ID H2R2M5_PANTR Unreviewed; 755 AA.
AC H2R2M5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=AOC1 {ECO:0000313|Ensembl:ENSPTRP00000044191.5,
GN ECO:0000313|VGNC:VGNC:4264};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000044191.5, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000044191.5, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000044191.5}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AC192002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001136656.1; XM_001136656.2.
DR RefSeq; XP_016813922.1; XM_016958433.1.
DR PaxDb; 9598-ENSPTRP00000044191; -.
DR Ensembl; ENSPTRT00000045116.5; ENSPTRP00000044191.5; ENSPTRG00000019866.6.
DR Ensembl; ENSPTRT00000084555.1; ENSPTRP00000076076.1; ENSPTRG00000045385.1.
DR GeneID; 107975990; -.
DR KEGG; ptr:107975990; -.
DR CTD; 26; -.
DR VGNC; VGNC:4264; AOC1.
DR eggNOG; KOG1186; Eukaryota.
DR GeneTree; ENSGT00950000183207; -.
DR HOGENOM; CLU_015739_1_0_1; -.
DR OMA; IGFEILL; -.
DR OrthoDB; 5490352at2759; -.
DR TreeFam; TF314750; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000019866; Expressed in adult mammalian kidney and 1 other cell type or tissue.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0052597; F:diamine oxidase activity; IBA:GO_Central.
DR GO; GO:0008131; F:primary amine oxidase activity; IBA:GO_Central.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009308; P:amine metabolic process; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IBA:GO_Central.
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:UP000002277};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..755
FT /note="Amine oxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015093282"
FT DOMAIN 43..129
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..712
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; 85986 MW; D6B2FA5D36AAD587 CRC64;
MEREMPALGW AVAAILMLQM AMAEPSPGTL PRKAGVFSDL SNQELKAVHS FLWSKKELRL
QPSSTTTMAK NTVFLIEMLL PKKYHVLRFL DKGERHPVRE ARAVIFFGDQ EHPNVTEFAV
GPLPGPCYMR ALSPRPGYQS SWASRPISTA EYALLYHTLQ EATKPLHQFF LNTTGFSFQD
CHDRCLAFTD VAPRGVASGQ RRSWLIIQRY VEGYFLHPTG LELLVDHGST DARHWVVEQV
WYNGKFYGSP EELARKYADG EVDVVVLEDP LPGGKGHDST EEPPLFSSHK PRGGFPSPIH
VSGPRLVQPH GPRFRLEGNA VLYGGWSFAF RLRSSSGLQV LNVHFGGERI AYEVSVQEAV
ALYGGHTPAG MQTKYLDVGW GLGSVTHELA PGIDCPETAT FLDTFHYYDA DDPVHYPRAL
CLFEMPTGVP LRRHFNSNFK GGFNFYAGLK GQVLVLRTTS TVYNYDYIWD FIFYPNGVME
AKMHATGYVH ATFYTPEGLR HGTRLHTHLI GNIHTHLVHY RVDLDVAGTK NSFQTLQMKL
ENITNPWSPR HRVVQPTLEQ TQYSWERQAA FRFKRKLPKY LLFTSPQENP WGHKRSYRLQ
IHSMADQVLP PGWQEEQAIT WARYPLAVTK YRESELCSSS IYHQNDPWDP PVVFEKFLHN
NENIENEDLV AWVTVGFLHI PHSEDIPNTA TPGNSVGFLL RPFNFFPEDP SLASRDTVIV
WPRDNGPNYV QRWIPEDRDC SMPPPFSYNG TYRPV
//
