FMO2_RAT
ID FMO2_RAT Reviewed; 535 AA.
AC Q6IRI9;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 2 {ECO:0000305};
DE EC=1.14.13.- {ECO:0000250|UniProtKB:Q99518};
DE AltName: Full=Dimethylaniline oxidase 2;
DE AltName: Full=Pulmonary flavin-containing monooxygenase 2;
DE Short=FMO 2;
GN Name=Fmo2 {ECO:0000312|RGD:628600};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Catalyzes the oxidative metabolism of numerous xenobiotics,
CC including mainly therapeutic drugs and insecticides that contain a soft
CC nucleophile, most commonly nitrogen and sulfur and participates to
CC their bioactivation. {ECO:0000250|UniProtKB:Q99518}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P17635}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P17635}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:P17635}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; BC070904; AAH70904.1; -; mRNA.
DR RefSeq; NP_653338.2; NM_144737.2.
DR AlphaFoldDB; Q6IRI9; -.
DR SMR; Q6IRI9; -.
DR STRING; 10116.ENSRNOP00000004762; -.
DR PaxDb; Q6IRI9; -.
DR GeneID; 246245; -.
DR KEGG; rno:246245; -.
DR UCSC; RGD:628600; rat.
DR CTD; 2327; -.
DR RGD; 628600; Fmo2.
DR eggNOG; KOG1399; Eukaryota.
DR InParanoid; Q6IRI9; -.
DR PhylomeDB; Q6IRI9; -.
DR Reactome; R-RNO-217271; FMO oxidises nucleophiles.
DR SABIO-RK; Q6IRI9; -.
DR PRO; PR:Q6IRI9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; ISO:RGD.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; ISO:RGD.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0006739; P:NADP metabolic process; ISO:RGD.
DR GO; GO:0070995; P:NADPH oxidation; ISS:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISO:RGD.
DR GO; GO:0006082; P:organic acid metabolic process; ISO:RGD.
DR GO; GO:0072592; P:oxygen metabolic process; ISO:RGD.
DR GO; GO:0009404; P:toxin metabolic process; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002254; Flavin_mOase_2.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01122; FMOXYGENASE2.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Isopeptide bond; Magnesium;
KW Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..535
FT /note="Dimethylaniline monooxygenase [N-oxide-forming] 2"
FT /id="PRO_0000147651"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 9..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 40..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 60..61
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 61..62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT BINDING 195..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT CROSSLNK 492
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q99518"
SQ SEQUENCE 535 AA; 60899 MW; 4BDABD847733F639 CRC64;
MVKKVAVIGA GVSGLISLKG CVDEGLEPTC FERTEDIGGL WRFKENVEDG RASIYHSVIT
NTSKEMSCFS DFPMPEDFPN FLHNSKLLEY FRIFAKKFDL LKYIQFQTTV ISVKKRPDFA
SSGQWDVYVQ SNGKEQRAVF DAVMVCSGHH IQPHLPLKSF PGIERFQGQY FHSRQYKHPV
GYEGKRILVV GIGNSAADIA SELSKRAAQV FVSTRHGSWV LSRISEDGYP WDMVFHTRFS
SMLRNVLPRT VVKWMMERQM NRWFNHENYG LVPQNKYLMK EPVLNDDLPS RLLYGAIKVK
TRVKELTETA VVFEDGTVEE DVDVIVFATG YTFSFPFLED SLVKVEDNKV SLYKAMFPPH
LEKPTLACIG LIQPLGSIFP TVELQARWAT RVFKGVCRLP SETTMMADIA ERNEKRIDLF
GKSQSQILQT NYIDYLDELA LEIGAKPDFI SLLFKDPKLA VKLYFGPCNS YQYRLVGPGQ
WEGARNAILT QKQRILKPLK TRTLQTSASA PVSFLIKVLG LLAIVLAFFF KLHGF
