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Database: UniProt
Entry: A0A3Q7SLL7_VULVU
LinkDB: A0A3Q7SLL7_VULVU
Original site: A0A3Q7SLL7_VULVU 
ID   A0A3Q7SLL7_VULVU        Unreviewed;       763 AA.
AC   A0A3Q7SLL7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   Name=AOC3 {ECO:0000313|RefSeq:XP_025842875.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025842875.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025842875.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025842875.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025842875.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|ARBA:ARBA00001935};
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU000672};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000256|RuleBase:RU000672};
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000256|PIRSR:PIRSR600269-51,
CC       ECO:0000256|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
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DR   RefSeq; XP_025842875.1; XM_025987090.1.
DR   AlphaFoldDB; A0A3Q7SLL7; -.
DR   STRING; 9627.ENSVVUP00000033097; -.
DR   Ensembl; ENSVVUT00000043705; ENSVVUP00000033095; ENSVVUG00000023933.
DR   Ensembl; ENSVVUT00000043707; ENSVVUP00000033097; ENSVVUG00000023933.
DR   OMA; CMFEIDK; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0052595; F:aliphatic amine oxidase activity; IEA:RHEA.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0008131; F:primary amine oxidase activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0009308; P:amine metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.10.450.40; -; 2.
DR   Gene3D; 2.70.98.20; Copper amine oxidase, catalytic domain; 1.
DR   InterPro; IPR000269; Cu_amine_oxidase.
DR   InterPro; IPR015798; Cu_amine_oxidase_C.
DR   InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR   InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR   InterPro; IPR015800; Cu_amine_oxidase_N2.
DR   InterPro; IPR015802; Cu_amine_oxidase_N3.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638:SF23; MEMBRANE PRIMARY AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   Pfam; PF02728; Cu_amine_oxidN3; 1.
DR   PRINTS; PR00766; CUDAOXIDASE.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000672};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000672};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..763
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018748772"
FT   DOMAIN          66..150
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          169..269
FT                   /note="Copper amine oxidase N3-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02728"
FT   DOMAIN          316..716
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
FT   ACT_SITE        386
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   ACT_SITE        471
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT   MOD_RES         471
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ   SEQUENCE   763 AA;  84230 MW;  821DC37DBEC4CD4B CRC64;
     MNQKTTLVLL ALAVITIFAL VCVLLAGRGG DGGEPGQPPS CAAVSPSAQP WTHPGQSQLF
     ADLSREELTA VMSFLTQQLG PGLVDAAQAR PSDNCVFSVE LHLPSKAAAL AHLDRGSPPP
     AREALAIIFF GGQPQPNVSE LVVGPLPHPT HLRDVTVERH GGPLPYHRRP VLIREYLDID
     QLIFDRELPQ AAGLLHHCCF YKRQGRNLVT MNTAPRGLQS GDRATWFGLY YNISGAGIFL
     HPVGLELLVD HKALDPAHWT IQKVFFQGRY YDSLAHLEDQ FEAGLVNVVL VPDNGTGGSW
     SLKSQVPPGP APPLQFLPQG PRFSVQGSRV SSSLWTFSFG LGAFSGPRIF DIRFQGERLA
     YEISLQEALA IYGGNSPAAM LTRYIDGSFG MGKYSTPLTR GVDCPYLATY VDWHYLLESH
     TPKTIRDAIC VFEQNQGLPL RRHHSDFYSH YFGGLAETVL ILRSVSTLLN YDYLWDMVFH
     PNGAIEVRLH ATGYISSAFL FGAARRYGNQ VREHTLGTVH THSAHFKVDL DVGGLENWVW
     AEDMTYVPTA VPWSPEHQMQ RLQVTRKLLE TEEQAAFPLG GTLPRYVHLA SNHSNKWGHP
     RGYRIQLLSF AGEPLPQNSS LERAFSWGRY QLAVTQRKEE EPSSTSIYNQ NDPWAPTVDF
     EDFINNETIA GEDLVAWVTA GFLHIPHAED VPNTVTVGNA VGFFLRPYNF FDQDPSFDSA
     DSVYFQGNQD AGACEVNPLA CLPQSAACAP DLPAFSHGGF SHN
//
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