FMO4_RAT
ID FMO4_RAT Reviewed; 560 AA.
AC Q8K4B7; Q66HR6;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 4;
DE EC=1.14.13.8;
DE AltName: Full=Dimethylaniline oxidase 4;
DE AltName: Full=Hepatic flavin-containing monooxygenase 4;
DE Short=FMO 4;
GN Name=Fmo4;
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 [MRNA].
RC STRAIN=Sprague-Dawley;
RA Lattard V., Longin-Sauvageon C., Benoit E.;
RT "Cloning, sequencing and tissue distribution of rat flavin-containing
RT monooxygenase 4. Two different FMO4 are produced by tissue specific
RT alternative splicing.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19307449; DOI=10.1124/jpet.109.152058;
RA Novick R.M., Mitzey A.M., Brownfield M.S., Elfarra A.A.;
RT "Differential localization of flavin-containing monooxygenase (FMO)
RT isoforms 1, 3, and 4 in rat liver and kidney and evidence for expression of
RT FMO4 in mouse, rat, and human liver and kidney microsomes.";
RL J. Pharmacol. Exp. Ther. 329:1148-1155(2009).
CC -!- FUNCTION: This protein is involved in the oxidative metabolism of a
CC variety of xenobiotics such as drugs and pesticides. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-
CC dimethylaniline N-oxide + NADP(+); Xref=Rhea:RHEA:24468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16269, ChEBI:CHEBI:17735, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.14.13.8;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:19307449};
CC Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000305|PubMed:19307449}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in liver and kidney (at protein level).
CC {ECO:0000269|PubMed:19307449}.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000305}.
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DR EMBL; AF458416; AAM46764.1; -; mRNA.
DR EMBL; BC081721; AAH81721.1; -; mRNA.
DR RefSeq; NP_653147.1; NM_144561.2.
DR RefSeq; XP_006250206.1; XM_006250144.3.
DR AlphaFoldDB; Q8K4B7; -.
DR SMR; Q8K4B7; -.
DR STRING; 10116.ENSRNOP00000004599; -.
DR iPTMnet; Q8K4B7; -.
DR PhosphoSitePlus; Q8K4B7; -.
DR PaxDb; Q8K4B7; -.
DR PRIDE; Q8K4B7; -.
DR Ensembl; ENSRNOT00000004599; ENSRNOP00000004599; ENSRNOG00000003400.
DR GeneID; 246247; -.
DR KEGG; rno:246247; -.
DR UCSC; RGD:628601; rat.
DR CTD; 2329; -.
DR RGD; 628601; Fmo4.
DR eggNOG; KOG1399; Eukaryota.
DR GeneTree; ENSGT00940000160256; -.
DR InParanoid; Q8K4B7; -.
DR OMA; SHYLKVW; -.
DR OrthoDB; 405736at2759; -.
DR PhylomeDB; Q8K4B7; -.
DR TreeFam; TF105285; -.
DR BRENDA; 1.14.13.8; 5301.
DR SABIO-RK; Q8K4B7; -.
DR PRO; PR:Q8K4B7; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003400; Expressed in kidney and 19 other tissues.
DR ExpressionAtlas; Q8K4B7; baseline and differential.
DR Genevisible; Q8K4B7; RN.
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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0097009; P:energy homeostasis; ISO:RGD.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISO:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR002256; Flavin_mOase_4.
DR Pfam; PF00743; FMO-like; 1.
DR PIRSF; PIRSF000332; FMO; 1.
DR PRINTS; PR00370; FMOXYGENASE.
DR PRINTS; PR01124; FMOXYGENASE4.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome;
KW Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..560
FT /note="Dimethylaniline monooxygenase [N-oxide-forming] 4"
FT /id="PRO_0000147663"
FT TRANSMEM 519..539
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 195..198
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9HFE4"
FT CONFLICT 244
FT /note="Q -> R (in Ref. 1; AAM46764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 560 AA; 63660 MW; 9A7A77C41A328EFB CRC64;
MAKKVAVIGA GVSGLSSIKC CLDENLEPTC FERSSDFGGL WKFAEASEDG MTRVYRSLVT
NVCKEMSCYS DFPFHEDYPN FMSHEKFWDY LREFAEHFGL LKYIRFKTTV RSVTKRPDFS
ETGQWEVVTE TEGKQDRAVF DAVMVCTGQF LSPRLPLESF PGIHKFKGQI LHSQEYRIPD
AFRGKRILVV GLGNTGGDVA VELSGIAAQV FLSTRTGAWV RSRSSVGGYP LNMMQTRWRN
FLAQVLPSRF VSWNQERQMN KIFNHENYGL SIAKGKKPKF IVNDELPTCI LCGKITMKTS
VKDFTESSIV FEDGTIEANI DVVIFTTGYE FSFPFFEEPL KSLCTKKVIL YKRVFPPNLE
RSTLAIIGLI SLTGSILVGT EFQARWATRV FKGLCNIPPS QKLMAEAIKK EELIKRGVIK
DTSQDKLDFI SYMDELTQCI GAKPNIPLLF LKDPRLAWEV FFGPCTPYQY RLMGPGRWDG
ARNAILTQWD RTVKPLKTRT VPKSQEPASL SRYLKTWGAP VLIVSLLLIY KSSLFLELVQ
SKLQGRFSPS RILWYIPQNS
