ID A0A1S3G1K5_DIPOR Unreviewed; 755 AA.
AC A0A1S3G1K5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=Aoc1 {ECO:0000313|RefSeq:XP_012882683.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012882683.1};
RN [1] {ECO:0000313|RefSeq:XP_012882683.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012882683.1};
RG RefSeq;
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 RefSeq; XP_012882683.1; XM_013027229.1.
DR AlphaFoldDB; A0A1S3G1K5; -.
DR STRING; 10020.ENSDORP00000003827; -.
DR GeneID; 105993860; -.
DR KEGG; dord:105993860; -.
DR CTD; 26; -.
DR InParanoid; A0A1S3G1K5; -.
DR OrthoDB; 5490352at2759; -.
DR Proteomes; UP000081671; Unplaced.
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: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:UP000081671};
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_5010255421"
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; 86157 MW; D2D2E0CBA544825D CRC64;
MGQESLALGW VAAALLVLQM AVAERPLWML EGKAGVFADL SAQELKAVHS FLRSRKELRL
QPSTVPTMAK NSVFLIEMLL PKKKRVLKFL DKGKRQPARE ARVVIFFGDQ EHPNITEFAV
GPLPEPCSMR MLPPRPGHQP SWESRPITTV EYDLLYAMVE EATRPLHQFF LDTTGFSFHK
CSDRCLTFTD VAPRGLASGQ RRSWLIFQRF VEGYFLHPTG LELLVDHGSL NPEHWTVEQL
WYNGKFYQSP MELAQKYDSG EVDKVVLEDP VPQGQTAESA EELPLFSSYT PRGDFPSPTR
TAGPRLVQPH TPRYLLEGNA VLYMGWSFAF RLRSSSGLQI LNVHFGGERV AYEVSVQEAV
ALYGGHTPAG MQTKYIDAGW GMGTVTHELA PGIDCPDTAT FLDAFHYYDT NDPVRYPRAL
CLFEMPTGVP LRRHFDSNFR GGFTFYAGLT GQVLVLRTTS TVYNYDYIWD FIFHPNGVME
AKMHATGYVH ATFYTPEGLR YGSRLHTHLL GNIHTHLVHY RVDLDVAGTK NSFQTLQMKL
ENITNPWSPR QQLVQPFLKQ KRHLHERQAA FHYDQALPKY LLFTSPQKNP WGHTRSYRLQ
IHSMAEQVLP LGWREEQAIT WARYPLAVTK HQDSEQSSSS IYNQNDPWHP PVVFEEFLRN
NESIENEDLV AWVTLGFLHI PHSEDIPNTA TPGNSVGFLL RPFNFFPEDP SLASRDTVIV
WPRDKGPNFV QRWLSEDKDC LAPPNFSYNG TYKPV
//
