ID W5P1J8_SHEEP Unreviewed; 766 AA.
AC W5P1J8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN Name=LOC101113086 {ECO:0000313|Ensembl:ENSOARP00000004297.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000004297.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000004297.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000004297.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000004297.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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 EMBL; AMGL01018695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01018696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01018697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01018698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5P1J8; -.
DR SMR; W5P1J8; -.
DR STRING; 9940.ENSOARP00000004297; -.
DR PaxDb; 9940-ENSOARP00000004297; -.
DR Ensembl; ENSOART00000004373.1; ENSOARP00000004297.1; ENSOARG00000004027.1.
DR eggNOG; KOG1186; Eukaryota.
DR HOGENOM; CLU_015739_1_0_1; -.
DR OMA; SSMWNMN; -.
DR Proteomes; UP000002356; Chromosome 11.
DR Bgee; ENSOARG00000004027; Expressed in lung and 47 other cell types or tissues.
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:UP000002356};
KW TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|PIRSR:PIRSR600269-50}.
FT DOMAIN 66..152
FT /note="Copper amine oxidase N2-terminal"
FT /evidence="ECO:0000259|Pfam:PF02727"
FT DOMAIN 170..270
FT /note="Copper amine oxidase N3-terminal"
FT /evidence="ECO:0000259|Pfam:PF02728"
FT DOMAIN 316..718
FT /note="Copper amine oxidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01179"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT ACT_SITE 472
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-50"
FT MOD_RES 472
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000256|PIRSR:PIRSR600269-51"
SQ SEQUENCE 766 AA; 85247 MW; 4FFED685DC2CF824 CRC64;
MNQKTTLVLL ALAVITIFAL VCVLLAGRGG DGGEASQPHY CPSGTPSVQP WTHPDHSQLF
ADLSREELRA VMSFLTQQLG PDLVDAAQAR PSDNCIFSVE LQLPPRAAAL AHLDRGSPPP
AREALAIIFF GRQPQPNVTE LVVGPLPQPS YMRDDVTVER HGGPLPYYRR PVLLREYLDI
DQMIFDRELP KAAGVLHRCC SYRQGGGNLV ILSTAPRGVQ SGNRATWFGL YYNISGFGVY
LHPVGLELLV DHKALDPAQW TIQKVFFQGR YYESLAQLEE QFEAGQVNVV VIPNNGTGGS
WSLKSQVPPG PTPPLQFHPQ GPRFKIEGNR VSSSLWTFSF GLGGFNGPRI FDIRFQGERI
AYELSVQEAL AIYGGNSPYA LRGRYADANF GLGYFSTPLS RGVDCPYLAT YVDWHFLLES
QAPKTLRDAF CVFEQNKGLP LRRHHSDFLS HYFGGVVETV LVFRSVSTML NYDYVWDMIF
HPNGAIEVKF HATGYIGSVF LFGDARRYGN QVRENTLGTI HTHSAHYKVD LDVGGLENWV
WAEDMAFVPT AIPWSPEHQI QRLQVTRKQL ETEDQAAFPL GGASPRYLYL ASKQSNKWGH
PRGYRIQTVS FAGEPLPQNS SMERAFSWAR YQLAVTQRKE GEPSSTSIYN LNDPWSPTLD
FSDFINNETI AGQDLVAWVT VGFLHIPHAE DIPNTVTVGN GVGFFLRPYN FFDQEPSMDS
ADSIYFREDQ DAGSCEVNSL ACLSQAPACV PDLPTFSHGG FSHNQV
//