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Protein

Amine oxidase [flavin-containing]

Gene

mao

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Oxidizes both 5-hydroxytryptamine (5-HT) and beta-phenylethylamine (PEA).By similarity2 Publications

Catalytic activityi

RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2.2 Publications

Cofactori

FADCurated

Enzyme regulationi

Inhibited by both clorgyline (selective MAOA inhibitor) and deprenyl (selective MAOB inhibitor).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei157 – 1571Important for catalytic activityBy similarity
Sitei366 – 3661Important for catalytic activityBy similarity
Sitei383 – 3831Important for catalytic activityBy similarity

GO - Molecular functioni

  • primary amine oxidase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Catecholamine metabolism, Neurotransmitter degradation

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.4.3.4. 928.
ReactomeiREACT_279415. Norepinephrine Neurotransmitter Release Cycle.
REACT_295205. Enzymatic degradation of dopamine by COMT.
REACT_295618. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
REACT_307985. Enzymatic degradation of Dopamine by monoamine oxidase.
REACT_325754. Metabolism of serotonin.

Names & Taxonomyi

Protein namesi
Recommended name:
Amine oxidase [flavin-containing] (EC:1.4.3.4)
Alternative name(s):
Monoamine oxidase
Short name:
MAO
Short name:
Z-MAO
Gene namesi
Name:maoImported
ORF Names:zgc:85761
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
ProteomesiUP000000437 Componenti: Chromosome 9

Organism-specific databases

ZFINiZDB-GENE-040329-3. mao.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 492492CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei493 – 51321Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini514 – 5229Mitochondrial intermembraneSequence Analysis

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Amine oxidase [flavin-containing]PRO_0000283788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei398 – 3981S-8alpha-FAD cysteineBy similarity

Proteomic databases

PRIDEiQ6NSN2.

Expressioni

Tissue specificityi

Strongest expression in brain and intestine, followed by liver, heart and gill. Little expression in spleen, eye or muscle. In brain, highest activity in noradrenergic and serotonergic cell groups and those of the habenulointerpeduncular pathway; moderate levels in dopaminergic cell clusters.1 Publication

Gene expression databases

BgeeiQ6NSN2.

Interactioni

Subunit structurei

Monomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6NSN2.
SMRiQ6NSN2. Positions 6-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Sequence Analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1231.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiQ6NSN2.
KOiK00274.
OMAiWTNAAKR.
OrthoDBiEOG7K6PTP.
PhylomeDBiQ6NSN2.
TreeFamiTF313314.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

Q6NSN2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTANAYDVIV IGGGISGLSA AKLLVDSGLN PVVLEARSRV GGRTYTVQNK
60 70 80 90 100
ETKWVDLGGA YIGPTQNRIL RIAKQYGVKT YKVNEEESLV HYVKGKSYPF
110 120 130 140 150
KGPFPPMWNP FAYMDYNNLW RTMDKMGMEI PKEAPWRAPH AEEWDKMTMQ
160 170 180 190 200
QLFDKICWTR SARRFATLFV NVNVTSEPHE VSALWFLWYV KQCGGTMRIF
210 220 230 240 250
STTNGGQERK FAGGANQISE GMARELGDRV KLSRAVCSID QTGDLVEVRT
260 270 280 290 300
VNEEVYKAKY VILAIPPGLN LKIHFNPELP PLRNQLIHRV PMGSVIKCMV
310 320 330 340 350
YYKENFWRKK GYCGSMVIEE EDAPIGLTLD DTKPDGSVPA IMGFILARKS
360 370 380 390 400
RKLANLTRDE RKRRICEIYA RVLGSEEALY PVHYEEKNWC EEEYSGGCYT
410 420 430 440 450
AYFPPGIMTQ FGRVLREPVG RLYFAGTETA TEWSGYMEGA VQAGERASRE
460 470 480 490 500
VMCAMGKLHA SQIWQSEPES MDVPARPFVT TFWERNLPSV GGFLKFMGVS
510 520
SFLAAATAAG LVACKKGLLP RC
Length:522
Mass (Da):58,765
Last modified:July 5, 2004 - v1
Checksum:i8FC58B2A13BFE15C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2242AR → QK in AAO16681 (PubMed:15621520).Curated
Sequence conflicti234 – 2341R → K in AAO16681 (PubMed:15621520).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY185211 mRNA. Translation: AAO16681.3.
BC070013 mRNA. Translation: AAH70013.1.
RefSeqiNP_997992.2. NM_212827.2.
UniGeneiDr.77508.

Genome annotation databases

EnsembliENSDART00000028225; ENSDARP00000032834; ENSDARG00000023712.
GeneIDi404730.
KEGGidre:404730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY185211 mRNA. Translation: AAO16681.3.
BC070013 mRNA. Translation: AAH70013.1.
RefSeqiNP_997992.2. NM_212827.2.
UniGeneiDr.77508.

3D structure databases

ProteinModelPortaliQ6NSN2.
SMRiQ6NSN2. Positions 6-504.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiQ6NSN2.
ChEMBLiCHEMBL1681610.

Proteomic databases

PRIDEiQ6NSN2.

Protocols and materials databases

DNASUi404730.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSDART00000028225; ENSDARP00000032834; ENSDARG00000023712.
GeneIDi404730.
KEGGidre:404730.

Organism-specific databases

CTDi404730.
ZFINiZDB-GENE-040329-3. mao.

Phylogenomic databases

eggNOGiCOG1231.
GeneTreeiENSGT00730000110903.
HOGENOMiHOG000221615.
HOVERGENiHBG004255.
InParanoidiQ6NSN2.
KOiK00274.
OMAiWTNAAKR.
OrthoDBiEOG7K6PTP.
PhylomeDBiQ6NSN2.
TreeFamiTF313314.

Enzyme and pathway databases

BRENDAi1.4.3.4. 928.
ReactomeiREACT_279415. Norepinephrine Neurotransmitter Release Cycle.
REACT_295205. Enzymatic degradation of dopamine by COMT.
REACT_295618. Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
REACT_307985. Enzymatic degradation of Dopamine by monoamine oxidase.
REACT_325754. Metabolism of serotonin.

Miscellaneous databases

NextBioi20817705.
PROiQ6NSN2.

Gene expression databases

BgeeiQ6NSN2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of monoamine oxidase in zebrafish (Danio rerio)."
    Setini A., Pierucci F., Senatori O., Nicotra A.
    Comp. Biochem. Physiol. 140B:153-161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, 3D-STRUCTURE MODELING.
    Tissue: LiverImported.
  2. "Distinct structure and activity of monoamine oxidase in the brain of zebrafish (Danio rerio)."
    Anichtchik O., Sallinen V., Peitsaro N., Panula P.
    J. Comp. Neurol. 498:593-610(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Brain1 Publication.
  3. NIH - Zebrafish Gene Collection (ZGC) project
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: KidneyImported.

Entry informationi

Entry nameiAOF_DANRE
AccessioniPrimary (citable) accession number: Q6NSN2
Secondary accession number(s): Q804D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There appears to be only one form of this enzyme in zebrafish, whereas in mammals two forms (MAOA and MAOB) exist.2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.