TYRO_FELCA
ID TYRO_FELCA Reviewed; 529 AA.
AC P55033; A0A0A0MQ28; Q2VPV8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tyrosinase;
DE EC=1.14.18.1;
DE AltName: Full=Monophenol monooxygenase;
DE Flags: Precursor;
GN Name=TYR;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-227 AND ARG-302.
RX PubMed=15858157; DOI=10.1093/jhered/esi066;
RA Schmidt-Kuntzel A., Eizirik E., O'Brien S.J., Menotti-Raymond M.;
RT "Tyrosinase and tyrosinase related protein 1 alleles specify domestic cat
RT coat color phenotypes of the albino and brown loci.";
RL J. Hered. 96:289-301(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian;
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 279-357.
RC STRAIN=European shorthair; TISSUE=Melanoma;
RX PubMed=9150543; DOI=10.1177/030098589703400105;
RA van der Linde-Sipman J.S., de Wit M.M., van Garderen E., Molenbeek R.F.,
RA van der Velde-Zimmermann D., de Weger R.A.;
RT "Cutaneous malignant melanomas in 57 cats: identification of (amelanotic)
RT signet-ring and balloon cell types and verification of their origin by
RT immunohistochemistry, electron microscopy, and in situ hybridization.";
RL Vet. Pathol. 34:31-38(1997).
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 -!- POLYMORPHISM: Allelic variations in TYR may be associated with coat
CC color phenotype in siamese and burmese cats. The coat color trait is
CC autosomal recessive. {ECO:0000269|PubMed:15858157}.
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; AH014863; AAY32311.1; -; Genomic_DNA.
DR EMBL; AANG04002890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U40716; AAB08729.1; -; mRNA.
DR RefSeq; XP_003992691.1; XM_003992642.3.
DR AlphaFoldDB; P55033; -.
DR SMR; P55033; -.
DR STRING; 9685.ENSFCAP00000020791; -.
DR Ensembl; ENSFCAT00000029640; ENSFCAP00000020791; ENSFCAG00000024128.
DR GeneID; 751100; -.
DR KEGG; fca:751100; -.
DR CTD; 7299; -.
DR VGNC; VGNC:66738; TYR.
DR eggNOG; ENOG502QRET; Eukaryota.
DR GeneTree; ENSGT00940000155336; -.
DR HOGENOM; CLU_038693_1_0_1; -.
DR OrthoDB; 881347at2759; -.
DR Proteomes; UP000011712; Chromosome D1.
DR Bgee; ENSFCAG00000024128; Expressed in eyeball of camera-type eye and 3 other tissues.
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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004503; F:tyrosinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0009637; P:response to blue light; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
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.
PE 2: Evidence at transcript level;
KW Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..529
FT /note="Tyrosinase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000452306"
FT TOPO_DOM 19..472
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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 362
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 366
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 389
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 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 227
FT /note="G -> W (may be associated with siamese coat color)"
FT /evidence="ECO:0000269|PubMed:15858157"
FT VARIANT 302
FT /note="G -> R (may be associated with burmese coat color)"
FT /evidence="ECO:0000269|PubMed:15858157"
FT CONFLICT 294
FT /note="R -> E (in Ref. 1; AAY32311 and 3; AAB08729)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="G -> GN (in Ref. 1; AAY32311 and 3; AAB08729)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 60391 MW; CB7EF8AFBF3C8952 CRC64;
MLLAALCCLL WSFRTSAGHF PRACASSKSL MEKECCPAWT GDSSPCGQLS GRGACQDITL
SKAPLGPQYP FTGMDDREAW PSVFYNRTCQ CFGNFMGFNC GNCKFGFWGP NCTEKRLLVR
RNIFDLSVPE KNKFLAYLTL AKHTISPDYV IPIGTYGQMN NGSTPMFNDI NVYDLFVWMH
YYVSRDTLLG GSEIWKDIDF AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD
AKSCDICTDE YMGGHNPANP NLLSPASFFS SWQIICTRLE EYNSRQALCD GTPRGPLLRN
PGHDKARTPR LPSSADVEFC LSLTQYESDS MDKAANFSFR NTLEGFASPL TGIADASQSS
MHNALHIYMN GTMSQVQGSA NDPIFLLHHA FVDSIFEQWL RRHHPLQEVY PEANAPIGHN
RESYMVPFIP LYRNGDFFIS SRDLGYDYSN LQDSERDIFQ DYIKPFLEQA SRIWPWLIGA
AVVGSVLTAV LGRLTSLLCR RKRKQLREER QPLLMEKEDY HSLLYQTHV
