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Database: UniProt
Entry: A0A4W3JJY3_CALMI
LinkDB: A0A4W3JJY3_CALMI
Original site: A0A4W3JJY3_CALMI 
ID   A0A4W3JJY3_CALMI        Unreviewed;       523 AA.
AC   A0A4W3JJY3;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
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:ENSCMIP00000032430.1};
OS   Callorhinchus milii (Ghost shark).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX   NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000032430.1, ECO:0000313|Proteomes:UP000314986};
RN   [1] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17185593; DOI=10.1126/science.1130708;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Ancient noncoding elements conserved in the human genome.";
RL   Science 314:1892-1892(2006).
RN   [2] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17407382;
RA   Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA   Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA   Brenner S.;
RT   "Survey sequencing and comparative analysis of the elephant shark
RT   (Callorhinchus milii) genome.";
RL   PLoS Biol. 5:E101-E101(2007).
RN   [3] {ECO:0000313|Proteomes:UP000314986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24402279; DOI=10.1038/nature12826;
RG   International Elephant Shark Genome Sequencing Consortium;
RA   Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA   Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA   Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA   Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA   Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA   Wilson R.K., Brenner S., Warren W.C.;
RT   "Elephant shark genome provides unique insights into gnathostome
RT   evolution.";
RL   Nature 505:174-179(2014).
RN   [4] {ECO:0000313|Ensembl:ENSCMIP00000032430.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A4W3JJY3; -.
DR   Ensembl; ENSCMIT00000032922.1; ENSCMIP00000032430.1; ENSCMIG00000013755.1.
DR   GeneTree; ENSGT00940000155336; -.
DR   Proteomes; UP000314986; 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   Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
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:UP000314986};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        470..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          198..215
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          379..390
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
FT   REGION          500..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  59513 MW;  264AF847ED752199 CRC64;
     ILISVLYQLD TVSPQFPRAC TPADNLMRKE CCPAWSGDGS PCGELSGRGS CQDVSVSDAP
     NGPQFPLSGV DDREGWPSVF YTRTCHCAEN FMGFNCADCR FGRFGINCTA RRTSIRKNIL
     ELSGAEKDKF LAYLNLAKST ISQDYQIAVG TYTQMSNGSN PMFRDISVYD LFVWMHYYVS
     RDTLLGASRV WKDIDFAHEA PAFLPWHRAF LLLWENEIRK TAGDENFTIP YWDWRDLESC
     EVCTDEYLGG RHSTIPNLLS PASFFSYWQV ICTRSEDYNN GNFLCDGTPE GPILRNPGHH
     DRTKTPNLPT SADVEFSLSL TEYETAPFDK FANFSFRNTL EGFANPNTGI SNTSQSSLHN
     ALHIYMNGSM SQVSGSANDP IFLLHHVFVD SIFEQWLRRH RPLQDIYPAM NTPIGHNRDY
     YMVPFIPIYR NIEFFLSSQE LGYDYDYLTE PAPRSVQNFL APYLEEARRI WPWLLSAAVI
     GALVNAIFSL IIAMARTKKK KQNGTTEEQQ PLLKNTNEYQ TTM
//
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