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Database: UniProt
Entry: Q53EZ0_HUMAN
LinkDB: Q53EZ0_HUMAN
Original site: Q53EZ0_HUMAN 
ID   Q53EZ0_HUMAN            Unreviewed;       527 AA.
AC   Q53EZ0;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU362067};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU362067};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD97219.1};
RN   [1] {ECO:0000313|EMBL:BAD97219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose tissue {ECO:0000313|EMBL:BAD97219.1};
RX   PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8;
RA   Maruyama K., Sugano S.;
RT   "Oligo-capping: a simple method to replace the cap structure of eukaryotic
RT   mRNAs with oligoribonucleotides.";
RL   Gene 138:171-174(1994).
RN   [2] {ECO:0000313|EMBL:BAD97219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose tissue {ECO:0000313|EMBL:BAD97219.1};
RX   PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3;
RA   Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.;
RT   "Construction and characterization of a full length-enriched and a 5'-end-
RT   enriched cDNA library.";
RL   Gene 200:149-156(1997).
RN   [3] {ECO:0000313|EMBL:BAD97219.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adipose tissue {ECO:0000313|EMBL:BAD97219.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00033614};
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:0000256|ARBA:ARBA00033618};
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:0000256|ARBA:ARBA00033669};
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:0000256|ARBA:ARBA00036170};
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:0000256|ARBA:ARBA00036674};
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:0000256|ARBA:ARBA00033622};
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:0000256|ARBA:ARBA00036934};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59597;
CC         Evidence={ECO:0000256|ARBA:ARBA00036934};
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:0000256|ARBA:ARBA00000205};
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:0000256|ARBA:ARBA00001138};
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:0000256|ARBA:ARBA00033704};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362067};
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. {ECO:0000256|ARBA:ARBA00025863}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000256|ARBA:ARBA00004362}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004362}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004362}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000256|ARBA:ARBA00005995, ECO:0000256|RuleBase:RU362067}.
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DR   EMBL; AK223499; BAD97219.1; -; mRNA.
DR   AlphaFoldDB; Q53EZ0; -.
DR   SMR; Q53EZ0; -.
DR   PeptideAtlas; Q53EZ0; -.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProt.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 6.10.250.130; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR   PANTHER; PTHR43563:SF11; AMINE OXIDASE [FLAVIN-CONTAINING] A; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   2: Evidence at transcript level;
KW   Catecholamine metabolism {ECO:0000256|ARBA:ARBA00022939};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362067};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362067}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362067};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          23..460
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD97219.1"
SQ   SEQUENCE   527 AA;  59656 MW;  10B0ECE543945F38 CRC64;
     MENQEKASIA GHMFDVVVIG GGISGLSAAK LLTEYGVSVL VLEARDRVGG RTYTIRNEHV
     DYVDVGGAYV GPTQNRILRL SKELGIETHK VNVSERLVQY VKGKTYPFRG AFPPVWNPIA
     YLDYNNLWRT IDNMGKEIPT DAPWEAQHAD KWDKMTMKEL IDKICWTKTA RRFAYLFVNI
     NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSV TNGGQERKFV GGSGQVSERI MDLLGDQVKL
     NHPVTHVDQS SDNIIIETLN HEHYECKYVI NAIPPTLTAK IHFRPELPAE RNQLIQRLPM
     GAVIKCMMYY KEAFWKKKDY CGCMIIEDED APISITLDDT KPDGSLPAIM GFILARKADR
     LAKLHKEIRK KKICELYAKV LGSQEALHPV HYEEKNWCEE QYSGGCYTAY FPPGIMTQYG
     RVIRQPVGRI FFAGTETATK WSGYMEGAVE AGERAAREVL NGLGKVTEKD IWVQEPESKD
     VPAVEITHTF WERNLPSVSG LLKIIGFSTS VTALGFVLYK YKLLPRS
//
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