ID   TYRO1_PINMG             Reviewed;         492 AA.
AC   H2A0L0;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Tyrosinase-like protein 1;
DE            EC=1.14.18.-;
DE   AltName: Full=Tyrosinase 1;
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 121-131 AND 458-469, SUBCELLULAR LOCATION, AND TISSUE
RP   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(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:P06845};
CC       Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:P06845};
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}.
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DR   EMBL; HE610377; CCE46151.1; -; mRNA.
DR   AlphaFoldDB; H2A0L0; -.
DR   SMR; H2A0L0; -.
DR   PRIDE; H2A0L0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016716; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, another compound as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR015559; Tyr-like.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF21; PTHR11474:SF21; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Metal-binding; Oxidoreductase; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..492
FT                   /note="Tyrosinase-like protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417979"
FT   REGION          472..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         147
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         155
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         164
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="A"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         289
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         293
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
FT   BINDING         316
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000250|UniProtKB:P06845"
SQ   SEQUENCE   492 AA;  55061 MW;  D4630DE7D3FC0930 CRC64;
     MDKMRTLQSL IVKLTLLYGA LCMLQTENVK EINKQECIQN AVYNFNTTDS KYLDPKCVTI
     FMDQYRGLKN LLNYTEDQMN YIFSLERAMM RKHHINDKRH KRQAMTRPRQ ECRTLTDDAR
     NNLFNTIVDL KAPSNGMSRY DTIAGLHRQA IANAHMGANF LGWHRLYLDM FEMALQETRS
     DVVLCYWDST LDFLMPGTSQ VNTVSFSAEL FGNGRGVVIN GPFRFWRLPG GRTLQRFIAR
     PGSSLTRPGV VDLIATDPRI NTNSQIVFRG QGFPDPDTGR PGHSWEDEHN NTHVWVGGVM
     QNVVSSPQDP VFWFHHTYVD YVWELFRQKI GPGAREQYPA DASGPHAPDA PMIGFDMLQN
     RDGYSDEHSR MYAMHPRCSN NCGNSRFLLC PNNGPMADPN RRCVSRAVNS DMVPAAAISA
     PEAAGFSAMS PMGAFGPAAV GPSSVGRMAS RSGAARVSLQ ATDTVAIRAA MSEPPLQLEG
     PSFTSSFDDP RI