ID   AMO_PINMG               Reviewed;         781 AA.
AC   H2A0M3;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Putative amine oxidase [copper-containing];
DE            EC=1.4.3.- {ECO:0000250|UniProtKB:P46883};
DE   Flags: Precursor;
OS   Margaritifera margaritifera (Freshwater pearl mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=102329;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle;
RX   PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA   Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA   Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT   "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT   mantle and shell: focus on biomineralization.";
RL   BMC Genomics 11:613-613(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 67-76; 80-87; 196-202; 286-293; 303-315; 427-443;
RP   449-467; 493-506; 544-553; 578-585; 603-612 AND 761-772, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA   Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA   Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT   "Different secretory repertoires control the biomineralization processes of
RT   prism and nacre deposition of the pearl oyster shell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000250|UniProtKB:P19801};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:P19801};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P19801};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P19801};
CC   -!- COFACTOR:
CC       Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC         Evidence={ECO:0000250|UniProtKB:P19801};
CC       Note=Contains 1 topaquinone per subunit.
CC       {ECO:0000250|UniProtKB:P19801};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q43077};
CC       Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P46883}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC   -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC       Expressed primarily in the mantle with highest level in the mantle edge
CC       and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
CC   -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC       a specific tyrosyl residue. {ECO:0000250|UniProtKB:P19801}.
CC   -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC       {ECO:0000255}.
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DR   EMBL; HE610390; CCE46164.1; -; mRNA.
DR   AlphaFoldDB; H2A0M3; -.
DR   SMR; H2A0M3; -.
DR   PRIDE; H2A0M3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:InterPro.
DR   Gene3D; 2.70.98.20; -; 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   PANTHER; PTHR10638; PTHR10638; 1.
DR   Pfam; PF01179; Cu_amine_oxid; 1.
DR   PRINTS; PR00766; CUDAOXIDASE.
DR   SUPFAM; SSF49998; SSF49998; 1.
DR   SUPFAM; SSF54416; SSF54416; 2.
DR   PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR   PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Copper; Direct protein sequencing; Disulfide bond; Manganese;
KW   Metal-binding; Oxidoreductase; Secreted; Signal; TPQ.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..781
FT                   /note="Putative amine oxidase [copper-containing]"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000418018"
FT   ACT_SITE        387
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   ACT_SITE        475
FT                   /note="Schiff-base intermediate with substrate; via
FT                   topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         385..395
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         472..477
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P46883"
FT   BINDING         525
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         527
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   BINDING         534
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         534
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         536
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         536
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         579
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         671
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         674
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P46883"
FT   BINDING         676
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         682
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         682
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:Q43077"
FT   BINDING         683
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   BINDING         693
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000250|UniProtKB:P12807"
FT   MOD_RES         475
FT                   /note="2',4',5'-topaquinone"
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   DISULFID        199..203
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
FT   DISULFID        405..432
FT                   /evidence="ECO:0000250|UniProtKB:P19801"
SQ   SEQUENCE   781 AA;  89950 MW;  49A8CBC587935AF0 CRC64;
     MSLPKTANGM DKLKLCYLLL FYLGSSSLTE VSGAQTCEID SVLCTSDLSE PDDPPIFHDL
     TTKEIKSVQT YLYHQRDLRL LRPGLAKINT SFIQGMELYL PNKKDVIHYL QSKVPTPKPP
     RAAVVTIFRG DCDPAVVEEY IVFPLPWPTQ HRLHRKVPYY LRPFNDVEFA TISDFLTKQV
     DGVLRQFLEE SFGGRLINCG NRCLNFQFAS PVGPSVSNEP GARKSWYWLH QLVEYSALHP
     VDFAVLMKIV GCVYTIEKVY FNNMYFNSLQ EVALHYRNPS FPRLRIPYPV DSKQLFSKME
     RRGILFPEKP VSPPRQVEPE GKRYSVKYQE VKYMNWKFNF RLSPGLGPRL HNIRYHDRLI
     VYELALQDIV VFYSGAEPPH QYANFFDSSY MIGMNLQGMV PGVDCPTGAT FIDSHILTES
     SLKPAKLINA FCVFEQNTGD FLRRHISKTS PDGPFYEGVP SIVLVLRAIT TIANYDYTID
     FIFHHNGVLQ TKVVPTGYIL PSLYTKQNEN KYGFRLNNKL IGNLHHHLFN FKVDIDINGQ
     HNRYETLDIV LDKTSHPVSK KPYDVWYQNK IKHNLRKTEM EALFKYDFDK PMHHIFYNNN
     LKSPEGNNMA YRLVNRGMSK SLLPECSGNE GTGAWMRHQI AVTKRKETEL TSSSVYSAFG
     TKNPVVNFRN FYADNENIVD EDLVAWVTMG TYHIPHTEDL PVTHTPGLDL SFFLSPFNYF
     PEDPAMGSRD SVRIEAVDKN NLKRGIKIDK QTFPEKMTCK APIGNYFEYI LKRPNVIFDI
     Q