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Database: UniProt
Entry: W5P1J8_SHEEP
LinkDB: W5P1J8_SHEEP
Original site: W5P1J8_SHEEP 
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
//
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