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AOFA_BOVIN
ID   AOFA_BOVIN              Reviewed;         527 AA.
AC   P21398; Q0IIE7;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Amine oxidase [flavin-containing] A {ECO:0000250|UniProtKB:P21397};
DE            EC=1.4.3.21 {ECO:0000250|UniProtKB:P21396};
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:0000250|UniProtKB:P21397};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2719656; DOI=10.1042/bj2590407;
RA   Powell J.F., Hsu Y.-P.P., Weyler W., Chen S.A., Salach J.,
RA   Andrikopoulos K., Mallet J., Breakefield X.O.;
RT   "The primary structure of bovine monoamine oxidase type A. Comparison with
RT   peptide sequences of bovine monoamine oxidase type B and other
RT   flavoenzymes.";
RL   Biochem. J. 259:407-413(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative deamination of primary and some
CC       secondary amine such as neurotransmitters, with concomitant reduction
CC       of oxygen to hydrogen peroxide and has important functions in the
CC       metabolism of neuroactive and vasoactive amines in the central nervous
CC       system and peripheral tissues. Preferentially oxidizes serotonin. Also
CC       catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-
CC       3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline.
CC       {ECO:0000250|UniProtKB:P21396}.
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:0000250|UniProtKB:P21396};
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 + 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: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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA33633.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X15609; CAA33632.1; -; mRNA.
DR   EMBL; X15609; CAA33633.1; ALT_INIT; mRNA.
DR   EMBL; BC122682; AAI22683.1; -; mRNA.
DR   PIR; S03974; S03974.
DR   RefSeq; NP_851357.2; NM_181014.2.
DR   AlphaFoldDB; P21398; -.
DR   SMR; P21398; -.
DR   STRING; 9913.ENSBTAP00000021570; -.
DR   BindingDB; P21398; -.
DR   ChEMBL; CHEMBL3254; -.
DR   DrugCentral; P21398; -.
DR   PaxDb; P21398; -.
DR   PeptideAtlas; P21398; -.
DR   Ensembl; ENSBTAT00000021570; ENSBTAP00000021570; ENSBTAG00000016206.
DR   GeneID; 281293; -.
DR   KEGG; bta:281293; -.
DR   CTD; 4128; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016206; -.
DR   VGNC; VGNC:31174; MAOA.
DR   eggNOG; KOG0029; Eukaryota.
DR   GeneTree; ENSGT00940000160514; -.
DR   HOGENOM; CLU_004498_0_1_1; -.
DR   InParanoid; P21398; -.
DR   OMA; EWTRGAY; -.
DR   OrthoDB; 1034142at2759; -.
DR   TreeFam; TF313314; -.
DR   BRENDA; 1.4.3.4; 908.
DR   Reactome; R-BTA-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR   Reactome; R-BTA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-BTA-379397; Enzymatic degradation of dopamine by COMT.
DR   Reactome; R-BTA-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR   Reactome; R-BTA-380612; Metabolism of serotonin.
DR   PRO; PR:P21398; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000016206; Expressed in rumen epithelium and 102 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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; ISS:UniProtKB.
DR   GO; GO:0042420; P:dopamine catabolic process; IEA:Ensembl.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009967; P:positive regulation of signal transduction; IEA:Ensembl.
DR   Gene3D; 3.50.50.60; -; 2.
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   2: Evidence at transcript level;
KW   Acetylation; Catecholamine metabolism; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Neurotransmitter degradation;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..527
FT                   /note="Amine oxidase [flavin-containing] A"
FT                   /id="PRO_0000099847"
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..527
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        376
FT                   /note="L -> R (in Ref. 1; CAA33632/CAA33633)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   527 AA;  59758 MW;  BC69ED43644DAF37 CRC64;
     MESLQKTSDA GQMFDVVVIG GGISGLSAAK LLAEHEVNVL VLEARERVGG RTYTVRNEHV
     DYVDVGGAYV GPTQNRILRL SKQLGLETYK VNVNERLVHY VKGKTYPFRG AFPPVWNPIA
     YLDYNNLWRT MDNMGKEIPA DAPWEAPHAV EWDKMTMKDL IEKICWTKTA RQFASLFVNI
     NVTSEPHEVS ALWFLWYVKQ CGGTTRIFSI TNGGQERKFV GGSGQVSERI MQLLGDRVKL
     RSPVTYVDQS SENITVETLN RELYECRYVI SAIPPTLTAK IHFRPELPSE RNQLIQRLPM
     GAVIKCMMYY KEAFWKKKDY CGCMIIEDEE APISITLDDT KPDGSLPAIM GFILARKADR
     LAKVHKDIRK RKICELYAKV LGSQEALHPV HYEEKNWCQE QYSGGCYTAY FPPGIMTQYG
     RVIRQPVGRI YFAGTETATQ WSGYMEGAVE AGERAAREVL NALGKLSAKD IWIQEPEAED
     VPAVEITPSF WERNLPSVSG LLKIVGFSTS ITALWFVMYR FRLLSRS
 
 
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