P31512 (FMO4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dimethylaniline monooxygenase [N-oxide-forming] 4
EC=1.14.13.8

Alternative name(s):
Dimethylaniline oxidase 4
Hepatic flavin-containing monooxygenase 4
Short name=FMO 4

Gene names

Name:	FMO4
Synonyms:	FMO2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides.
Catalytic activity	N,N-dimethylaniline + NADPH + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O.
Cofactor	FAD.
Subcellular location	Microsome membrane. Endoplasmic reticulum membrane.
Tissue specificity	Liver.
Sequence similarities	Belongs to the FMO family.
Caution	Was originally (Ref.1) termed FMO2.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	FAD Flavoprotein NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	xenobiotic metabolic process Non-traceable author statement. Source: UniProtKB
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular membrane-bounded organelle Non-traceable author statement. Source: UniProtKB intrinsic to endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	N,N-dimethylaniline monooxygenase activity Non-traceable author statement Ref.1. Source: UniProtKB NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 558	558	Dimethylaniline monooxygenase [N-oxide-forming] 4		PRO_0000147660
Regions
	Transmembrane	517 – 531	15	Helical; Potential
	Nucleotide binding	9 – 14	6	FAD Potential
	Nucleotide binding	191 – 196	6	NADP Potential
Natural variations
	Natural variant	37	1	I → T. Ref.7		VAR_015367
	Natural variant	308	1	T → S. Corresponds to variant rs3737925 [ dbSNP | Ensembl ].		VAR_049090
	Natural variant	323	1	V → A. Ref.2 Ref.7 Corresponds to variant rs1042767 [ dbSNP | Ensembl ].		VAR_015368
	Natural variant	339	1	E → Q. Ref.7		VAR_015369
	Natural variant	372	1	G → S. Ref.2		VAR_022305
	Natural variant	536	1	F → L. Ref.2		VAR_022306
	Natural variant	544	1	L → R. Ref.2		VAR_022307

Sequences

	Sequence		Length	Mass (Da)
	P31512 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6981AE9180C07802	FASTA	558	63,343
	10 20 30 40 50 60 MAKKVAVIGA GVSGLSSIKC CVDEDLEPTC FERSDDIGGL WKFTESSKDG MTRVYKSLVT 70 80 90 100 110 120 NVCKEMSCYS DFPFHEDYPN FMNHEKFWDY LQEFAEHFDL LKYIQFKTTV CSITKRPDFS 130 140 150 160 170 180 ETGQWDVVTE TEGKQNRAVF DAVMVCTGHF LNPHLPLEAF PGIHKFKGQI LHSQEYKIPE 190 200 210 220 230 240 GFQGKRVLVI GLGNTGGDIA VELSRTAAQV LLSTRTGTWV LGRSSDWGYP YNMMVTRRCC 250 260 270 280 290 300 SFIAQVLPSR FLNWIQERKL NKRFNHEDYG LSITKGKKAK FIVNDELPNC ILCGAITMKT 310 320 330 340 350 360 SVIEFTETSA VFEDGTVEEN IDVVIFTTGY TFSFPFFEEP LKSLCTKKIF LYKQVFPLNL 370 380 390 400 410 420 ERATLAIIGL IGLKGSILSG TELQARWVTR VFKGLCKIPP SQKLMMEATE KEQLIKRGVF 430 440 450 460 470 480 KDTSKDKFDY IAYMDDIAAC IGTKPSIPLL FLKDPRLAWE VFFGPCTPYQ YRLMGPGKWD 490 500 510 520 530 540 GARNAILTQW DRTLKPLKTR IVPDSSKPAS MSHYLKAWGA PVLLASLLLI CKSSLFLKLV 550 RDKLQDRMSP YLVSLWRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family." Dolphin C.T., Shephard E.A., Povey S., Smith R.L., Phillips I.R. Biochem. J. 287:261-267(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-323; SER-372; LEU-536 AND ARG-544.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[7]	"Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans." Furnes B., Feng J., Sommer S.S., Schlenk D. Drug Metab. Dispos. 31:187-193(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS THR-37; ALA-323 AND GLN-339.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z11737 mRNA. Translation: CAA77797.1. AY882422 Genomic DNA. Translation: AAW56938.1. BT007444 mRNA. Translation: AAP36112.1. AL031274 Genomic DNA. Translation: CAB42008.1. CH471067 Genomic DNA. Translation: EAW90896.1. BC002780 mRNA. Translation: AAH02780.1.
IPI	IPI00219008.
PIR	S29125.
RefSeq	NP_002013.1. NM_002022.1.
UniGene	Hs.386502.
3D structure databases
ProteinModelPortal	P31512.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000356723.
PTM databases
PhosphoSite	P31512.
Polymorphism databases
DMDM	399506.
Proteomic databases
PaxDb	P31512.
PRIDE	P31512.
Protocols and materials databases
DNASU	2329.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367749; ENSP00000356723; ENSG00000076258.
GeneID	2329.
KEGG	hsa:2329.
UCSC	uc001gho.3. human.
Organism-specific databases
CTD	2329.
GeneCards	GC01P171283.
HGNC	HGNC:3772. FMO4.
HPA	HPA049100.
MIM	136131. gene.
neXtProt	NX_P31512.
PharmGKB	PA28188.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2072.
HOGENOM	HOG000076537.
HOVERGEN	HBG002037.
InParanoid	P31512.
KO	K00485.
OMA	CKIPPSQ.
OrthoDB	EOG4KPT9G.
PhylomeDB	P31512.
Gene expression databases
Bgee	P31512.
CleanEx	HS_FMO2. HS_FMO4.
Genevestigator	P31512.
GermOnline	ENSG00000076258. Homo sapiens.
Family and domain databases
InterPro	IPR012143. DiMe-aniline_mOase. IPR000960. Flavin_mOase. IPR020946. Flavin_mOase-like. IPR002256. Flavin_mOase_4. [Graphical view]
Pfam	PF00743. FMO-like. 1 hit. [Graphical view]
PIRSF	PIRSF000332. FMO. 1 hit.
PRINTS	PR00370. FMOXYGENASE. PR01124. FMOXYGENASE4.
ProtoNet	Search...
Other
GenomeRNAi	2329.
NextBio	9453.
SOURCE	Search...

Entry information

Entry name

FMO4_HUMAN

Accession

Primary (citable) accession number: P31512
Secondary accession number(s): Q53XR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 125 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.