Reviewed, UniProtKB/Swiss-Prot A7BHQ9 (TYRO_PHONA)

Names and origin

Protein names

Recommended name:
    Tyrosinase
    EC=1.14.18.1

Gene names

Name:

tyr1

Organism

Pholiota nameko

Taxonomic identifier

61267 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Strophariaceae › Pholiota

Protein attributes

Sequence length	625 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. UniProtKB Q92396
Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O. Ref.1
Cofactor	Binds 2 copper ions per subunit. Ref.1
Subunit structure	Monomer. Ref.1
Post-translational modification	The N-terminus is blocked. Ref.1
Sequence similarities	Belongs to the tyrosinase family.
Biophysicochemical properties	Kinetic parameters: KM=1930 µM for L-dopa Ref.1 KM=119 µM for t-butylphenol Ref.1 KM=30.6 µM for p-cresol Ref.1 KM=163 µM for t-butylcatechol Ref.1 KM=1240 µM for 3-(3,4-dihydroxyphenyl) propionic acid Ref.1 KM=122 µM for dopamine Ref.1
Mass spectrometry	Molecular mass is 42424.39 Da from positions 1 - 387. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Melanin biosynthesis
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	copper ion binding Ref.1 Inferred from direct assay. Source: UniProtKB monophenol monooxygenase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 387	387	Tyrosinase Ref.1		PRO_0000352767
	Propeptide	388 – 625	238	Ref.1		PRO_0000352768
Regions
	Compositional bias	367 – 451	85	Ala-rich
Sites
	Metal binding	58	1	Copper A By similarity UniProtKB Q9ZP19
	Metal binding	86	1	Copper A By similarity UniProtKB Q9ZP19
	Metal binding	95	1	Copper A By similarity UniProtKB Q9ZP19
	Metal binding	258	1	Copper B By similarity UniProtKB Q9ZP19
	Metal binding	262	1	Copper B By similarity UniProtKB Q9ZP19
	Metal binding	287	1	Copper B By similarity UniProtKB Q9ZP19
Experimental info
	Sequence conflict	13	1	I → V in BAF74396. Ref.1
	Sequence conflict	151	1	V → A in BAF74396. Ref.1
	Sequence conflict	272	1	G → A in BAF74396. Ref.1
	Sequence conflict	425	1	P → S in BAF74396. Ref.1
	Sequence conflict	528	1	S → N in BAF74396. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A7BHQ9-1 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: 26E8AEFA285F871B	FASTA	625	67,499
	10 20 30 40 50 60 MSRVVITGVS GTIANRLEIN DFVKNDKFFS LYIQALQVMS SVPPQENVRS FFQIGGIHGL 70 80 90 100 110 120 PYTPWDGITG DQPFDPNTQW GGYCTHGSVL FPTWHRPYVL LYEQILHKHV QDIAATYTTS 130 140 150 160 170 180 DKAAWVQAAA NLRQPYWDWA ANAVPPDQVI VSKKVTITGS NGHKVEVDNP LYHYKFHPID 190 200 210 220 230 240 SSFPRPYSEW PTTLRQPNSS RPNATDNVAK LRNVLRASQE NITSNTYSML TRVHTWKAFS 250 260 270 280 290 300 NHTVGDGGST SNSLEAIHDG IHVDVGGGGH MGDPAVAAFD PIFFLHHCNV DRLLSLWAAI 310 320 330 340 350 360 NPGVWVSPGD SEDGTFILPP EAPVDVSTPL TPFSNTETTF WASGGITDTT KLGYTYPEFN 370 380 390 400 410 420 GLDLGNAQAV KAAIGNIVNR LYGASVFSGF AAATSAIGAG SVASLAADVP LEKAPAPAPE 430 440 450 460 470 480 AAAQPPVPAP AHVEPAVRAV SVHAAAAQPH AEPPVHVSAG GHPSPHGFYD WTARIEFKKY 490 500 510 520 530 540 EFGSSFSVLL FLGPVPEDPE QWLVSPNFVG AHHAFVNSAA GHCANCRSQG NVVVEGFVHL 550 560 570 580 590 600 TKYISEHAGL RSLNPEVVEP YLTNELHWRV LKADGSVGQL ESLEVSVYGT PMNLPVGAMF 610 620 PVPGNRRHFH GITHGRVGGS RHAIV

References

[1]

"Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko." Kawamura-Konishi Y., Tsuji M., Hatana S., Asanuma M., Kakuta D., Kawano T., Mukouyama E.B., Goto H., Suzuki H. Biosci. Biotechnol. Biochem. 71:1752-1760(2007) [PubMed: 17617709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164; 175-195; 351-362 AND 384-387, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY. Tissue: Fruiting body.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB275646 mRNA. Translation: BAF74395.1. AB275647 mRNA. Translation: BAF74396.1.
3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PRINTS	PR00092. TYROSINASE.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYRO_PHONA

Accession

Primary (citable) accession number: A7BHQ9
Secondary accession number(s): A7BHR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 14, 2008
Last sequence update:	September 11, 2007
Last modified:	September 22, 2009
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)