778 FAD.
Nucleotide-binding: 903 913 FAD.
Nucleotide-binding: 978 996 NADP.
Nucleotide-binding: 1076 1091 NADP.
Region: 509 529 Calmodulin-binding.
Metal binding site: 110 110 Zinc.
Metal binding site: 115 115 Zinc.
Metal binding site: 200 200 Iron (heme axial ligand).
Modified residue: 234 234 Phosphoserine; by PKA.
Modified residue: 578 578 Phosphoserine; by PKA.
Modified residue: 892 892 Phosphoserine; by PKA.

Protein Length

1153 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0030863; C:cortical cytoskeleton; IEA:Ensembl
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; IMP:BHF-UCL
GO:0005622; C:intracellular; IDA:BHF-UCL
GO:0005634; C:nucleus; ISS:BHF-UCL
GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl
GO:0005777; C:peroxisome; IDA:UniProtKB
GO:0034618; F:arginine binding; ISS:BHF-UCL
GO:0050660; F:flavin adenine dinucleotide binding; ISS:BHF-UCL
GO:0010181; F:FMN binding; ISS:BHF-UCL
GO:0020037; F:heme binding; ISS:BHF-UCL
GO:0005506; F:iron ion binding; IEA:InterPro
GO:0050661; F:NADP binding; TAS:BHF-UCL
GO:0003958; F:NADPH-hemoprotein reductase activity; IBA:RefGenome
GO:0004517; F:nitric-oxide synthase activity; IDA:UniProtKB
GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL
GO:0005102; F:receptor binding; IPI:UniProtKB
GO:0034617; F:tetrahydrobiopterin binding; ISS:BHF-UCL
GO:0006527; P:arginine catabolic process; IDA:BHF-UCL
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl
GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl
GO:0007623; P:circadian rhythm; IEA:Ensembl
GO:0042742; P:defense response to bacterium; ISS:UniProtKB
GO:0050829; P:defense response to Gram-negative bacterium; NAS:BHF-UCL
GO:0006954; P:inflammatory response; IBA:RefGenome
GO:0002227; P:innate immune response in mucosa; NAS:BHF-UCL
GO:0051701; P:interaction with host; TAS:Reactome
GO:0045776; P:negative regulation of blood pressure; IBA:RefGenome
GO:0010629; P:negative regulation of gene expression; IGI:UniProtKB
GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl
GO:0006809; P:nitric oxide biosynthetic process; IDA:UniProtKB
GO:0007263; P:nitric oxide mediated signal transduction; IBA:RefGenome
GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISS:UniProtKB
GO:0090382; P:phagosome maturation; TAS:Reactome
GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:RefGenome
GO:0051712; P:positive regulation of killing of cells of other organism; IMP:BHF-UCL
GO:0001912; P:positive regulation of leukocyte mediated cytotoxicity; TAS:BHF-UCL
GO:0045909; P:positive regulation of vasodilation; IBA:RefGenome
GO:0042127; P:regulation of cell proliferation; IEA:Ensembl
GO:0043457; P:regulation of cellular respiration; TAS:BHF-UCL
GO:0050796; P:regulation of insulin secretion; IMP:BHF-UCL
GO:0009617; P:response to bacterium; NAS:UniProtKB
GO:0001666; P:response to hypoxia; IEA:Ensembl
GO:0006801; P:superoxide metabolic process; ISS:UniProtKB

Interpro

InterPro; IPR003097; FAD-binding_1
InterPro; IPR017927; Fd_Rdtase_FAD-bd
InterPro; IPR001094; Flavdoxin
InterPro; IPR008254; Flavodoxin/NO_synth
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase
InterPro; IPR029039; Flavoprotein-like
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3
InterPro; IPR012144; NOS_euk
InterPro; IPR004030; NOS_N
InterPro; IPR001433; OxRdtase_FAD/NAD-bd
InterPro; IPR017938; Riboflavin_synthase-like_b-brl

Pfam

Pfam; PF00667; FAD_binding_1;
Pfam; PF00258; Flavodoxin_1;
Pfam; PF00175; NAD_binding_1;
Pfam; PF02898; NO_synthase;

SMART

PROSITE

PROSITE; PS51384; FAD_FR;
PROSITE; PS50902; FLAVODOXIN_LIKE;
PROSITE; PS60001; NOS;

PRINTS

PRINTS; PR00369; FLAVODOXIN;
PRINTS; PR00371; FPNCR;