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P11344 (TYRO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosinase

EC=1.14.18.1
Alternative name(s):
Albino locus protein
Monophenol monooxygenase
Gene names
Name:Tyr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Catalytic activity

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

L-tyrosine + O2 = dopaquinone + H2O.

Cofactor

Binds 2 copper ions per subunit.

Subcellular location

Melanosome membrane; Single-pass type I membrane protein.

Involvement in disease

Defects in Tyr result in various forms of albinism. Himalayan strain tyrosinase is temperature-sensitive.

Sequence similarities

Belongs to the tyrosinase family.

Sequence caution

The sequence BAA00079.1 differs from that shown. Reason:

Ontologies

Keywords
   Biological processMelanin biosynthesis
   Cellular componentMembrane
   DiseaseAlbinism
Disease mutation
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from mutant phenotype PubMed 9548375. Source: MGI

melanin biosynthetic process

Inferred from mutant phenotype PubMed 7665913PubMed 9548375. Source: MGI

pigmentation

Inferred from mutant phenotype PubMed 13880466PubMed 17247639PubMed 9548375. Source: MGI

thymus development

Inferred from mutant phenotype PubMed 10890980. Source: MGI

   Cellular_componentintegral component of membrane

Traceable author statement PubMed 9918801. Source: UniProtKB

melanosome

Inferred from direct assay PubMed 9918801. Source: UniProtKB

melanosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: Ensembl

monophenol monooxygenase activity

Traceable author statement PubMed 9918801. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9918801. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 9918801. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 9918801. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Tyrp1P071472EBI-821603,EBI-821614

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 533515Tyrosinase
PRO_0000035880

Regions

Topological domain19 – 476458Lumenal, melanosome Potential
Transmembrane477 – 49721Helical; Potential
Topological domain498 – 53336Cytoplasmic Potential
Compositional bias503 – 5086Poly-Lys

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

Natural variations

Natural variant1031C → S in albino mice. Ref.2 Ref.7 Ref.8
Natural variant4201H → R in strain: Himalayan. Ref.4
Natural variant4821A → T in chinchilla mice. Ref.9

Experimental info

Sequence conflict401M → I in AAA37806. Ref.4
Sequence conflict1971D → Q in AAA37806. Ref.4
Sequence conflict2641S → I in CAA31273. Ref.3
Sequence conflict3461G → V in AAA40516. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11344 [UniParc].

Last modified May 29, 2007. Version 3.
Checksum: A4C109A97CBD5D6A

FASTA53360,606
        10         20         30         40         50         60 
MFLAVLYCLL WSFQISDGHF PRACASSKNL LAKECCPPWM GDGSPCGQLS GRGSCQDILL 

        70         80         90        100        110        120 
SSAPSGPQFP FKGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFGGP NCTEKRVLIR 

       130        140        150        160        170        180 
RNIFDLSVSE KNKFFSYLTL AKHTISSVYV IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH 

       190        200        210        220        230        240 
YYVSRDTLLG GSEIWRDIDF AHEAPGFLPW HRLFLLLWEQ EIRELTGDEN FTVPYWDWRD 

       250        260        270        280        290        300 
AENCDICTDE YLGGRHPENP NLLSPASFFS SWQIICSRSE EYNSHQVLCD GTPEGPLLRN 

       310        320        330        340        350        360 
PGNHDKAKTP RLPSSADVEF CLSLTQYESG SMDRTANFSF RNTLEGFASP LTGIADPSQS 

       370        380        390        400        410        420 
SMHNALHIFM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLLEV YPEANAPIGH 

       430        440        450        460        470        480 
NRDSYMVPFI PLYRNGDFFI TSKDLGYDYS YLQESDPGFY RNYIEPYLEQ ASRIWPWLLG 

       490        500        510        520        530 
AALVGAVIAA ALSGLSSRLC LQKKKKKKQP QEERQPLLMD KDDYHSLLYQ SHL 

« Hide

References

[1]"Cloning and sequencing of mouse tyrosinase cDNA."
Yamamoto H., Takeuchi S., Kudo T., Makino K., Nakata A., Shinoda T., Takeuchi T.
Jpn. J. Genet. 62:271-274(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[2]"Sequence analysis of mouse tyrosinase cDNA and the effect of melanotropin on its gene expression."
Kwon B.S., Wakulchik M., Haq A.K., Halaban R., Kestler D.
Biochem. Biophys. Res. Commun. 153:1301-1309(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-103.
Strain: DBA/2J.
[3]"Functional analysis of alternatively spliced tyrosinase gene transcripts."
Mueller G., Ruppert S., Schmid E., Schuetz G.
EMBO J. 7:2723-2730(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Molecular basis of mouse Himalayan mutation."
Kwon B.S., Halaban R., Chintamaneni C.
Biochem. Biophys. Res. Commun. 161:252-260(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-420.
Strain: Himalayan.
[5]"Isolation and characterization of variant cDNAs encoding mouse tyrosinase."
Terao M., Tabe L., Garattini E., Sartori D., Studer M., Mintz B.
Biochem. Biophys. Res. Commun. 159:848-853(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Melanin production in cultured albino melanocytes transfected with mouse tyrosinase cDNA."
Yamamoto H., Takeuchi S., Kudo T., Sato C., Takeuchi T.
Jpn. J. Genet. 64:121-135(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.
[7]"Isolation, chromosomal mapping, and expression of the mouse tyrosinase gene."
Kwon B.S., Haq A.K., Wakulchik M., Kestler D., Barton D.E., Francke U., Lamoreux M.L., Whitney J.B. III, Halaban R.
J. Invest. Dermatol. 93:589-594(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-273, VARIANT ALBINO SER-103.
Strain: BALB/c.
[8]"A point mutation in the tyrosinase gene of BALB/c albino mouse causing the cysteine-->serine substitution at position 85."
Shibahara S., Okinaga S., Tomita Y., Takeda A., Yamamoto H., Sato M., Takeuchi T.
Eur. J. Biochem. 189:455-461(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13, VARIANT ALBINO SER-103.
Strain: BALB/c.
[9]"Rescue of the albino phenotype by introduction of a functional tyrosinase gene into mice."
Beermann F., Ruppert S., Hummler E., Bosch F.X., Mueller G., Ruether U., Schuetz G.
EMBO J. 9:2819-2826(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CHINCHILLA MICE THR-482.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00440 mRNA. Translation: BAA00341.1.
D00131 mRNA. Translation: BAA00079.1. Sequence problems.
M20234 mRNA. Translation: AAA40516.1.
X12782 mRNA. Translation: CAA31273.1.
M26729 mRNA. Translation: AAA37806.1.
M24560 mRNA. Translation: AAA40517.1.
D00439 Genomic DNA. Translation: BAA00340.1.
X51743 Genomic DNA. Translation: CAA36033.1.
CCDSCCDS52304.1.
PIRYRMSCS. A27711.
RefSeqNP_035791.1. NM_011661.4.
UniGeneMm.238127.

3D structure databases

ProteinModelPortalP11344.
SMRP11344. Positions 172-449.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204394. 7 interactions.
IntActP11344. 1 interaction.

Chemistry

BindingDBP11344.
ChEMBLCHEMBL5346.

PTM databases

PhosphoSiteP11344.

Proteomic databases

PRIDEP11344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000004770; ENSMUSP00000004770; ENSMUSG00000004651.
GeneID22173.
KEGGmmu:22173.
UCSCuc009ifo.1. mouse.

Organism-specific databases

CTD7299.
MGIMGI:98880. Tyr.

Phylogenomic databases

eggNOGNOG08919.
HOGENOMHOG000118376.
HOVERGENHBG003553.
InParanoidP11344.
KOK00505.
OMACLSLTQY.
OrthoDBEOG7TJ3HG.
PhylomeDBP11344.
TreeFamTF315865.

Gene expression databases

BgeeP11344.
CleanExMM_TYR.
GenevestigatorP11344.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. SSF48056. 2 hits.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio302123.
PROP11344.
SOURCESearch...

Entry information

Entry nameTYRO_MOUSE
AccessionPrimary (citable) accession number: P11344
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 148 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot