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P54834

- TYRO_CANFA

UniProt

P54834 - TYRO_CANFA

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Protein

Tyrosinase

Gene

TYR

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Binds 2 copper ions per subunit.By similarity

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. metal ion binding Source: UniProtKB-KW
  2. monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-KW
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):
Monophenol monooxygenase
Gene namesi
Name:TYR
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 530512TyrosinasePRO_0000035877Add
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

Structurei

3D structure databases

ProteinModelPortaliP54834.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 473455Lumenal, melanosomeSequence AnalysisAdd
BLAST
Topological domaini495 – 53036CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei474 – 49421HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG08919.
HOGENOMiHOG000118376.
HOVERGENiHBG003553.
InParanoidiP54834.
KOiK00505.

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. 1 hit.
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.

P54834-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLAALCCLL WSFRTSTGHF PRACASSKSL MEKECCPPWS GDGSPCGQLS
60 70 80 90 100
GRGACQDIIL SNAPFGPQFP FTGVDDRESW PSVFYNRTCQ CFGNFMGFNC
110 120 130 140 150
GNCKFGFWGQ NCTEKRLLVR KNIFDLSVPE KNKFLAYLTL AKHTTSPDYV
160 170 180 190 200
IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH YYVSRDTLLG GSEIWKDIDF
210 220 230 240 250
AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD AKSCDICTDE
260 270 280 290 300
YMGGRNPANP NLLSPASFFS SWQIVCTRLE EYNSRQALCD GTPEGPLLRN
310 320 330 340 350
PGNHDKARTP RLPSSADVEF CLSLTQYESD SMDKAANFSF RNTLEGFASP
360 370 380 390 400
LTGIADASQS SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW
410 420 430 440 450
LRRHHPLREV YPEANAPIGH NRESYMVPFI PLYRNGDLFI SSRDLGYDYS
460 470 480 490 500
NLQESERDIF QDYIKPYLEQ ASRIWPWLIG AAVVGCVVTA VLGGLTSLLC
510 520 530
RRNRKQLHEE KQPLLMEKED YHSLLYQTHL
Length:530
Mass (Da):60,336
Last modified:April 12, 2005 - v2
Checksum:iB1C45F6362ACF0E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31L → V in AAA86420. 1 PublicationCurated
Sequence conflicti7 – 71C → R in AAA86420. 1 PublicationCurated
Sequence conflicti59 – 591I → V in AAA86420. 1 PublicationCurated
Sequence conflicti115 – 1151K → R in AAA86420. 1 PublicationCurated
Sequence conflicti132 – 1321N → D in AAA86420. 1 PublicationCurated
Sequence conflicti212 – 2121R → T in AAA86420. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY336053 mRNA. Translation: AAQ17535.1.
U42219 Genomic DNA. Translation: AAA86420.1.
RefSeqiNP_001002941.1. NM_001002941.1.
UniGeneiCfa.104.

Genome annotation databases

GeneIDi403405.
KEGGicfa:403405.

Cross-referencesi

Web resourcesi

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY336053 mRNA. Translation: AAQ17535.1 .
U42219 Genomic DNA. Translation: AAA86420.1 .
RefSeqi NP_001002941.1. NM_001002941.1.
UniGenei Cfa.104.

3D structure databases

ProteinModelPortali P54834.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 403405.
KEGGi cfa:403405.

Organism-specific databases

CTDi 7299.

Phylogenomic databases

eggNOGi NOG08919.
HOGENOMi HOG000118376.
HOVERGENi HBG003553.
InParanoidi P54834.
KOi K00505.

Miscellaneous databases

NextBioi 20816926.

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. 1 hit.
PROSITEi PS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Schmutz S.M., Berryere T.G.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Doberman pinscher.
    Tissue: Skin.
  2. "Cloning and chromosomal in situ hybridization of the dog tyrosinase exon 1."
    Tang Q., Williams R.W., Hogan D., Valentine V., Goldowitz D.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.

Entry informationi

Entry nameiTYRO_CANFA
AccessioniPrimary (citable) accession number: P54834
Secondary accession number(s): Q7YRB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 12, 2005
Last modified: October 29, 2014
This is version 93 of the entry and version 2 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3