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P11344

- TYRO_MOUSE

UniProt

P11344 - TYRO_MOUSE

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Protein

Tyrosinase

Gene

Tyr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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+Note: Binds 2 copper ions per subunit.

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

  1. copper ion binding Source: Ensembl
  2. monophenol monooxygenase activity Source: UniProtKB
  3. protein heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: MGI
  2. melanin biosynthetic process Source: MGI
  3. pigmentation Source: MGI
  4. thymus development Source: MGI
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):
Albino locus protein
Monophenol monooxygenase
Gene namesi
Name:Tyr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:98880. Tyr.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 476458Lumenal, melanosomeSequence AnalysisAdd
BLAST
Transmembranei477 – 49721HelicalSequence AnalysisAdd
BLAST
Topological domaini498 – 53336CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. melanosome Source: UniProtKB
  3. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Albinism, Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 533515TyrosinasePRO_0000035880Add
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

Proteomic databases

PRIDEiP11344.

PTM databases

PhosphoSiteiP11344.

Expressioni

Gene expression databases

BgeeiP11344.
CleanExiMM_TYR.
GenevestigatoriP11344.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Tyrp1P071472EBI-821603,EBI-821614

Protein-protein interaction databases

BioGridi204394. 7 interactions.
IntActiP11344. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP11344.
SMRiP11344. Positions 172-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi503 – 5086Poly-Lys

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG08919.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiP11344.
KOiK00505.
OMAiCLSLTQY.
OrthoDBiEOG7TJ3HG.
PhylomeDBiP11344.
TreeFamiTF315865.

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. 2 hits.
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.

P11344-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLAVLYCLL WSFQISDGHF PRACASSKNL LAKECCPPWM GDGSPCGQLS
60 70 80 90 100
GRGSCQDILL SSAPSGPQFP FKGVDDRESW PSVFYNRTCQ CSGNFMGFNC
110 120 130 140 150
GNCKFGFGGP NCTEKRVLIR RNIFDLSVSE KNKFFSYLTL AKHTISSVYV
160 170 180 190 200
IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH YYVSRDTLLG GSEIWRDIDF
210 220 230 240 250
AHEAPGFLPW HRLFLLLWEQ EIRELTGDEN FTVPYWDWRD AENCDICTDE
260 270 280 290 300
YLGGRHPENP NLLSPASFFS SWQIICSRSE EYNSHQVLCD GTPEGPLLRN
310 320 330 340 350
PGNHDKAKTP RLPSSADVEF CLSLTQYESG SMDRTANFSF RNTLEGFASP
360 370 380 390 400
LTGIADPSQS SMHNALHIFM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW
410 420 430 440 450
LRRHRPLLEV YPEANAPIGH NRDSYMVPFI PLYRNGDFFI TSKDLGYDYS
460 470 480 490 500
YLQESDPGFY RNYIEPYLEQ ASRIWPWLLG AALVGAVIAA ALSGLSSRLC
510 520 530
LQKKKKKKQP QEERQPLLMD KDDYHSLLYQ SHL
Length:533
Mass (Da):60,606
Last modified:May 29, 2007 - v3
Checksum:iA4C109A97CBD5D6A
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401M → I in AAA37806. (PubMed:2567165)Curated
Sequence conflicti197 – 1971D → Q in AAA37806. (PubMed:2567165)Curated
Sequence conflicti264 – 2641S → I in CAA31273. (PubMed:3141148)Curated
Sequence conflicti346 – 3461G → V in AAA40516. (PubMed:3134020)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031C → S in albino mice. 3 Publications
Natural varianti420 – 4201H → R in strain: Himalayan. 1 Publication
Natural varianti482 – 4821A → T in chinchilla mice. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS52304.1.
PIRiA27711. YRMSCS.
RefSeqiNP_035791.1. NM_011661.4.
UniGeneiMm.238127.

Genome annotation databases

EnsembliENSMUST00000004770; ENSMUSP00000004770; ENSMUSG00000004651.
GeneIDi22173.
KEGGimmu:22173.
UCSCiuc009ifo.1. mouse.

Cross-referencesi

Web resourcesi

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS52304.1.
PIRi A27711. YRMSCS.
RefSeqi NP_035791.1. NM_011661.4.
UniGenei Mm.238127.

3D structure databases

ProteinModelPortali P11344.
SMRi P11344. Positions 172-449.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204394. 7 interactions.
IntActi P11344. 1 interaction.

Chemistry

BindingDBi P11344.
ChEMBLi CHEMBL5346.

PTM databases

PhosphoSitei P11344.

Proteomic databases

PRIDEi P11344.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004770 ; ENSMUSP00000004770 ; ENSMUSG00000004651 .
GeneIDi 22173.
KEGGi mmu:22173.
UCSCi uc009ifo.1. mouse.

Organism-specific databases

CTDi 7299.
MGIi MGI:98880. Tyr.

Phylogenomic databases

eggNOGi NOG08919.
HOGENOMi HOG000118376.
HOVERGENi HBG003553.
InParanoidi P11344.
KOi K00505.
OMAi CLSLTQY.
OrthoDBi EOG7TJ3HG.
PhylomeDBi P11344.
TreeFami TF315865.

Miscellaneous databases

NextBioi 302123.
PROi P11344.
SOURCEi Search...

Gene expression databases

Bgeei P11344.
CleanExi MM_TYR.
Genevestigatori P11344.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 2 hits.
PROSITEi PS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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. 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.

Entry informationi

Entry nameiTYRO_MOUSE
AccessioniPrimary (citable) accession number: P11344
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 29, 2007
Last modified: November 26, 2014
This is version 151 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3