TYRO_GORGO
ID TYRO_GORGO Reviewed; 529 AA.
AC Q9BDE0; Q2KP17; Q9GLU5; Q9GLU6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Tyrosinase;
DE EC=1.14.18.1;
DE AltName: Full=Monophenol monooxygenase;
DE Flags: Precursor;
GN Name=TYR;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN ALBINISM.
RC STRAIN=Isolate Machinda, Isolate Ndengue, and Isolate Snowflake;
RC TISSUE=Blood;
RX PubMed=11153699; DOI=10.1034/j.1600-0749.2000.130609.x;
RA Martinez-Arias R., Comas D., Andres A., Abello M.-T., Domingo-Roura X.,
RA Bertranpetit J.;
RT "The tyrosinase gene in gorillas and the albinism of 'Snowflake'.";
RL Pigment Cell Res. 13:467-470(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Snowflake, and Isolate Urko;
RA Roy R., Cantero M., Montoliu L.;
RT "Analysis of 5' upstream regulatory sequences and LCR-like region of the
RT Gorilla tyrosinase locus.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-388 AND 396-529.
RA Ding B., Ryder O.A., Shi P., Zhang Y.-P.;
RT "Molecular evolution of tyrosinase gene in primates.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC formation of pigments such as melanins and other polyphenolic compounds
CC (By similarity). Catalyzes the initial and rate limiting step in the
CC cascade of reactions leading to melanin production from tyrosine (By
CC similarity). In addition to hydroxylating tyrosine to DOPA (3,4-
CC dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-
CC quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to
CC indole-5,6 quinone (By similarity). {ECO:0000250|UniProtKB:P11344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504,
CC ChEBI:CHEBI:57924; EC=1.14.18.1;
CC Evidence={ECO:0000250|UniProtKB:P11344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924,
CC ChEBI:CHEBI:58315; EC=1.14.18.1;
CC Evidence={ECO:0000250|UniProtKB:P11344};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19};
CC -!- SUBUNIT: Forms an OPN3-dependent complex with DCT in response to blue
CC light in melanocytes. {ECO:0000250|UniProtKB:P14679}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane
CC {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P14679}. Melanosome
CC {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to melanosome
CC is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
CC {ECO:0000250|UniProtKB:P11344}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P11344}.
CC -!- DISEASE: Note=Defects in TYR are the cause of oculocutaneous albinism
CC (OCA). The only known albino gorilla, called Floquet de Neu
CC ('Snowflake') had white hair, pink skin and blue eyes (zoologic park of
CC Barcelona, 1964-2003). No differences were found at the amino-acid
CC level but the activity of this enzyme was lacking in 'Snowflake'.
CC {ECO:0000269|PubMed:11153699}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Snowy stardom - Issue 49 of
CC August 2004;
CC URL="https://web.expasy.org/spotlight/back_issues/049";
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DR EMBL; AF237806; AAK00804.1; -; Genomic_DNA.
DR EMBL; AF237802; AAK00804.1; JOINED; Genomic_DNA.
DR EMBL; AF237803; AAK00804.1; JOINED; Genomic_DNA.
DR EMBL; AF237804; AAK00804.1; JOINED; Genomic_DNA.
DR EMBL; AF237805; AAK00804.1; JOINED; Genomic_DNA.
DR EMBL; AF237796; AAK00802.1; -; Genomic_DNA.
DR EMBL; AF237792; AAK00802.1; JOINED; Genomic_DNA.
DR EMBL; AF237793; AAK00802.1; JOINED; Genomic_DNA.
DR EMBL; AF237794; AAK00802.1; JOINED; Genomic_DNA.
DR EMBL; AF237795; AAK00802.1; JOINED; Genomic_DNA.
DR EMBL; AF237801; AAK00803.1; -; Genomic_DNA.
DR EMBL; AF237797; AAK00803.1; JOINED; Genomic_DNA.
DR EMBL; AF237798; AAK00803.1; JOINED; Genomic_DNA.
DR EMBL; AF237799; AAK00803.1; JOINED; Genomic_DNA.
DR EMBL; AF237800; AAK00803.1; JOINED; Genomic_DNA.
DR EMBL; AY874469; AAX82902.1; -; Genomic_DNA.
DR EMBL; AY874465; AAX82902.1; JOINED; Genomic_DNA.
DR EMBL; AY874466; AAX82902.1; JOINED; Genomic_DNA.
DR EMBL; AY874468; AAX82902.1; JOINED; Genomic_DNA.
DR EMBL; AY874467; AAX82902.1; JOINED; Genomic_DNA.
DR EMBL; AY874464; AAX82905.1; -; Genomic_DNA.
DR EMBL; AY874460; AAX82905.1; JOINED; Genomic_DNA.
DR EMBL; AY874462; AAX82905.1; JOINED; Genomic_DNA.
DR EMBL; AY874463; AAX82905.1; JOINED; Genomic_DNA.
DR EMBL; AY874461; AAX82905.1; JOINED; Genomic_DNA.
DR EMBL; AF183601; AAG27271.1; -; Genomic_DNA.
DR EMBL; AF183599; AAG27271.1; JOINED; Genomic_DNA.
DR EMBL; AF183600; AAG27271.1; JOINED; Genomic_DNA.
DR EMBL; AF183603; AAG27272.1; -; Genomic_DNA.
DR EMBL; AF183602; AAG27272.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q9BDE0; -.
DR SMR; Q9BDE0; -.
DR STRING; 9593.ENSGGOP00000008910; -.
DR eggNOG; ENOG502QRET; Eukaryota.
DR InParanoid; Q9BDE0; -.
DR Proteomes; UP000001519; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004503; F:tyrosinase activity; IBA:GO_Central.
DR GO; GO:0042438; P:melanin biosynthetic process; IBA:GO_Central.
DR GO; GO:0043473; P:pigmentation; IBA:GO_Central.
DR GO; GO:0009637; P:response to blue light; ISS:UniProtKB.
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 3: Inferred from homology;
KW Albinism; Copper; Glycoprotein; Melanin biosynthesis; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..529
FT /note="Tyrosinase"
FT /id="PRO_0000035878"
FT TOPO_DOM 19..476
FT /note="Lumenal, melanosome"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 287..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 202
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 363
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 367
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 390
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="V -> A (in Ref. 3; AAG27271)"
FT /evidence="ECO:0000305"
FT CONFLICT 5
FT /note="V -> I (in Ref. 2; AAX82902/AAX82905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 60365 MW; D1C574D63DFF8EBC CRC64;
MLLAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDRSPCGQLS GRGSCQNILL
SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFWGP NCTERRLLVR
RNIFDLSAPE KDKFFAYLTL AKHTISSDYV IPIGTYGQMK NGSTPMFNDI NIYDLFVWMH
YYVSMDALLG GSEIWRDIDF AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD
AEKCDICTDE YMGGQHPTNP NLLSPASFFS SWQIVCSRLE EYNSHQSLCN GTPEGPLQRN
PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP LTGIADASQS
SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLQEV YPEANAPIGH
NRESYMVPFI PLYRNGDFFI SSKDLGYDYS YLQDSDPDSF QDYIKSYLEQ ASRIWSWLLG
AAMVGAVLTA LLAGLVSLLC RHKRKQLPEE KQPLLMEKED YHSLYQSHL
