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Database: UniProt
Entry: P55028
LinkDB: P55028
Original site: P55028 
ID   TYRP1_CARAU             Reviewed;         522 AA.
AC   P55028;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   22-NOV-2017, entry version 86.
DE   RecName: Full=5,6-dihydroxyindole-2-carboxylic acid oxidase;
DE            Short=DHICA oxidase;
DE            EC=1.14.18.-;
DE   AltName: Full=Tyrosinase-related protein 1;
DE            Short=TRP-1;
DE            Short=TRP1;
DE   Flags: Precursor;
GN   Name=tyrp1;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8072947; DOI=10.1111/j.1600-0749.1994.tb00014.x;
RA   Peng G., Taylor J.D., Tchen T.T.;
RT   "Goldfish tyrosinase related protein I (TRP-1): deduced amino acid
RT   sequence from cDNA and comments on structural features.";
RL   Pigment Cell Res. 7:9-16(1994).
CC   -!- FUNCTION: Catalyzes the oxidation of 5,6-dihydroxyindole-2-
CC       carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid.
CC       May regulate or influence the type of melanin synthesized. Also to
CC       a lower extent, capable of hydroxylating tyrosine and producing
CC       melanin. {ECO:0000250|UniProtKB:P07147}.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC       Note=Binds 2 copper ions per subunit.
CC       {ECO:0000250|UniProtKB:Q9ZP19};
CC   -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000250|UniProtKB:P07147}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P07147}. Melanosome
CC       {ECO:0000250|UniProtKB:P07147}. Note=Located to mature stage III
CC       and IV melanosomes and apposed endosomal tubular membranes.
CC       Transported to pigmented melanosomes by the BLOC-1 complex. Proper
CC       trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A,
CC       RAB32 and RAB38. {ECO:0000250|UniProtKB:P07147}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
DR   EMBL; S71755; AAC60750.1; -; mRNA.
DR   PIR; I51245; I51245.
DR   ProteinModelPortal; P55028; -.
DR   SMR; P55028; -.
DR   HOVERGEN; HBG003553; -.
DR   UniPathway; UPA00785; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   InterPro; IPR008922; Unchr_di-copper_centre.
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   2: Evidence at transcript level;
KW   Copper; Disulfide bond; Glycoprotein; Melanin biosynthesis; Membrane;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    522       5,6-dihydroxyindole-2-carboxylic acid
FT                                oxidase.
FT                                /FTId=PRO_0000035887.
FT   TOPO_DOM     22    470       Lumenal, melanosome. {ECO:0000255}.
FT   TRANSMEM    471    491       Helical. {ECO:0000255}.
FT   TOPO_DOM    492    522       Cytoplasmic. {ECO:0000255}.
FT   METAL       182    182       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       205    205       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       214    214       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       367    367       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       371    371       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       394    394       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   CARBOHYD    164    164       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    171    171       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    294    294       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    375    375       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     38       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID     39     59       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID     50     89       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID     91    100       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID    103    112       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID    248    251       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID    280    293       {ECO:0000250|UniProtKB:P17643}.
SQ   SEQUENCE   522 AA;  57519 MW;  D12410BF828C1D31 CRC64;
     MLRTSCGGML LLVHALGLVR AQFPRACVTP EGLRSAQCCP SPSALESDPC GALAGPGRCV
     DVRMRAHGPQ YPYEGATTRA LARASSRACR CNGNFGGFDC GGCAHGFTGD ACEQRVPVVR
     RNVMQLSADE KRFFVNALDQ AKRAPHPDTV IATRRYSEIL GPDNSTTQFE NISIYNLFVW
     THYYSVSKTF LGAGQDSFGG VDFSHEGPGF LTWHRYHLLQ LERDMQVMLG DPSFALPYWD
     FAIGGSECDI CTDELMGARS SSDSSSISSN SIFSRWRVIC ESVEEYDTLG TICNSSESSP
     IRRNPAGNTA RPMVQRLPEP QDVEACLELT AFDSPPFYST SSDSFRNSIE GYSAPQGNYD
     PVVRSLHNLA HLFLNGTGGQ THLSPNDPIF VLLHTFTDAV FDEWLRRHAS DASIYPLENT
     PIGHNREFNM VPFWPPVTNA EMFVTAAENL GYSYEAEWPA RPLTPTQIVT VAVVAALLLV
     AIIFAASTCV VHLRGNRTEG RQPLLGDQYQ RYEDHNKTQS VV
//
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