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Database: UniProt
Entry: A0A5N4D8R0_CAMDR
LinkDB: A0A5N4D8R0_CAMDR
Original site: A0A5N4D8R0_CAMDR 
ID   A0A5N4D8R0_CAMDR        Unreviewed;       517 AA.
AC   A0A5N4D8R0;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=L-dopachrome tautomerase {ECO:0000256|ARBA:ARBA00039823};
DE            EC=5.3.3.12 {ECO:0000256|ARBA:ARBA00038932};
DE   AltName: Full=L-dopachrome Delta-isomerase {ECO:0000256|ARBA:ARBA00042019};
DE   AltName: Full=Tyrosinase-related protein 2 {ECO:0000256|ARBA:ARBA00041443};
GN   ORFNames=Cadr_000012856 {ECO:0000313|EMBL:KAB1267482.1};
OS   Camelus dromedarius (Dromedary) (Arabian camel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX   NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1267482.1, ECO:0000313|Proteomes:UP000299084};
RN   [1] {ECO:0000313|EMBL:KAB1267482.1, ECO:0000313|Proteomes:UP000299084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Drom800 {ECO:0000313|EMBL:KAB1267482.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:KAB1267482.1};
RX   PubMed=30972949; DOI=.1111/1755-0998.13020;
RA   Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA   Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA   Burger P.A.;
RT   "Improving Illumina assemblies with Hi-C and long reads: an example with
RT   the North African dromedary.";
RL   Mol. Ecol. Resour. 19:1015-1026(2019).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dopachrome = 5,6-dihydroxyindole-2-carboxylate;
CC         Xref=Rhea:RHEA:13041, ChEBI:CHEBI:16875, ChEBI:CHEBI:57509;
CC         EC=5.3.3.12; Evidence={ECO:0000256|ARBA:ARBA00036823};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037907}.
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004573}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family.
CC       {ECO:0000256|ARBA:ARBA00009928}.
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:KAB1267482.1}.
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DR   EMBL; JWIN03000014; KAB1267482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5N4D8R0; -.
DR   Proteomes; UP000299084; Unassembled WGS sequence.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:SF4; L-DOPACHROME TAUTOMERASE; 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   Isomerase {ECO:0000256|ARBA:ARBA00023235};
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:UP000299084};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..517
FT                   /note="L-dopachrome tautomerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5024387507"
FT   TRANSMEM        467..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          211..228
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00497"
FT   DOMAIN          389..400
FT                   /note="Tyrosinase copper-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00498"
SQ   SEQUENCE   517 AA;  58351 MW;  12D0F5E7571B63F7 CRC64;
     MGPLGWGLLL GCLGCGLPPG ARAQFPRVCM TVGSLRSKEC CPPVGADPAN VCGSREGRGQ
     CTEVQADTRP WSGPYVLRNQ DDREQWPRKF FHRTCRCTGN FAGHDCGDCK FGWTGPKCEQ
     KKPLVVRQNV HSLTLQEREQ FLGALDLAKH TPHPDYVITT QHWLGLLGPN GTQPQIANCS
     IYDFFVWLHY YSVRDTLLGP GRPYKAIDFS HQGPAFVTWH RYHLLWLERD LQRLIGNESF
     ALPYWNFATG RNECDVCTDQ LLGAARPDDP TLISQNSRFS SWEIVCDSLD DYNRRVTLCN
     GTYEGLLRRN QVARNSERLP TLKDVQDCLS LKKFDNPPFF QNSTFSFRNA LEGFDKADGT
     LDSQVVGLHN LVHSFLNGTS ALPHSAANDP VFVVLHSFTD AIFDEWMKRY SPPAGAWPQE
     LAPIGHNRMY NMVPFFPPVT NEELFLTADQ LGYSYAIDLP VEETPGWTTS LSVVLGMLVV
     LVGLLALLLF LQYRRLRKGY TPLVETHLSS RRYTEEA
//
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