ID A0A2K6F3B0_PROCO Unreviewed; 755 AA.
AC A0A2K6F3B0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=AOC1 {ECO:0000313|Ensembl:ENSPCOP00000008463.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000008463.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000008463.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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_012517603.1; XM_012662149.1.
DR AlphaFoldDB; A0A2K6F3B0; -.
DR STRING; 379532.ENSPCOP00000008463; -.
DR Ensembl; ENSPCOT00000019017.1; ENSPCOP00000008463.1; ENSPCOG00000015517.1.
DR GeneID; 105824630; -.
DR KEGG; pcoq:105824630; -.
DR CTD; 26; -.
DR GeneTree; ENSGT00950000183207; -.
DR OMA; PYNSQDV; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0052597; F:diamine oxidase activity; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:Ensembl.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0048038; F:quinone binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0097185; P:cellular response to azide; IEA:Ensembl.
DR GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
DR GO; GO:0035874; P:cellular response to copper ion starvation; IEA:Ensembl.
DR GO; GO:0071420; P:cellular response to histamine; IEA:Ensembl.
DR GO; GO:0009445; P:putrescine metabolic process; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
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:SF3; AMILORIDE-SENSITIVE AMINE OXIDASE [COPPER-CONTAINING]; 1.
DR PANTHER; PTHR10638; COPPER 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 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:UP000233160};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..755
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014386848"
FT DOMAIN 43..127
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 145..245
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 305..711
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 377
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 465
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 465
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 755 AA; 86122 MW; 0B8ACF0D46D07897 CRC64;
MGQETLALLG ATAAILVLQA AAVEHSPWTL HGKARVFADL SAQELKAVHS FLRSRKDLRL
EPSTALTMAK NTVFLIEMLL PKKQHVLRFL DKGERRPVRE ARVVIFFGAQ EHPNITEFAV
GPLPWPYHMR VLSPRPGHQP SWASRPISMA EYALLYHTLQ EATKPLHQFF LDTTGFSFQD
CHNRCLTFSD VAPRGLASGQ RRTWFIIQRF VEDYFLHPTG LELLVDHGST DAQRWAVEQV
WYNGKFYRSP EELAQKYADG EVDVVVLEDP MPKEKGQEST EEPTLFFSHK SHGDFSSPIS
VSGPRLVQPH GPRYRLEGNA VLYGGWSFAF RLRSSSGLQV LNVHFGVERI AYEVSVQEAV
ALYGGHTPAG MQTKYMDVGW GLGSVTHELA PGIDCPETAT FVDALHYYDA DDPVNYPRAL
CLFEMPTGVP LRRHFNSNFS GGFDFYAGLK GQVLVLRTTS TVYNYDYIWD FIFYPNGVME
AKMHATGYVH ATFYTPEGLR YGTRLHTHLM GNMHTHLVHY RVDLDVAGTK NSFQTLQMKL
ENITNPWSPR HHLVQPTLQQ TRYPRERQAA FRFGRTLPRY LLFSSPEHNP WGHQRSYRLQ
IHSMADQVLP PGWQEEQAVT WARYPLAVTK YRESELCSSS IYNQNDPWAP PVVFEEFLHN
NENIENEDLV AWVTVGFLHI PHSEDVPNTA TPGNSVGFLL RPFNFFPEDP SVASRDTVIV
WPRDNGSNYV QRWIPEDRDC SVPPPFSYNG TYRPV
//
