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Protein

Tyrosinase

Gene

TYR

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

SABIO-RKQ8MIU0.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosinase (EC:1.14.18.1)
Alternative name(s):
Monophenol monooxygenase
Gene namesi
Name:TYR
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 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

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in TYR are the cause of a form of albinism in Braunvieh calf.

Keywords - Diseasei

Albinism

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 530513TyrosinasePRO_0000035876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi337 – 3371N-linked (GlcNAc...)Sequence Analysis
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ8MIU0.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG08919.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiQ8MIU0.
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.

Q8MIU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLAALYCLL WSFRTSAGHF PRACASSKSL TEKECCPPWA GDGSPCGRLS
60 70 80 90 100
GRGSCQDVIL STAPLGPQFP FTGVDDRESW PSIFYNRTCQ CFSNFMGFNC
110 120 130 140 150
GSCKFGFRGP RCTERRLLVR RNIFDLSVPE KNKFLAYLTL AKHTTSPDYV
160 170 180 190 200
IPTGTYGQMN HGTTPLFNDV SVYDLFVWMH YYVSRDTLLG DSEVWRDIDF
210 220 230 240 250
AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD AENCDVCTDE
260 270 280 290 300
YMGGRNPANP NLLSPASFFS SWQIVCSRLE EYNSRQALCN GTSEGPLLRN
310 320 330 340 350
PGNHDKARTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFADP
360 370 380 390 400
VTGIADASQS SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW
410 420 430 440 450
LRKYHPLQDV YPEANAPIGH NRESYMVPFI PLYRNGDFFI SSKDXGYDYS
460 470 480 490 500
YLQDSEPDIF QDYIKPYLEQ AQRIWPWLIG AAVVGSVLTA VLGGLTSLLC
510 520 530
RRKRNQLPEE KQPLLMEKED YHNLMYQSHL
Length:530
Mass (Da):60,304
Last modified:March 1, 2003 - v2
Checksum:i1C0CEF3D8CB1356C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721V → A in AAL38168 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046527 mRNA. Translation: AAL02331.2.
AF445639 mRNA. Translation: AAL38168.1.
RefSeqiNP_851344.1. NM_181001.3.
UniGeneiBt.9028.

Genome annotation databases

GeneIDi280951.
KEGGibta:280951.

Cross-referencesi

Web resourcesi

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY046527 mRNA. Translation: AAL02331.2.
AF445639 mRNA. Translation: AAL38168.1.
RefSeqiNP_851344.1. NM_181001.3.
UniGeneiBt.9028.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ8MIU0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280951.
KEGGibta:280951.

Organism-specific databases

CTDi7299.

Phylogenomic databases

eggNOGiNOG08919.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiQ8MIU0.
KOiK00505.

Enzyme and pathway databases

SABIO-RKQ8MIU0.

Miscellaneous databases

NextBioi20805063.

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. "A form of albinism in cattle is caused by a tyrosinase frameshift mutation."
    Schmutz S.M., Berryere T.G., Ciobanu D.C., Mileham A.J., Schmidtz B.H., Fredholm M.
    Mamm. Genome 15:62-67(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN ALBINISM.
    Strain: White Galloway.
  2. "Transcriptional regulation of bovine TYR gene."
    Guibert S., Julien R., Oulmouden A.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skin.

Entry informationi

Entry nameiTYRO_BOVIN
AccessioniPrimary (citable) accession number: Q8MIU0
Secondary accession number(s): Q8WN56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2003
Last modified: January 7, 2015
This is version 81 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.