ID   AOFA_MOUSE              Reviewed;         526 AA.
AC   Q64133; Q8K0Z8;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 2.
DT   16-JUN-2009, entry version 70.
DE   RecName: Full=Amine oxidase [flavin-containing] A;
DE            EC=1.4.3.4;
DE   AltName: Full=Monoamine oxidase type A;
DE            Short=MAO-A;
GN   Name=Maoa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-40.
RX   MEDLINE=95312871; PubMed=7792602; DOI=10.1126/science.7792602;
RA   Cases O., Seif I., Grimsby J., Gaspar P., Chen K., Pournin S.,
RA   Mueller U., 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   [3]
RP   PROTEIN SEQUENCE OF 137-147; 207-217; 268-280 AND 380-395, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
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
CC       and peripheral tissues. MAOA preferentially oxidizes biogenic
CC       amines such as 5-hydroxytryptamine (5-HT), norepinephrine and
CC       epinephrine (By similarity).
CC   -!- CATALYTIC ACTIVITY: RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) +
CC       H(2)O(2).
CC   -!- COFACTOR: FAD.
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   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       type IV membrane protein; Cytoplasmic side.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
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DR   EMBL; BC029100; AAH29100.1; -; mRNA.
DR   EMBL; S78615; AAB34677.1; -; Genomic_DNA.
DR   EMBL; S78606; AAB34677.1; JOINED; Genomic_DNA.
DR   IPI; IPI00169711; -.
DR   UniGene; Mm.21108; -.
DR   SMR; Q64133; 23-509.
DR   PRIDE; Q64133; -.
DR   Ensembl; ENSMUSG00000025037; Mus musculus.
DR   MGI; MGI:96915; Maoa.
DR   HOGENOM; Q64133; -.
DR   HOVERGEN; Q64133; -.
DR   BRENDA; 1.4.3.4; 244.
DR   ArrayExpress; Q64133; -.
DR   Bgee; Q64133; -.
DR   CleanEx; MM_MAOA; -.
DR   GermOnline; ENSMUSG00000025037; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008131; F:amine oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0042420; P:dopamine catabolic process; IDA:MGI.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001613; Amineoxid_fl.
DR   InterPro; IPR002937; Amino_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
PE   1: Evidence at protein level;
KW   Catecholamine metabolism; Direct protein sequencing; FAD;
KW   Flavoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Neurotransmitter degradation; Oxidoreductase; Transmembrane.
FT   CHAIN         1    526       Amine oxidase [flavin-containing] A.
FT                                /FTId=PRO_0000099851.
FT   TOPO_DOM      1    497       Cytoplasmic (By similarity).
FT   TRANSMEM    498    518       Anchor for type IV membrane protein (By
FT                                similarity).
FT   TOPO_DOM    519    526       Mitochondrial intermembrane (By
FT                                similarity).
FT   REGION      520    522       Interaction with membrane phospholipid
FT                                headgroups (By similarity).
FT   SITE        335    335       Important for substrate specificity (By
FT                                similarity).
FT   SITE        374    374       Important for catalytic activity (By
FT                                similarity).
FT   MOD_RES     406    406       S-8alpha-FAD cysteine (By similarity).
SQ   SEQUENCE   526 AA;  59588 MW;  47FACA3581758217 CRC64;
     MTDLEKPSIT GHMFDVVVIG GGISGLAAAK LLSEYKINVL VLEARDRVGG RTYTVRNEHV
     KWVDVGGAYV GPTQNRILRL SKDLGIETYK 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
//