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Q8MIU0 (TYRO_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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 By similarity.

Catalytic activity

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

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit By similarity.

Subcellular location

Melanosome membrane; Single-pass type I membrane protein By similarity.

Involvement in disease

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

Sequence similarities

Belongs to the tyrosinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 530513Tyrosinase
PRO_0000035876

Regions

Topological domain19 – 473455Lumenal, melanosome Potential
Transmembrane474 – 49421Helical; Potential
Topological domain495 – 53036Cytoplasmic 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
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1721V → A in AAL38168. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8MIU0 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: 1C0CEF3D8CB1356C

FASTA53060,304
        10         20         30         40         50         60 
MLLAALYCLL WSFRTSAGHF PRACASSKSL TEKECCPPWA GDGSPCGRLS GRGSCQDVIL 

        70         80         90        100        110        120 
STAPLGPQFP FTGVDDRESW PSIFYNRTCQ CFSNFMGFNC GSCKFGFRGP RCTERRLLVR 

       130        140        150        160        170        180 
RNIFDLSVPE KNKFLAYLTL AKHTTSPDYV IPTGTYGQMN HGTTPLFNDV SVYDLFVWMH 

       190        200        210        220        230        240 
YYVSRDTLLG DSEVWRDIDF AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD 

       250        260        270        280        290        300 
AENCDVCTDE YMGGRNPANP NLLSPASFFS SWQIVCSRLE EYNSRQALCN GTSEGPLLRN 

       310        320        330        340        350        360 
PGNHDKARTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFADP VTGIADASQS 

       370        380        390        400        410        420 
SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW LRKYHPLQDV YPEANAPIGH 

       430        440        450        460        470        480 
NRESYMVPFI PLYRNGDFFI SSKDXGYDYS YLQDSEPDIF QDYIKPYLEQ AQRIWPWLIG 

       490        500        510        520        530 
AAVVGSVLTA VLGGLTSLLC RRKRNQLPEE KQPLLMEKED YHNLMYQSHL

« Hide

References

[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.

Web resources

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY046527 mRNA. Translation: AAL02331.2.
AF445639 mRNA. Translation: AAL38168.1.
IPIIPI00689730.
RefSeqNP_851344.1. NM_181001.3.
UniGeneBt.9028.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID280951.
KEGGbta:280951.

Organism-specific databases

CTD7299.

Phylogenomic databases

eggNOGNOG08919.
HOGENOMHOG000118376.
HOVERGENHBG003553.
InParanoidQ8MIU0.
KOK00505.
OrthoDBEOG4D26PK.

Enzyme and pathway databases

SABIO-RKQ8MIU0.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. Di-copper_centre. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805063.

Entry information

Entry nameTYRO_BOVIN
AccessionPrimary (citable) accession number: Q8MIU0
Secondary accession number(s): Q8WN56
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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