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Database: UniProt
Entry: O57405
LinkDB: O57405
Original site: O57405 
ID   TYRP1_CHICK             Reviewed;         535 AA.
AC   O57405;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   16-JAN-2019, entry version 116.
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 {ECO:0000303|PubMed:9434144};
DE            Short=TRP-1 {ECO:0000303|PubMed:9434144};
DE            Short=TRP1;
DE   Flags: Precursor;
GN   Name=TYRP1;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Black Australorp X New Hampshire red; TISSUE=Neural crest;
RX   PubMed=9434144; DOI=10.1016/S0167-4781(97)00144-9;
RA   April C.S., Jackson I.J., Kidson S.H.;
RT   "The cloning and sequencing of a cDNA coding for chick tyrosinase-
RT   related protein-1.";
RL   Biochim. Biophys. Acta 1395:7-12(1998).
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   -!- SUBUNIT: Tyrosinase, TYRP1 and TYRP2 may form a multienzyme
CC       complex. {ECO:0000250}.
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; AF003631; AAC00213.1; -; mRNA.
DR   UniGene; Gga.541; -.
DR   ProteinModelPortal; O57405; -.
DR   SMR; O57405; -.
DR   STRING; 9031.ENSGALP00000037537; -.
DR   PaxDb; O57405; -.
DR   PRIDE; O57405; -.
DR   eggNOG; ENOG410IEEB; Eukaryota.
DR   eggNOG; ENOG410XSJD; LUCA.
DR   HOGENOM; HOG000118376; -.
DR   HOVERGEN; HBG003553; -.
DR   InParanoid; O57405; -.
DR   OrthoDB; 518234at2759; -.
DR   PhylomeDB; O57405; -.
DR   UniPathway; UPA00785; -.
DR   Proteomes; UP000000539; Unplaced.
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:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006582; P:melanin metabolic process; IBA:GO_Central.
DR   GO; GO:0030318; P:melanocyte differentiation; IBA:GO_Central.
DR   GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
DR   GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0097066; P:response to thyroid hormone; IBA:GO_Central.
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   Complete proteome; Copper; Disulfide bond; Glycoprotein;
KW   Melanin biosynthesis; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    535       5,6-dihydroxyindole-2-carboxylic acid
FT                                oxidase.
FT                                /FTId=PRO_0000035891.
FT   TOPO_DOM     24    478       Lumenal, melanosome. {ECO:0000255}.
FT   TRANSMEM    479    499       Helical. {ECO:0000255}.
FT   TOPO_DOM    500    535       Cytoplasmic. {ECO:0000255}.
FT   METAL       191    191       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       214    214       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       223    223       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       376    376       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       380    380       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       403    403       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   CARBOHYD     95     95       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    180    180       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    303    303       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    349    349       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    384    384       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     29     40       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID     41     64       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID     55     98       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID    100    109       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID    112    121       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID    257    260       {ECO:0000250|UniProtKB:P17643}.
FT   DISULFID    289    302       {ECO:0000250|UniProtKB:P17643}.
SQ   SEQUENCE   535 AA;  60595 MW;  96AA3EAB5AF1AC47 CRC64;
     MQLPMLLLVS LPLLLNMFKP AEAQFPRQCA TIESLRSGMC CPDYFPVFGP GSDQCGVSTG
     RGRCVQVTVD SRPHGPQYIH DGRDDREQWP IRFFNQTCRC NGNFSGYNCG SCRPGWTGPT
     CSQQINIVRR NLLDLSTEER RRFVNALHQA KVTIHPDIVI ATRRREEIFG PDGNTPQFEN
     ISIYNYFVWS HYYSVRKTFL GAGQQSFERV DFSHEGPAFV TWHRYHLLQL ERDMQNMLQD
     STFGLPYWNF ATGQNTCDIC SDDLMGARSN FDVSLISQNS IFSTWRVLCE SIEDYDSLGT
     ICNSTEGGPI RRNPAGNVAR PMVQRLPEPE DVPQCLEVGI FDTPPFYSNS TDSFRNTVEG
     YSDPSGKYDP AVRSLHNLAH LFLNGTGGQT HLSPNDPIFV LLHTFTDAVF DEWLRRYSAD
     ISTYPLENAP IGHNREYNMV PFWPPVTNNE MFVTAPENLG YSYDIEWPGP LRVTEMITIA
     IVTALVLVAI IFAAAACIVR AKKNRDELHQ PLLTDQYQHY SDDYDGIATP SQSVV
//
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