TYRP1_CARAU
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 03-AUG-2022, entry version 94.
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; Cyprininae; 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 sequence
RT from cDNA and comments on structural features.";
RL Pigment Cell Res. 7:9-16(1994).
CC -!- FUNCTION: Plays a role in melanin biosynthesis. Catalyzes the oxidation
CC of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-
CC quinone-2-carboxylic acid. May regulate or influence the type of
CC melanin synthesized. Also to a lower extent, capable of hydroxylating
CC tyrosine and producing melanin. {ECO:0000250|UniProtKB:P07147}.
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P17643};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P17643};
CC Note=Contains bound zinc ions after heterologous expression in insect
CC cells. {ECO:0000250|UniProtKB:P17643};
CC -!- PATHWAY: Pigment biosynthesis; melanin biosynthesis.
CC {ECO:0000250|UniProtKB:P17643}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane
CC {ECO:0000250|UniProtKB:P07147}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P07147}. Melanosome
CC {ECO:0000250|UniProtKB:P07147}. Note=Located to mature stage III and IV
CC melanosomes and apposed endosomal tubular membranes. Transported to
CC pigmented melanosomes by the BLOC-1 complex. Proper trafficking to
CC melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
CC {ECO:0000250|UniProtKB:P07147}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC -!- CAUTION: The precise function of this protein in melanin biosynthesis
CC is still under debate. DHICA oxidase activity is controversial. The
CC mouse protein has been shown to have DHICA oxidase activity (By
CC similarity). In contrast, the human protein was shown lack DHICA
CC oxidase activity, or to have DHICA oxidase activity only in the
CC presence of Cu(2+), but not with Zn(2+) (By similarity).
CC {ECO:0000250|UniProtKB:P07147, ECO:0000250|UniProtKB:P17643,
CC ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S71755; AAC60750.1; -; mRNA.
DR PIR; I51245; I51245.
DR AlphaFoldDB; P55028; -.
DR SMR; P55028; -.
DR UniPathway; UPA00785; -.
DR Proteomes; UP000515129; Genome assembly.
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; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
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; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..522
FT /note="5,6-dihydroxyindole-2-carboxylic acid oxidase"
FT /id="PRO_0000035887"
FT TOPO_DOM 22..470
FT /note="Lumenal, melanosome"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..38
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 39..59
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 50..89
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 91..100
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 103..112
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 248..251
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 280..293
FT /evidence="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
