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Protein

Tyrosinase

Gene

TYR

Organism
Gorilla gorilla gorilla (Western lowland gorilla)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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.

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

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosinase (EC:1.14.18.1)
Alternative name(s):
Monophenol monooxygenase
Gene namesi
Name:TYR
OrganismiGorilla gorilla gorilla (Western lowland gorilla)
Taxonomic identifieri9595 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeGorilla
ProteomesiUP000001519 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 476458Lumenal, melanosomeSequence AnalysisAdd
BLAST
Transmembranei477 – 49721HelicalSequence AnalysisAdd
BLAST
Topological domaini498 – 52932CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Defects in TYR are the cause of oculocutaneous albinism (OCA). The only known albino gorilla, called Floquet de Neu ('Snowflake') had white hair, pink skin and blue eyes (zoologic park of Barcelona, 1964-2003). No differences were found at the amino-acid level but the activity of this enzyme was lacking in 'Snowflake'.

Keywords - Diseasei

Albinism

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 529511TyrosinasePRO_0000035878Add
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

ProteinModelPortaliQ9BDE0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG003553.
InParanoidiQ9BDE0.

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.

Q9BDE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDRSPCGQLS
60 70 80 90 100
GRGSCQNILL SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFNC
110 120 130 140 150
GNCKFGFWGP NCTERRLLVR RNIFDLSAPE KDKFFAYLTL AKHTISSDYV
160 170 180 190 200
IPIGTYGQMK NGSTPMFNDI NIYDLFVWMH YYVSMDALLG GSEIWRDIDF
210 220 230 240 250
AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD AEKCDICTDE
260 270 280 290 300
YMGGQHPTNP NLLSPASFFS SWQIVCSRLE EYNSHQSLCN GTPEGPLQRN
310 320 330 340 350
PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP
360 370 380 390 400
LTGIADASQS SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW
410 420 430 440 450
LRRHRPLQEV YPEANAPIGH NRESYMVPFI PLYRNGDFFI SSKDLGYDYS
460 470 480 490 500
YLQDSDPDSF QDYIKSYLEQ ASRIWSWLLG AAMVGAVLTA LLAGLVSLLC
510 520
RHKRKQLPEE KQPLLMEKED YHSLYQSHL
Length:529
Mass (Da):60,365
Last modified:June 7, 2004 - v2
Checksum:iD1C574D63DFF8EBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51V → A in AAG27271 (Ref. 3) Curated
Sequence conflicti5 – 51V → I in AAX82902 (Ref. 2) Curated
Sequence conflicti5 – 51V → I in AAX82905 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237806
, AF237802, AF237803, AF237804, AF237805 Genomic DNA. Translation: AAK00804.1.
AF237796
, AF237792, AF237793, AF237794, AF237795 Genomic DNA. Translation: AAK00802.1.
AF237801
, AF237797, AF237798, AF237799, AF237800 Genomic DNA. Translation: AAK00803.1.
AY874469
, AY874465, AY874466, AY874468, AY874467 Genomic DNA. Translation: AAX82902.1.
AY874464
, AY874460, AY874462, AY874463, AY874461 Genomic DNA. Translation: AAX82905.1.
AF183601, AF183599, AF183600 Genomic DNA. Translation: AAG27271.1.
AF183603, AF183602 Genomic DNA. Translation: AAG27272.1.

Cross-referencesi

Web resourcesi

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF237806
, AF237802, AF237803, AF237804, AF237805 Genomic DNA. Translation: AAK00804.1.
AF237796
, AF237792, AF237793, AF237794, AF237795 Genomic DNA. Translation: AAK00802.1.
AF237801
, AF237797, AF237798, AF237799, AF237800 Genomic DNA. Translation: AAK00803.1.
AY874469
, AY874465, AY874466, AY874468, AY874467 Genomic DNA. Translation: AAX82902.1.
AY874464
, AY874460, AY874462, AY874463, AY874461 Genomic DNA. Translation: AAX82905.1.
AF183601, AF183599, AF183600 Genomic DNA. Translation: AAG27271.1.
AF183603, AF183602 Genomic DNA. Translation: AAG27272.1.

3D structure databases

ProteinModelPortaliQ9BDE0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG003553.
InParanoidiQ9BDE0.

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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN ALBINISM.
    Strain: Isolate Machinda, Isolate Ndengue and Isolate Snowflake.
    Tissue: Blood.
  2. "Analysis of 5' upstream regulatory sequences and LCR-like region of the Gorilla tyrosinase locus."
    Roy R., Cantero M., Montoliu L.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Isolate Snowflake and Isolate Urko.
  3. "Molecular evolution of tyrosinase gene in primates."
    Ding B., Ryder O.A., Shi P., Zhang Y.-P.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-388 AND 396-529.

Entry informationi

Entry nameiTYRO_GORGO
AccessioniPrimary (citable) accession number: Q9BDE0
Secondary accession number(s): Q2KP17, Q9GLU5, Q9GLU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: February 4, 2015
This is version 75 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.