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Database: UniProt
Entry: A0A210QB47_MIZYE
LinkDB: A0A210QB47_MIZYE
Original site: A0A210QB47_MIZYE 
ID   A0A210QB47_MIZYE        Unreviewed;       805 AA.
AC   A0A210QB47;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Amine oxidase {ECO:0000256|RuleBase:RU000672};
DE            EC=1.4.3.- {ECO:0000256|RuleBase:RU000672};
GN   ORFNames=KP79_PYT15397 {ECO:0000313|EMBL:OWF45958.1};
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF45958.1, ECO:0000313|Proteomes:UP000242188};
RN   [1] {ECO:0000313|Proteomes:UP000242188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX   PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA   Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA   Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA   Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA   Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA   Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA   Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA   Chourrout D., Li R., Bao Z.;
RT   "Scallop genome provides insights into evolution of bilaterian karyotype
RT   and development.";
RL   Nat. Ecol. Evol. 1:120-120(2017).
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|RuleBase:RU000672}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000256|ARBA:ARBA00007983, ECO:0000256|RuleBase:RU000672}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OWF45958.1}.
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DR   EMBL; NEDP02004357; OWF45958.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A210QB47; -.
DR   STRING; 6573.A0A210QB47; -.
DR   EnsemblMetazoa; XM_021507066.1; XP_021362741.1; LOC110456370.
DR   OrthoDB; 2961225at2759; -.
DR   Proteomes; UP000242188; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR10638:SF20; AMINE OXIDASE; 1.
DR   PANTHER; PTHR10638; COPPER AMINE OXIDASE; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   Pfam; PF02727; Cu_amine_oxidN2; 1.
DR   PRINTS; PR00766; CUDAOXIDASE.
DR   SUPFAM; SSF49998; Amine oxidase catalytic domain; 1.
DR   SUPFAM; SSF54416; Amine oxidase N-terminal region; 2.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000672};
KW   Membrane {ECO:0000256|SAM:Phobius};
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:UP000242188};
KW   TPQ {ECO:0000256|ARBA:ARBA00022772, ECO:0000256|RuleBase:RU000672};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          109..168
FT                   /note="Copper amine oxidase N2-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02727"
FT   DOMAIN          340..751
FT                   /note="Copper amine oxidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01179"
SQ   SEQUENCE   805 AA;  93572 MW;  747FEBB37D4C5D39 CRC64;
     MERIEKQVVT MEKTLDSARR WRSFSVCLLI VIIFLMAAIA TAIVYYELIM RPKKLAHEVI
     IQETVDIEEE PTEPSMFRDL TKLEMKRLKK YLYTHRVFNL KYTEPVVISS SFMFLAELHL
     PNKSQALDTF NSLHKAPPRE AKVVLFRGDK KIPVIEEYVV GPLANITYHR LLVSKHYQRP
     APYLFRPNSQ AEYAEVKKLL VEVDNIIKYV LLESYDASFF NCNRKCLVMQ QWTAVSPAVS
     GSDVRKVWYW AHHSTEYYLF NPVDFFILFN LDGKDPSKYH VETIWYNGQS FDTAEHLADA
     FTAGTIKKSS MIFPKENQML FSTLNLRGNQ FPNKNMRSPK QVEPDGRRYN RKDRHITYMG
     WEFDFRMSTT TGPQLFNIKH MGHRIVYELS LQEMSSFHSG FKPWNRYSDM LYSNSLMGYQ
     ARNLVPGADC PPSASFVSAT HWTEHRSEPV TYERAFCLFE QSTGVPLRRH HAYDSVTGRF
     YGSLEDIVLV LRTIISVYNQ DCVVDFIFHQ NGALEVKTSL TGYMMAMLHS LPEGRYGFQL
     RDRLIGTVSQ HAFNFKVDLD IHETKNRYET LQFEPHSINN NDWSTEKNSR YEQIKFTRNS
     KMTELHTLYR QNASVPMYHI FYNKGYKTTY NDPRAYRLQI DGGLTQLLSQ GTGNEPSISW
     ARYQMAVTRR KDDEGQSSSI YAMWDKKEPI VNFQSFLDDN ESIVDTDLVA WVTLGLHHLP
     QMEDLPLISS IGKRLSFFLT PFNYHDSDPS MASRDAIRMS YDGTSGTDQA VRVENYGLPK
     DFTCDSEYQG GSESNYNLST LFEQN
//
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