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UniProtKB/Swiss-Prot entry Q9BDE0

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TYRO_GORGO
Primary accession number Q9BDE0
Secondary accession numbers Q2KP17 Q9GLU5 Q9GLU6
Integrated into Swiss-Prot on June 7, 2004
Sequence was last modified on June 7, 2004 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 43)
Name and origin of the protein
Protein name Tyrosinase [Precursor]
Synonyms EC 1.14.18.1
Monophenol monooxygenase
Gene name
Name: TYR
From
Gorilla gorilla gorilla (Lowland gorilla) [TaxID: 9595] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Gorilla.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN ALBINISM.
STRAIN=Isolate Machinda, Isolate Ndengue, and Isolate Snowflake;
TISSUE=Blood;
PubMed=11153699 [NCBI, ExPASy, EBI, Israel, Japan]
Martinez-Arias R., Comas D., Andres A., Abello M.-T., Domingo-Roura X., Bertranpetit J.;
"The tyrosinase gene in gorillas and the albinism of 'Snowflake'.";
Pigment Cell Res. 13:467-470(2000).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate Snowflake, and Isolate Urko;
Roy R., Cantero M., Montoliu L.;
"Analysis of 5' upstream regulatory sequences and LCR-like region of the Gorilla tyrosinase locus.";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-388 AND 396-529.
Ding B., Ryder O.A., Shi P., Zhang Y.-P.;
"Molecular evolution of tyrosinase gene in primates.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
Comments
  • FUNCTION: 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 ACTIVITY: L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.
  • COFACTOR: Binds 2 copper ions per subunit (By similarity).
  • SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane protein (By similarity).
  • DISEASE: 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'.
  • SIMILARITY: Belongs to the tyrosinase family.
  • WEB RESOURCE: Name=Protein Spotlight; Note=Snowy stardom - Issue 49 of August 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt049.shtml";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF237806; AAK00804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237802; AAK00804.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237803; AAK00804.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237804; AAK00804.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237805; AAK00804.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237796; AAK00802.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237792; AAK00802.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237793; AAK00802.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237794; AAK00802.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237795; AAK00802.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237801; AAK00803.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237797; AAK00803.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237798; AAK00803.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237799; AAK00803.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237800; AAK00803.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874469; AAX82902.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874465; AAX82902.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874466; AAX82902.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874468; AAX82902.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874467; AAX82902.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874464; AAX82905.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874460; AAX82905.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874462; AAX82905.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874463; AAX82905.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY874461; AAX82905.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF183601; AAG27271.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF183599; AAG27271.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF183600; AAG27271.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF183603; AAG27272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF183602; AAG27272.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q9BDE0.
Ontologies
GO
GO:0042470; Cellular component: melanosome (inferred from sequence or structural similarity from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from sequence or structural similarity from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR008922; Di-copper_centre.
IPR002227; Tyrosinase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.1280.10; Di-copper_centre; 1.
Pfam PF00264; Tyrosinase; 1.
Pfam graphical view of domain structure.
PRINTS PR00092; TYROSINASE.
PROSITE PS00497; TYROSINASE_1; 1.
PS00498; TYROSINASE_2; 1.
BLOCKS Q9BDE0.
Phylogenomic databases
HOVERGEN Q9BDE0; -.
Other
ProtoNet Q9BDE0.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Albinism; Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18     Potential. 
CHAIN   19   529  511     Tyrosinase. PRO_0000035878
TOPO_DOM   19   476  458     Lumenal, melanosome (Potential). 
TRANSMEM   477   497  21     Potential. 
TOPO_DOM   498   529  32     Cytoplasmic (Potential). 
METAL   180   180        Copper A (By similarity). 
METAL   202   202        Copper A (By similarity). 
METAL   211   211        Copper A (By similarity). 
METAL   363   363        Copper B (By similarity). 
METAL   367   367        Copper B (By similarity). 
METAL   390   390        Copper B (By similarity). 
CARBOHYD   86    86        N-linked (GlcNAc...) (Potential). 
CARBOHYD   111   111        N-linked (GlcNAc...) (Potential). 
CARBOHYD   161   161        N-linked (GlcNAc...) (Potential). 
CARBOHYD   230   230        N-linked (GlcNAc...) (Potential). 
CARBOHYD   337   337        N-linked (GlcNAc...) (Potential). 
CARBOHYD   371   371        N-linked (GlcNAc...) (Potential). 
CONFLICT   5     5        V -> A (in Ref. 3; AAG27271). 
CONFLICT   5     5        V -> I (in Ref. 2; AAX82902/AAX82905). 
Sequence information
Length: 529 AA [This is the length of the unprocessed precursor] Molecular weight: 60365 Da [This is the MW of the unprocessed precursor] CRC64: D1C574D63DFF8EBC [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLLAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDRSPCGQLS GRGSCQNILL 

        70         80         90        100        110        120 
SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFWGP NCTERRLLVR 

       130        140        150        160        170        180 
RNIFDLSAPE KDKFFAYLTL AKHTISSDYV IPIGTYGQMK NGSTPMFNDI NIYDLFVWMH 

       190        200        210        220        230        240 
YYVSMDALLG GSEIWRDIDF AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD 

       250        260        270        280        290        300 
AEKCDICTDE YMGGQHPTNP NLLSPASFFS SWQIVCSRLE EYNSHQSLCN GTPEGPLQRN 

       310        320        330        340        350        360 
PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP LTGIADASQS 

       370        380        390        400        410        420 
SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLQEV YPEANAPIGH 

       430        440        450        460        470        480 
NRESYMVPFI PLYRNGDFFI SSKDLGYDYS YLQDSDPDSF QDYIKSYLEQ ASRIWSWLLG 

       490        500        510        520 
AAMVGAVLTA LLAGLVSLLC RHKRKQLPEE KQPLLMEKED YHSLYQSHL
Q9BDE0 in FASTA format

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View entry in raw text format (no links)
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