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MGP001867

UniProt Annotations

Entry Information
Gene Namemonoamine oxidase A
Protein EntryAOFA_HUMAN
UniProt IDP21397
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P21397-1; Sequence=Displayed; Name=2; IsoId=P21397-2; Sequence=VSP_045173;
Catalytic ActivityRCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + H(2)O(2).
CofactorName=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16129825, ECO:0000269|PubMed:18391214};
DiseaseBrunner syndrome (BRUNS) [MIM:300615]: A form of X-linked non-dysmorphic mild mental retardation. Male patients are affected by borderline mental retardation and exhibit abnormal behavior, including disturbed regulation of impulsive aggression. Obligate female carriers have normal intelligence and behavior. {ECO:0000269|PubMed:8211186}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionCatalyzes 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. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.
Mass SpectrometryMass=60512; Mass_error=6; Method=Electrospray; Range=1-527; Evidence={ECO:0000269|PubMed:11812236};
PolymorphismA polymorphism 1.2 kb upstream of the MAOA coding sequences consists of a 30-bp repeated sequence present in 3, 3.5, 4, or 5 copies. The polymorphism affect transcriptional activity of the MAOA gene promoter. Alleles with 3.5 or 4 copies of the repeat sequence are transcribed 2 to 10 times more efficiently than those with 3 or 5 copies of the repeat.
SimilarityBelongs to the flavin monoamine oxidase family. {ECO:0000305}.
Subcellular LocationMitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.
SubunitMonomer, homo- or heterodimer (containing two subunits of similar size). Each subunit contains a covalently bound flavin. Enzymatically active as monomer. {ECO:0000269|PubMed:16129825, ECO:0000269|PubMed:18391214}.
Tissue SpecificityHeart, liver, duodenum, blood vessels and kidney.
Web ResourceName=Wikipedia; Note=Monoamine oxidase entry; URL="http://en.wikipedia.org/wiki/Monoamine_oxidase";
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