ID D3YC69_MOUSE Unreviewed; 109 AA.
AC D3YC69;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=nitric-oxide synthase (NADPH) {ECO:0000256|ARBA:ARBA00012989};
DE EC=1.14.13.39 {ECO:0000256|ARBA:ARBA00012989};
DE Flags: Fragment;
GN Name=Nos2 {ECO:0000313|EMBL:ADD25171.1, ECO:0000313|MGI:MGI:97361};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:ADD25171.1};
RN [1] {ECO:0000313|EMBL:ADD25171.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MF1 {ECO:0000313|EMBL:ADD25171.1};
RC TISSUE=Spleen {ECO:0000313|EMBL:ADD25171.1};
RX PubMed=12654089; DOI=10.1046/j.1365-3024.2002.00490.x;
RA Nahrevanian H., Dascombe M.J.;
RT "Expression of inducible nitric oxide synthase (iNOS) mRNA in target organs
RT of lethal and non-lethal strains of murine malaria.";
RL Parasite Immunol. 24:471-478(2002).
RN [2] {ECO:0000313|EMBL:ADD25171.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MF1 {ECO:0000313|EMBL:ADD25171.1};
RC TISSUE=Spleen {ECO:0000313|EMBL:ADD25171.1};
RA Nahrevanian H., Dascombe M.J.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00035595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898;
CC Evidence={ECO:0000256|ARBA:ARBA00035595};
CC -!- COFACTOR:
CC Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000256|ARBA:ARBA00001950};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000256|ARBA:ARBA00006267}.
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DR EMBL; GU451261; ADD25171.1; -; mRNA.
DR AGR; MGI:97361; -.
DR MGI; MGI:97361; Nos2.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR PANTHER; PTHR43410; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR PANTHER; PTHR43410:SF1; NITRIC OXIDE SYNTHASE OXYGENASE; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
PE 2: Evidence at transcript level;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 3..100
FT /note="Oxidoreductase FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF00175"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD25171.1"
FT NON_TER 109
FT /evidence="ECO:0000313|EMBL:ADD25171.1"
SQ SEQUENCE 109 AA; 12644 MW; 6CE5B9B0CBF14C75 CRC64;
CXWQQRLHDS QHKGLKGGRM SLVFGCRHPE EDHLYQEEMQ EMVRKRVLFQ VHTGYSRLPG
KPKVYVQDIL QKQXANEVLS VLHGEQGHLY ICGDVRMXXD XAXTXXXTX
//
