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UniProtKB/Swiss-Prot entry P54834

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TYRO_CANFA
Primary accession number P54834
Secondary accession number Q7YRB8
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on April 12, 2005 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 58)
Name and origin of the protein
Protein name Tyrosinase [Precursor]
Synonyms EC 1.14.18.1
Monophenol monooxygenase
Gene name
Name: TYR
From
Canis familiaris (Dog) [TaxID: 9615] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Doberman pinscher;
TISSUE=Skin;
Schmutz S.M., Berryere T.G.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.
Tang Q., Williams R.W., Hogan D., Valentine V., Goldowitz D.;
"Cloning and chromosomal in situ hybridization of the dog tyrosinase exon 1.";
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY336053; AAQ17535.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U42219; AAA86420.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001002941.1; -.
UniGene Cfa.104
3D structure databases
ModBase P54834.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0033162; Cellular component: melanosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004503; Molecular function: monophenol monooxygenase activity (inferred from electronic annotation from EC).
GO:0006583; Biological process: melanin biosynthetic process from tyrosine (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR008922; Di-copper_centre.
IPR002227; Tyrosinase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.1280.10; Di-copper_centre; 1.
Pfam PF00264; Tyrosinase; 1.
Pfam graphical view of domain structure.
PRINTS PR00092; TYROSINASE.
PROSITE PS00497; TYROSINASE_1; 1.
PS00498; TYROSINASE_2; 1.
Genome annotation databases
Ensembl ENSCAFG00000004373; Canis familiaris. [Contig view]
GeneID 403405; -.
KEGG cfa:403405; -.
Phylogenomic databases
HOVERGEN P54834; -.
Other
ProtoNet P54834.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18     Potential. 
CHAIN   19   530  512     Tyrosinase. PRO_0000035877
TOPO_DOM   19   473  455     Lumenal, melanosome (Potential). 
TRANSMEM   474   494  21     Potential. 
TOPO_DOM   495   530  36     Cytoplasmic (Potential). 
METAL   180   180        Copper A (By similarity). 
METAL   202   202        Copper A (By similarity). 
METAL   211   211        Copper A (By similarity). 
METAL   363   363        Copper B (By similarity). 
METAL   367   367        Copper B (By similarity). 
METAL   390   390        Copper B (By similarity). 
CARBOHYD   86    86        N-linked (GlcNAc...) (Potential). 
CARBOHYD   111   111        N-linked (GlcNAc...) (Potential). 
CARBOHYD   161   161        N-linked (GlcNAc...) (Potential). 
CARBOHYD   230   230        N-linked (GlcNAc...) (Potential). 
CARBOHYD   337   337        N-linked (GlcNAc...) (Potential). 
CARBOHYD   371   371        N-linked (GlcNAc...) (Potential). 
CONFLICT   3     3        L -> V (in Ref. 2; AAA86420). 
CONFLICT   7     7        C -> R (in Ref. 2; AAA86420). 
CONFLICT   59    59        I -> V (in Ref. 2; AAA86420). 
CONFLICT   115   115        K -> R (in Ref. 2; AAA86420). 
CONFLICT   132   132        N -> D (in Ref. 2; AAA86420). 
CONFLICT   212   212        R -> T (in Ref. 2; AAA86420). 
Sequence information
Length: 530 AA [This is the length of the unprocessed precursor] Molecular weight: 60336 Da [This is the MW of the unprocessed precursor] CRC64: B1C45F6362ACF0E3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLLAALCCLL WSFRTSTGHF PRACASSKSL MEKECCPPWS GDGSPCGQLS GRGACQDIIL 

        70         80         90        100        110        120 
SNAPFGPQFP FTGVDDRESW PSVFYNRTCQ CFGNFMGFNC GNCKFGFWGQ NCTEKRLLVR 

       130        140        150        160        170        180 
KNIFDLSVPE KNKFLAYLTL AKHTTSPDYV IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH 

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

       250        260        270        280        290        300 
AKSCDICTDE YMGGRNPANP NLLSPASFFS SWQIVCTRLE EYNSRQALCD GTPEGPLLRN 

       310        320        330        340        350        360 
PGNHDKARTP RLPSSADVEF CLSLTQYESD SMDKAANFSF RNTLEGFASP LTGIADASQS 

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

       430        440        450        460        470        480 
NRESYMVPFI PLYRNGDLFI SSRDLGYDYS NLQESERDIF QDYIKPYLEQ ASRIWPWLIG 

       490        500        510        520        530 
AAVVGCVVTA VLGGLTSLLC RRNRKQLHEE KQPLLMEKED YHSLLYQTHL
P54834 in FASTA format

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