TYRP1_CHICK
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 03-AUG-2022, entry version 129.
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; Phasianidae;
OC 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-related
RT protein-1.";
RL Biochim. Biophys. Acta 1395:7-12(1998).
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 -!- SUBUNIT: Tyrosinase, TYRP1 and TYRP2 may form a multienzyme complex.
CC {ECO:0000250}.
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}.
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DR EMBL; AF003631; AAC00213.1; -; mRNA.
DR AlphaFoldDB; O57405; -.
DR SMR; O57405; -.
DR STRING; 9031.ENSGALP00000037537; -.
DR PaxDb; O57405; -.
DR VEuPathDB; HostDB:geneid_395913; -.
DR eggNOG; ENOG502QRNA; Eukaryota.
DR InParanoid; O57405; -.
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:0042438; P:melanin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030318; P:melanocyte differentiation; IBA:GO_Central.
DR GO; GO:0032438; P:melanosome organization; IBA:GO_Central.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..535
FT /note="5,6-dihydroxyindole-2-carboxylic acid oxidase"
FT /id="PRO_0000035891"
FT TOPO_DOM 24..478
FT /note="Lumenal, melanosome"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 191
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 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 380
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT BINDING 403
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..40
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 41..64
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 55..98
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 100..109
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 112..121
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 257..260
FT /evidence="ECO:0000250|UniProtKB:P17643"
FT DISULFID 289..302
FT /evidence="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
