ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P36367


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FMO4_RABIT
Primary accession number P36367
Secondary accession numbers None
Integrated into Swiss-Prot on June 1, 1994
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 60)
Name and origin of the protein
Protein name Dimethylaniline monooxygenase [N-oxide-forming] 4
Synonyms EC 1.14.13.8
Hepatic flavin-containing monooxygenase 4
FMO 4
FMO 1E1
Dimethylaniline oxidase 4
Gene name
Name: FMO4
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New Zealand white;
TISSUE=Liver;
PubMed=8188717 [NCBI, ExPASy, EBI, Israel, Japan]
Burnett V.L., Lawton M.P., Philpot R.M.;
"Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3.";
J. Biol. Chem. 269:14314-14322(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L10392; AAA21177.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A54096; A54096.
RefSeq NP_001076253.1; -.
UniGene Ocu.1822
3D structure databases
ModBase P36367.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031227; Cellular component: intrinsic to endoplasmic reticulum membrane (inferred from electronic annotation from InterPro).
GO:0005792; Cellular component: microsome (inferred from electronic annotation from InterPro).
GO:0050660; Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004499; Molecular function: flavin-containing monooxygenase activity (inferred from electronic annotation from InterPro).
GO:0050661; Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012143; dManiline_mOase.
IPR000960; Flavin_mOase.
IPR002256; Flavin_mOase_4.
Graphical view of domain structure.
Pfam PF00743; FMO-like; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000332; FMO; 1.
PRINTS PR00370; FMOXYGENASE.
PR01124; FMOXYGENASE4.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
ProtoNet P36367.
Genome annotation databases
Ensembl ENSOCUG00000002795; Oryctolagus cuniculus. [Contig view]
GeneID 100009582; -.
Phylogenomic databases
HOVERGEN P36367; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; Microsome; Monooxygenase; NADP; Oxidoreductase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   555  554     Dimethylaniline monooxygenase [N-oxide-forming] 4. PRO_0000147662
TRANSMEM   518   532  15     Potential. 
NP_BIND   9    14  6     FAD (Potential). 
NP_BIND   191   196  6     NADP (Potential). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
Sequence information
Length: 555 AA [This is the length of the unprocessed precursor] Molecular weight: 62992 Da [This is the MW of the unprocessed precursor] CRC64: 5A7219CAD1DEB3A2 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAKKVAVIGA GVSGLTSIKC CLDEDLEPTC FERSNDIGGL WKYTETSKDG MTRIYWSLVT 

        70         80         90        100        110        120 
NVCKEMSCYS DFPFQEDYPN FMSHSKFWNY LQEFAEHFDL LKYIQFKTTV CSVTKRPDFS 

       130        140        150        160        170        180 
KTGQWDVVTE TEGKQHRAVF DAVMVCTGKF LNPRLPLESF PGILKFRGQI LHCQEYKIPE 

       190        200        210        220        230        240 
GFRGQRVLVI GLGNSGGDVA VELSRVAAQV LLSTRTGTWV ISRSSNGGYP FNMMITRRCL 

       250        260        270        280        290        300 
NVIEQVLPSC FLRWINERQM NKRFNHENYG LSITKGKNPK FIVNDELPTC ILCGTVTVKT 

       310        320        330        340        350        360 
SVKEFTETSA IFEDGTVEEN IDSVIFTTGY VFSFPFLEEP LRSLCMKKMF LYKHVFPSNL 

       370        380        390        400        410        420 
ERASMAIIGL ISLKGSILTG TELQARWATR VFKGLCKIPP PQQLMAEVTK KEELIKRGVI 

       430        440        450        460        470        480 
KDTSEEKLSY IPYMDDLAAC IGTKPNIPLL FLKDPRLAWE VFFGPCTPYQ YRLMGPGKWD 

       490        500        510        520        530        540 
GARNAILTQW DRTLKPLKTR TVSSDSSKSA SLSHYLKVWG APLLLASVLL ICKSSHFLKS 

       550 
VRDKLQNRIF PYLVL 

P36367 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!