AOFA_MOUSE
ID AOFA_MOUSE Reviewed; 526 AA.
AC Q64133; B1AX52; Q8K0Z8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Amine oxidase [flavin-containing] A {ECO:0000305};
DE EC=1.4.3.21 {ECO:0000269|PubMed:7792602};
DE EC=1.4.3.4 {ECO:0000250|UniProtKB:P21396};
DE AltName: Full=Monoamine oxidase type A;
DE Short=MAO-A;
GN Name=Maoa {ECO:0000312|MGI:MGI:96915};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-40, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=7792602; DOI=10.1126/science.7792602;
RA Cases O., Seif I., Grimsby J., Gaspar P., Chen K., Pournin S., Mueller U.,
RA Aguet M., Babinet C., Shih J.C., de Maeyer E.;
RT "Aggressive behavior and altered amounts of brain serotonin and
RT norepinephrine in mice lacking MAOA.";
RL Science 268:1763-1766(1995).
RN [5]
RP PROTEIN SEQUENCE OF 137-147; 207-217; 268-280 AND 380-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:7792602). Preferentially oxidizes serotonin
CC (PubMed:7792602). Also catalyzes the oxidative deamination of
CC kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously
CC condense to 4-hydroxyquinoline (By similarity).
CC {ECO:0000250|UniProtKB:P21396, ECO:0000269|PubMed:7792602}.
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:P21396};
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:7792602};
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:7792602};
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=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:0000250|UniProtKB:P21396};
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: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 -!- 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:0000250|UniProtKB:P21396};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P21397};
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 -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AL805907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466584; EDL35717.1; -; Genomic_DNA.
DR EMBL; BC029100; AAH29100.1; -; mRNA.
DR EMBL; S78615; AAB34677.1; -; Genomic_DNA.
DR EMBL; S78606; AAB34677.1; JOINED; Genomic_DNA.
DR CCDS; CCDS30033.1; -.
DR RefSeq; NP_776101.3; NM_173740.3.
DR AlphaFoldDB; Q64133; -.
DR SMR; Q64133; -.
DR BioGRID; 201307; 6.
DR IntAct; Q64133; 3.
DR MINT; Q64133; -.
DR STRING; 10090.ENSMUSP00000026013; -.
DR BindingDB; Q64133; -.
DR ChEMBL; CHEMBL3681; -.
DR iPTMnet; Q64133; -.
DR PhosphoSitePlus; Q64133; -.
DR EPD; Q64133; -.
DR jPOST; Q64133; -.
DR MaxQB; Q64133; -.
DR PaxDb; Q64133; -.
DR PRIDE; Q64133; -.
DR ProteomicsDB; 281779; -.
DR TopDownProteomics; Q64133; -.
DR Antibodypedia; 10933; 470 antibodies from 40 providers.
DR DNASU; 17161; -.
DR Ensembl; ENSMUST00000026013; ENSMUSP00000026013; ENSMUSG00000025037.
DR GeneID; 17161; -.
DR KEGG; mmu:17161; -.
DR UCSC; uc009ssa.2; mouse.
DR CTD; 4128; -.
DR MGI; MGI:96915; Maoa.
DR VEuPathDB; HostDB:ENSMUSG00000025037; -.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000160514; -.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; Q64133; -.
DR OMA; EWTRGAY; -.
DR OrthoDB; 1034142at2759; -.
DR PhylomeDB; Q64133; -.
DR TreeFam; TF313314; -.
DR BRENDA; 1.4.3.4; 3474.
DR Reactome; R-MMU-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-379397; Enzymatic degradation of dopamine by COMT.
DR Reactome; R-MMU-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR Reactome; R-MMU-380612; Metabolism of serotonin.
DR BioGRID-ORCS; 17161; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Maoa; mouse.
DR PRO; PR:Q64133; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q64133; protein.
DR Bgee; ENSMUSG00000025037; Expressed in small intestine Peyer's patch and 269 other tissues.
DR Genevisible; Q64133; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; ISO:MGI.
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:MGI.
DR GO; GO:0051378; F:serotonin binding; ISO:MGI.
DR GO; GO:0042420; P:dopamine catabolic process; IDA:MGI.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042443; P:phenylethylamine metabolic process; ISO:MGI.
DR GO; GO:0009967; P:positive regulation of signal transduction; IMP:MGI.
DR GO; GO:0042428; P:serotonin metabolic process; ISO:MGI.
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 Acetylation; Catecholamine metabolism; Direct protein sequencing; FAD;
KW Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Neurotransmitter degradation; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..526
FT /note="Amine oxidase [flavin-containing] A"
FT /id="PRO_0000099851"
FT TOPO_DOM 1..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 498..518
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000250"
FT TOPO_DOM 519..526
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT REGION 520..522
FT /note="Interaction with membrane phospholipid headgroups"
FT /evidence="ECO:0000250"
FT SITE 335
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250"
FT SITE 374
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P21397"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21396"
FT MOD_RES 406
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21397"
FT CONFLICT 83
FT /note="E -> D (in Ref. 3; AAH29100)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59602 MW; 5375D1B0C4C5ACF9 CRC64;
MTDLEKPSIT GHMFDVVVIG GGISGLAAAK LLSEYKINVL VLEARDRVGG RTYTVRNEHV
KWVDVGGAYV GPTQNRILRL SKELGIETYK VNVNERLVQY VKGKTYPFRG AFPPVWNPLA
YLDYNNLWRT MDDMGKEIPV DAPWQARHAE EWDKITMKDL IDKICWTKTA REFAYLFVNI
NVTSEPHEVS ALWFLWYVRQ CGGTSRIFSV TNGGQERKFV GGSGQISEQI MVLLGDKVKL
SSPVTYIDQT DDNIIIETLN HEHYECKYVI SAIPPVLTAK IHFKPELPPE RNQLIQRLPM
GAVIKCMVYY KEAFWKKKDY CGCMIIEDEE APISITLDDT KPDGSMPAIM GFILARKAER
LAKLHKDIRK RKICELYAKV LGSQEALSPV HYEEKNWCEE QYSGGCYTAY FPPGIMTLYG
RVIRQPVGRI YFAGTETATQ WSGYMEGAVE AGERAAREVL NALGKVAKKD IWVQEPESKD
VPALEITHTF LERNLPSVPG LLKITGFSTS VALLCFVLYK FKQPQS
