LOCUS NP_001002294 532 aa linear PRI 29-OCT-2008
DEFINITION flavin containing monooxygenase 3 isoform 2 [Homo sapiens].
ACCESSION NP_001002294
VERSION NP_001002294.1 GI:50541961
DBSOURCE REFSEQ: accession NM_001002294.1
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 532)
AUTHORS Alfieri,A., Malito,E., Orru,R., Fraaije,M.W. and Mattevi,A.
TITLE Revealing the moonlighting role of NADP in the structure of a
flavin-containing monooxygenase
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 105 (18), 6572-6577 (2008)
PUBMED 18443301
REMARK GeneRIF: Localization of mutations in human FMO3 that are known to
cause trimethylaminuria (fish-odor syndrome) in the elucidated FMO
structure provides a structural explanation for their biological
effects.
REFERENCE 2 (residues 1 to 532)
AUTHORS Fung,M.M., Nguyen,C., Mehtani,P., Salem,R.M., Perez,B., Thomas,B.,
Das,M., Schork,N.J., Mahata,S.K., Ziegler,M.G. and O'Connor,D.T.
TITLE Genetic variation within adrenergic pathways determines in vivo
effects of presynaptic stimulation in humans
JOURNAL Circulation 117 (4), 517-525 (2008)
PUBMED 18180394
REMARK GeneRIF: Observational study of gene-disease association. (HuGE
Navigator)
REFERENCE 3 (residues 1 to 532)
AUTHORS Shimizu,M., Murayama,N., Nagashima,S., Fujieda,M. and Yamazaki,H.
TITLE Complex mechanism underlying transcriptional control of the
haplotyped flavin-containing monooxygenase 3 (FMO3) gene in
Japanese: different regulation between mutations in 5'-upstream
distal region and common element in proximal region
JOURNAL Drug Metab. Pharmacokinet. 23 (1), 54-58 (2008)
PUBMED 18305374
REMARK GeneRIF: Site-directed mutagenesis studies suggest that the
putative hepatic nuclear factor-4 (HNF-4) binding site and CCAAT
box could be responsible cis-acting elements of the FMO3 gene in a
Japanese population.
REFERENCE 4 (residues 1 to 532)
AUTHORS Kousba,A., Soll,R., Yee,S. and Martin,M.
TITLE Cyclic conversion of the novel Src kinase inhibitor
[7-(2,6-dichloro-phenyl)-5-methyl-benzo[1,2,
4]triazin-3-yl]-[4-(2-pyrrolidin-1-yl-ethoxy)-phenyl]-amine
(TG100435) and Its N-oxide metabolite by flavin-containing
monoxygenases and cytochrome P450 reductase
JOURNAL Drug Metab. Dispos. 35 (12), 2242-2251 (2007)
PUBMED 17881660
REMARK GeneRIF: TG100435 and TG100855 were interconverted metabolically.
FMO3 seem to be the major N-oxidizing enzyme, whereas cytochrome
P450 reductase seems to be responsible for the retroreduction
reaction.
REFERENCE 5 (residues 1 to 532)
AUTHORS Allerston,C.K., Shimizu,M., Fujieda,M., Shephard,E.A., Yamazaki,H.
and Phillips,I.R.
TITLE Molecular evolution and balancing selection in the
flavin-containing monooxygenase 3 gene (FMO3)
JOURNAL Pharmacogenet. Genomics 17 (10), 827-839 (2007)
PUBMED 17885620
REMARK GeneRIF: The results provide evidence that FMO3 has been the
subject of balancing selection.
REFERENCE 6 (residues 1 to 532)
AUTHORS Lomri,N., Gu,Q. and Cashman,J.R.
TITLE Molecular cloning of the flavin-containing monooxygenase (form II)
cDNA from adult human liver
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 92 (21), 9910 (1995)
PUBMED 7568243
REMARK Correction to:[Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1685-9.
PMID: 1542660]
REFERENCE 7 (residues 1 to 532)
AUTHORS Lomri,N., Gu,Q. and Cashman,J.R.
TITLE Molecular cloning of the flavin-containing monooxygenase (form II)
cDNA from adult human liver
JOURNAL Proc. Natl. Acad. Sci. U.S.A. 89 (5), 1685-1689 (1992)
PUBMED 1542660
REMARK Erratum:[Proc Natl Acad Sci U S A. 1995 Oct 10;92(21):9910. PMID:
7568243]
REFERENCE 8 (residues 1 to 532)
AUTHORS Ziegler,D.M.
TITLE Flavin-containing monooxygenases: enzymes adapted for
multisubstrate specificity
JOURNAL Trends Pharmacol. Sci. 11 (8), 321-324 (1990)
PUBMED 2203193
REMARK Review article
REFERENCE 9 (residues 1 to 532)
AUTHORS Higgins,T., Chaykin,S., Hammond,K.B. and Humbert,J.R.
TITLE Trimethylamine N-oxide synthesis: a human variant
JOURNAL Biochem Med 6 (4), 392-396 (1972)
PUBMED 5048998
REFERENCE 10 (residues 1 to 532)
AUTHORS Humbert,J.A., Hammond,K.B. and Hathaway,W.E.
TITLE Trimethylaminuria: the fish-odour syndrome
JOURNAL Lancet 2 (7676), 770-771 (1970)
PUBMED 4195988
COMMENT VALIDATED REFSEQ: This record has undergone validation or
preliminary review. The reference sequence was derived from
Z47552.1, BC032016.1, M83772.1 and AI478384.1.
Summary: The mammalian flavin-containing monooxygenases (FMO; EC
1.14.13.8) represent a multigene family whose gene products are
localized in the endoplasmic reticulum of many tissues. These
enzymes catalyze the NADPH-dependent oxidative metabolism of many
drugs, pesticides, and other foreign compounds. Their substrates
are soft nucleophiles with an electron-rich center, typically a
nitrogen, sulfur or phosphorus-containing functional group, as the
site for oxidative attack by the enzyme (Ziegler, 1990 [PubMed
2203193]; Hines et al., 1994 [PubMed 8128486]).[supplied by OMIM].
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the
Entrez Gene record to access additional publications.
FEATURES Location/Qualifiers
source 1..532
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="1"
/map="1q23-q25"
Protein 1..532
/product="flavin containing monooxygenase 3 isoform 2"
/EC_number="1.14.13.8"
/note="Flavin-containing monooxygenase-3"
/calculated_mol_wt=59903
CDS 1..532
/gene="FMO3"
/gene_synonym="TMAU"
/gene_synonym="FMOII"
/gene_synonym="MGC34400"
/gene_synonym="dJ127D3.1"
/coded_by="NM_001002294.1:94..1692"
/note="isoform 2 is encoded by transcript variant 2"
/db_xref="CCDS:CCDS1292.1"
/db_xref="GeneID:2328"
/db_xref="HGNC:3771"
/db_xref="HPRD:00633"
/db_xref="MIM:136132"
ORIGIN
1 mgkkvaiiga gvsglasirs cleegleptc feksndiggl wkfsdhaeeg rasiyksvfs
61 nsskemmcfp dfpfpddfpn fmhnskiqey iiafakeknl lkyiqfktfv ssvnkhpdfa
121 ttgqwdvtte rdgkkesavf davmvcsghh vypnlpkesf pglnhfkgkc fhsrdykepg
181 vfngkrvlvv glgnsgcdia telsrtaeqv missrsgswv msrvwdngyp wdmllvtrfg
241 tflknnlpta isdwlyvkqm narfkhenyg lmplngvlrk epvfndelpa silcgivsvk
301 pnvkeftets aifedgtife gidcvifatg ysfaypflde siiksrnnei ilfkgvfppl
361 lekstiavig fvqslgaaip tvdlqsrwaa qvikgtctlp smedmmndin ekmekkrkwf
421 gksetiqtdy ivymdelssf igakpnipwl fltdpklame vyfgpcspyq frlvgpgqwp
481 garnailtqw drslkpmqtr vvgrlqkpcf ffhwlklfai pilliavflv lt
//