AOF_DANRE
ID AOF_DANRE Reviewed; 522 AA.
AC Q6NSN2; Q804D6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Amine oxidase [flavin-containing] {ECO:0000250|UniProtKB:P21397};
DE EC=1.4.3.21 {ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825};
DE EC=1.4.3.4 {ECO:0000250|UniProtKB:P21397};
DE AltName: Full=Monoamine oxidase;
DE Short=MAO;
DE Short=Z-MAO;
GN Name=mao {ECO:0000312|EMBL:AAH70013.1, ECO:0000312|ZFIN:ZDB-GENE-040329-3};
GN ORFNames=zgc:85761;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAO16681.3}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Liver {ECO:0000312|EMBL:AAO16681.3};
RX PubMed=15621520; DOI=10.1016/j.cbpc.2004.10.002;
RA Setini A., Pierucci F., Senatori O., Nicotra A.;
RT "Molecular characterization of monoamine oxidase in zebrafish (Danio
RT rerio).";
RL Comp. Biochem. Physiol. 140B:153-161(2005).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain {ECO:0000269|PubMed:16917825};
RX PubMed=16917825; DOI=10.1002/cne.21057;
RA Anichtchik O., Sallinen V., Peitsaro N., Panula P.;
RT "Distinct structure and activity of monoamine oxidase in the brain of
RT zebrafish (Danio rerio).";
RL J. Comp. Neurol. 498:593-610(2006).
RN [3] {ECO:0000312|EMBL:AAH70013.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH70013.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidative deamination of biogenic and
CC xenobiotic amines and has important functions in the metabolism of
CC neuroactive and vasoactive amines in the central nervous system and
CC peripheral tissues (PubMed:15621520, PubMed:16917825). Preferentially
CC oxidizes serotonin and tyramine (PubMed:15621520, PubMed:16917825).
CC Also catalyzes the oxidative deamination of kynuramine to 3-(2-
CC aminophenyl)-3-oxopropanal that can spontaneously condense to 4-
CC hydroxyquinoline (By similarity). {ECO:0000250|UniProtKB:P21396,
CC ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000250|UniProtKB:P21397};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + serotonin = (5-hydroxyindol-3-yl)acetaldehyde +
CC H2O2 + NH4(+); Xref=Rhea:RHEA:69072, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:50157, ChEBI:CHEBI:350546;
CC Evidence={ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:225237; Evidence={ECO:0000269|PubMed:15621520,
CC ECO:0000269|PubMed:16917825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:30591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15621, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:16917825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dopamine + H2O + O2 = 3,4-dihydroxyphenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:27946, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:16917825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-adrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde +
CC H2O2 + methylamine; Xref=Rhea:RHEA:51168, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:59338,
CC ChEBI:CHEBI:71406, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000250|UniProtKB:P21396};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-noradrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde
CC + H2O2 + NH4(+); Xref=Rhea:RHEA:69076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:72587, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000250|UniProtKB:P21396};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + kynuramine + O2 = 3-(2-aminophenyl)-3-oxopropanal + H2O2
CC + NH4(+); Xref=Rhea:RHEA:59596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:180898,
CC ChEBI:CHEBI:180899; Evidence={ECO:0000250|UniProtKB:P21396};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597;
CC Evidence={ECO:0000250|UniProtKB:P21396};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + tryptamine = H2O2 + indole-3-acetaldehyde + NH4(+);
CC Xref=Rhea:RHEA:59416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:18086, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:57887; Evidence={ECO:0000250|UniProtKB:P21396};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P27338};
CC -!- ACTIVITY REGULATION: Inhibited by both clorgyline (selective MAOA
CC inhibitor) and deprenyl (selective MAOB inhibitor).
CC {ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825}.
CC -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
CC similar size). Each subunit contains a covalently bound flavin.
CC Enzymatically active as monomer (By similarity).
CC {ECO:0000250|UniProtKB:P21397}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P21396}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:P21396}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P21396}.
CC -!- TISSUE SPECIFICITY: Strongest expression in brain and intestine,
CC followed by liver, heart and gill. Little expression in spleen, eye or
CC muscle. In brain, highest activity in noradrenergic and serotonergic
CC cell groups and those of the habenulointerpeduncular pathway; moderate
CC levels in dopaminergic cell clusters. {ECO:0000269|PubMed:16917825}.
CC -!- MISCELLANEOUS: There appears to be only one form of this enzyme in
CC zebrafish, whereas in mammals two forms (MAOA and MAOB) exist.
CC {ECO:0000269|PubMed:15621520, ECO:0000269|PubMed:16917825}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY185211; AAO16681.3; -; mRNA.
DR EMBL; BC070013; AAH70013.1; -; mRNA.
DR RefSeq; NP_997992.2; NM_212827.3.
DR AlphaFoldDB; Q6NSN2; -.
DR SMR; Q6NSN2; -.
DR STRING; 7955.ENSDARP00000032834; -.
DR BindingDB; Q6NSN2; -.
DR ChEMBL; CHEMBL1681610; -.
DR DrugCentral; Q6NSN2; -.
DR PaxDb; Q6NSN2; -.
DR DNASU; 404730; -.
DR Ensembl; ENSDART00000028225; ENSDARP00000032834; ENSDARG00000023712.
DR GeneID; 404730; -.
DR KEGG; dre:404730; -.
DR CTD; 404730; -.
DR ZFIN; ZDB-GENE-040329-3; mao.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000166446; -.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; Q6NSN2; -.
DR OMA; IGPGQDR; -.
DR OrthoDB; 1151887at2759; -.
DR PhylomeDB; Q6NSN2; -.
DR TreeFam; TF313314; -.
DR BRENDA; 1.4.3.4; 928.
DR Reactome; R-DRE-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR PRO; PR:Q6NSN2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 9.
DR Bgee; ENSDARG00000023712; Expressed in intestine and 52 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0097621; F:monoamine oxidase activity; ISS:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:RHEA.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042402; P:cellular biogenic amine catabolic process; IDA:UniProtKB.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Catecholamine metabolism; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Neurotransmitter degradation; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Amine oxidase [flavin-containing]"
FT /id="PRO_0000283788"
FT TOPO_DOM 1..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..522
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT SITE 157
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P27338"
FT SITE 366
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P27338"
FT SITE 383
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P27338"
FT MOD_RES 398
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000250|UniProtKB:P27338"
FT CONFLICT 223..224
FT /note="AR -> QK (in Ref. 1; AAO16681)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="R -> K (in Ref. 1; AAO16681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 58765 MW; 8FC58B2A13BFE15C CRC64;
MTANAYDVIV IGGGISGLSA AKLLVDSGLN PVVLEARSRV GGRTYTVQNK ETKWVDLGGA
YIGPTQNRIL RIAKQYGVKT YKVNEEESLV HYVKGKSYPF KGPFPPMWNP FAYMDYNNLW
RTMDKMGMEI PKEAPWRAPH AEEWDKMTMQ QLFDKICWTR SARRFATLFV NVNVTSEPHE
VSALWFLWYV KQCGGTMRIF STTNGGQERK FAGGANQISE GMARELGDRV KLSRAVCSID
QTGDLVEVRT VNEEVYKAKY VILAIPPGLN LKIHFNPELP PLRNQLIHRV PMGSVIKCMV
YYKENFWRKK GYCGSMVIEE EDAPIGLTLD DTKPDGSVPA IMGFILARKS RKLANLTRDE
RKRRICEIYA RVLGSEEALY PVHYEEKNWC EEEYSGGCYT AYFPPGIMTQ FGRVLREPVG
RLYFAGTETA TEWSGYMEGA VQAGERASRE VMCAMGKLHA SQIWQSEPES MDVPARPFVT
TFWERNLPSV GGFLKFMGVS SFLAAATAAG LVACKKGLLP RC
