NOS2_CARAU
ID NOS2_CARAU Reviewed; 164 AA.
AC Q92037;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Nitric oxide synthase, inducible;
DE EC=1.14.13.39 {ECO:0000250|UniProtKB:P35228};
DE AltName: Full=Inducible NO synthase;
DE Short=Inducible NOS;
DE Short=iNOS;
DE AltName: Full=NOS type II;
DE AltName: Full=Peptidyl-cysteine S-nitrosylase NOS2;
DE Flags: Fragment;
GN Name=nos2;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Macrophage;
RX PubMed=8872189; DOI=10.1038/icb.1996.65;
RA Laing K.J., Grawbowski P.S., Belosevic M., Secombes C.J.;
RT "A partial sequence for nitric oxide synthase from a goldfish (Carassius
RT auratus) macrophage cell line.";
RL Immunol. Cell Biol. 74:374-379(1996).
CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC diverse functions throughout the body. In macrophages, NO mediates
CC tumoricidal and bactericidal actions. Also has nitrosylase activity and
CC mediates cysteine S-nitrosylation of cytoplasmic target proteins such
CC COX2 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC Evidence={ECO:0000250|UniProtKB:P35228};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC Evidence={ECO:0000250|UniProtKB:P35228};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN. {ECO:0000250};
CC -!- COFACTOR:
CC Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250};
CC Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC enzyme. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Not stimulated by calcium/calmodulin.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P35228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P35228}.
CC -!- INDUCTION: By lipopolysaccharide (LPS).
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR EMBL; X97603; CAA66203.1; -; mRNA.
DR AlphaFoldDB; Q92037; -.
DR SMR; Q92037; -.
DR Proteomes; UP000515129; Genome assembly.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004517; F:nitric-oxide synthase activity; ISS:UniProtKB.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IEA:InterPro.
DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.360; -; 1.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR036119; NOS_N_sf.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56512; SSF56512; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding; Cytoplasm; FAD; Flavoprotein; FMN; Heme; Iron;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome.
FT CHAIN <1..>164
FT /note="Nitric oxide synthase, inducible"
FT /id="PRO_0000170940"
FT DOMAIN 66..>164
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT REGION 36..56
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT BINDING 3
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 18
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P29474"
FT BINDING 150..>164
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT NON_TER 1
FT NON_TER 164
SQ SEQUENCE 164 AA; 19045 MW; CD584B9D47A285F4 CRC64;
FGFHQQMLNY ILSPFFYYQP DPWLTHKWKD EKRNMRKHSI SFKGLIRAVL FSQTLIKSAL
AKRVRCTVLY ATETGKSKTL AKKLNTMMNY AFSSKVVCME DYNFSELEKE SLLFVVTSTF
GNGDCPGNGE SFKKQLLSLN NLRNQVRYSV FGLGSRMYPH FCAF
