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Protein

Tyrosinase

Gene

TYR

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone (By similarity).By similarity

Catalytic activityi

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
L-tyrosine + O2 = dopaquinone + H2O.

Cofactori

Cu2+By similarityNote: Binds 2 copper ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi180 – 1801Copper ABy similarity
Metal bindingi202 – 2021Copper ABy similarity
Metal bindingi211 – 2111Copper ABy similarity
Metal bindingi363 – 3631Copper BBy similarity
Metal bindingi367 – 3671Copper BBy similarity
Metal bindingi390 – 3901Copper BBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosinase (EC:1.14.18.1)
Alternative name(s):
Monophenol monooxygenase
Gene namesi
Name:TYR
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 473455Lumenal, melanosomeSequence AnalysisAdd
BLAST
Transmembranei474 – 49421HelicalSequence AnalysisAdd
BLAST
Topological domaini495 – 53036CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. melanosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 530512TyrosinasePRO_0000035877Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP54834.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG08919.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiP54834.
KOiK00505.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P54834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLAALCCLL WSFRTSTGHF PRACASSKSL MEKECCPPWS GDGSPCGQLS
60 70 80 90 100
GRGACQDIIL SNAPFGPQFP FTGVDDRESW PSVFYNRTCQ CFGNFMGFNC
110 120 130 140 150
GNCKFGFWGQ NCTEKRLLVR KNIFDLSVPE KNKFLAYLTL AKHTTSPDYV
160 170 180 190 200
IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH YYVSRDTLLG GSEIWKDIDF
210 220 230 240 250
AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD AKSCDICTDE
260 270 280 290 300
YMGGRNPANP NLLSPASFFS SWQIVCTRLE EYNSRQALCD GTPEGPLLRN
310 320 330 340 350
PGNHDKARTP RLPSSADVEF CLSLTQYESD SMDKAANFSF RNTLEGFASP
360 370 380 390 400
LTGIADASQS SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW
410 420 430 440 450
LRRHHPLREV YPEANAPIGH NRESYMVPFI PLYRNGDLFI SSRDLGYDYS
460 470 480 490 500
NLQESERDIF QDYIKPYLEQ ASRIWPWLIG AAVVGCVVTA VLGGLTSLLC
510 520 530
RRNRKQLHEE KQPLLMEKED YHSLLYQTHL
Length:530
Mass (Da):60,336
Last modified:April 11, 2005 - v2
Checksum:iB1C45F6362ACF0E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31L → V in AAA86420 (Ref. 2) Curated
Sequence conflicti7 – 71C → R in AAA86420 (Ref. 2) Curated
Sequence conflicti59 – 591I → V in AAA86420 (Ref. 2) Curated
Sequence conflicti115 – 1151K → R in AAA86420 (Ref. 2) Curated
Sequence conflicti132 – 1321N → D in AAA86420 (Ref. 2) Curated
Sequence conflicti212 – 2121R → T in AAA86420 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY336053 mRNA. Translation: AAQ17535.1.
U42219 Genomic DNA. Translation: AAA86420.1.
RefSeqiNP_001002941.1. NM_001002941.1.
UniGeneiCfa.104.

Genome annotation databases

GeneIDi403405.
KEGGicfa:403405.

Cross-referencesi

Web resourcesi

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY336053 mRNA. Translation: AAQ17535.1.
U42219 Genomic DNA. Translation: AAA86420.1.
RefSeqiNP_001002941.1. NM_001002941.1.
UniGeneiCfa.104.

3D structure databases

ProteinModelPortaliP54834.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403405.
KEGGicfa:403405.

Organism-specific databases

CTDi7299.

Phylogenomic databases

eggNOGiNOG08919.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiP54834.
KOiK00505.

Miscellaneous databases

NextBioi20816926.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Schmutz S.M., Berryere T.G.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Doberman pinscher.
    Tissue: Skin.
  2. "Cloning and chromosomal in situ hybridization of the dog tyrosinase exon 1."
    Tang Q., Williams R.W., Hogan D., Valentine V., Goldowitz D.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.

Entry informationi

Entry nameiTYRO_CANFA
AccessioniPrimary (citable) accession number: P54834
Secondary accession number(s): Q7YRB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: April 11, 2005
Last modified: January 6, 2015
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.