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Reviewed, UniProtKB/Swiss-Prot Q9BDE0 (TYRO_GORGO)

Last modified July 22, 2008. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Tyrosinase
    EC=1.14.18.1
Alternative name(s):
    Monophenol monooxygenase
Gene names
Name: TYR
OrganismGorilla gorilla gorilla (Lowland gorilla)
Taxonomic identifier9595 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Gorilla

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Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (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 + O(2) = L-dopa + dopaquinone + H(2)O.

Cofactor

Binds 2 copper ions per subunit By similarity.

Subcellular location

Melanosome membrane; Single-pass type I membrane proteinBy similarity.

Involvement in 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'.

Sequence similarities

Belongs to the tyrosinase family.

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Ontologies

Keywords

   Biological processMelanin biosynthesis
   Cellular componentMembrane
   DiseaseAlbinism
   DomainSignal
Transmembrane
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMGlycoprotein

Gene Ontology (GO)

   Cellular componentmelanosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionprotein heterodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 529511Tyrosinase
PRO_0000035878

Regions

Topological domain19 – 476458Lumenal, melanosome Potential
Transmembrane477 – 49721 Potential
Topological domain498 – 52932Cytoplasmic Potential

Sites

Metal binding1801Copper A By similarity
Metal binding2021Copper A By similarity
Metal binding2111Copper A By similarity
Metal binding3631Copper B By similarity
Metal binding3671Copper B By similarity
Metal binding3901Copper B By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict51V → A in AAG27271. Ref.3
Sequence conflict51V → I in AAX82902 and AAX82905. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
Q9BDE0-1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: D1C574D63DFF8EBC

FASTA52960,365
        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

« Hide

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References

[1]"The tyrosinase gene in gorillas and the albinism of 'Snowflake'."
Martinez-Arias R., Comas D., Andres A., Abello M.-T., Domingo-Roura X., Bertranpetit J.
Pigment Cell Res. 13:467-470(2000) [PubMed: 11153699] [Abstract]
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.

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Web resources

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

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Cross-references

Sequence databases

AF237806 expand/collapse EMBL AC list , AF237802, AF237803, AF237804, AF237805 Genomic DNA. Translation: AAK00804.1.
AF237796 expand/collapse EMBL AC list , AF237792, AF237793, AF237794, AF237795 Genomic DNA. Translation: AAK00802.1.
AF237801 expand/collapse EMBL AC list , AF237797, AF237798, AF237799, AF237800 Genomic DNA. Translation: AAK00803.1.
AY874469 expand/collapse EMBL AC list , AY874465, AY874466, AY874468, AY874467 Genomic DNA. Translation: AAX82902.1.
AY874464 expand/collapse EMBL AC list , 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

ModBaseSearch...

Phylogenomic databases

HOVERGENQ9BDE0.

Family and domain databases

InterProIPR008922. Di-copper_centre.
IPR002227. Tyrosinase.
[Graphical view]
Gene3DG3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

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Entry information

Entry nameTYRO_GORGO
AccessionPrimary (citable) accession number: Q9BDE0
Secondary accession number(s): Q2KP17, Q9GLU5, Q9GLU6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 22, 2008
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents