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Database: UniProt
Entry: M4ATE9_XIPMA
LinkDB: M4ATE9_XIPMA
Original site: M4ATE9_XIPMA 
ID   M4ATE9_XIPMA            Unreviewed;       541 AA.
AC   M4ATE9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Tyrosinase {ECO:0000256|ARBA:ARBA00039304};
DE            EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
DE   AltName: Full=Monophenol monooxygenase {ECO:0000256|ARBA:ARBA00042251};
GN   Name=TYR {ECO:0000313|Ensembl:ENSXMAP00000017744.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000017744.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000017744.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000017744.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|ARBA:ARBA00001973};
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004573}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
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DR   RefSeq; XP_005807149.1; XM_005807092.1.
DR   AlphaFoldDB; M4ATE9; -.
DR   STRING; 8083.ENSXMAP00000017744; -.
DR   Ensembl; ENSXMAT00000017769.2; ENSXMAP00000017744.1; ENSXMAG00000017698.2.
DR   GeneID; 102216777; -.
DR   KEGG; xma:102216777; -.
DR   eggNOG; ENOG502QRET; Eukaryota.
DR   GeneTree; ENSGT00940000155336; -.
DR   HOGENOM; CLU_038693_1_0_1; -.
DR   InParanoid; M4ATE9; -.
DR   OMA; FLLRWEH; -.
DR   OrthoDB; 70287at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd00055; EGF_Lam; 1.
DR   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   PANTHER; PTHR11474:SF124; TYROSINASE; 1.
DR   PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   3: Inferred from homology;
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..541
FT                   /note="Tyrosinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004048464"
FT   TRANSMEM        474..499
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..220
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          384..395
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   541 AA;  62037 MW;  3DE487C8384923EB CRC64;
     MWRLKVIIFI LYLVPTYQQF PRLCVTQQAL RTKECCPVWE GDGSACGAGS GRGSCEDVKI
     SEQPDGPQYP FSGLDDREKW PLVFYNRTCQ CAGNFMGFNC GDCKFGYFGD NCNERRVSLR
     RNIFHLTRAE RNRLISYLNL AKQTISREYV VATGTYREME NGSNPMFADV SVYDVFVWMH
     YYVSRNALLG GPGNVWRNVD FGHWAPAFPP WHRVYLLHWE HEIRKLTGDM TFSIPYWDWR
     DAQDCEVCTD ELMGARSPQN PNLISPSSVF SSWKVLCSQA EEYSNRGVLC DARNEGPLRR
     NPGNHNQNIV ERLPTSADVE FTLSLPNYDT GAMDRTANMS FRNTLEGFGD PQTGLGSSSR
     LGMHASLHVF MNGSMSSVQG SANDPIFMLH HAFVDSIYEQ WLRRHKPSPS QYPESNAPIG
     HNGDYHMPPF IPLHRNKEYF ISSKDLGYEY SYLLDANQRL AESMRPYLDE LHDVWPLLIL
     AVLCGGIVTV AIAIAILLAK HRFKAWPRRK SWKNFFALPE KQPLIWNNET EASHHNYQTT
     M
//
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