O42713 (PPO2_AGABI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyphenol oxidase 2
Short name=PPO2
Short name=Phenolase 2
EC=1.14.18.1

Alternative name(s):
Cresolase 2
Tyrosinase 2

Gene names

Name:

PPO2

Organism

Agaricus bisporus (White button mushroom)

Taxonomic identifier

5341 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Copper-containing oxidase that catalyzes both the o-hydroxylation of monophenols and the subsequent oxidation of the resulting o-diphenols into reactive o-quinones, which evolve spontaneously to produce intermediates, which associate in dark brown pigments. Involved in the initial step of melanin synthesis. Melanins constitute a mechanism of defense and resistance to stress such as UV radiations, free radicals, gamma rays, dehydratation and extreme temperatures, and contribute to the fungal cell-wall resistance against hydrolytic enzymes in avoiding cellular lysis. Fungal pigments are also involved in the formation and stability of spores By similarity.
Catalytic activity	2 L-dopa + O2 = 2 dopaquinone + 2 H2O. L-tyrosine + O2 = dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit By similarity.
Subunit structure	Heterotetramer By similarity.
Developmental stage	Expressed during the fruiting body stage. Ref.3
Post-translational modification	The C-ter is probably cleaved after Gly-378 since the mature active protein is smaller than the protein encoded by the gene By similarity.
Sequence similarities	Belongs to the tyrosinase family.
Sequence caution	The sequence CAA61562.1 differs from that shown. Reason: Frameshift at position 445.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Thioether bond
Gene Ontology (GO)
Biological_process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 378	378	Polyphenol oxidase 2		PRO_0000186731
	Propeptide	379 – 556	178	Removed in mature form Probable		PRO_0000416863
Sites
	Metal binding	57	1	Copper 1; via tele nitrogen By similarity
	Metal binding	81	1	Copper 1; via tele nitrogen By similarity
	Metal binding	90	1	Copper 1; via tele nitrogen By similarity
	Metal binding	250	1	Copper 2; via tele nitrogen By similarity
	Metal binding	254	1	Copper 2; via tele nitrogen By similarity
	Metal binding	282	1	Copper 2; via tele nitrogen By similarity
	Binding site	254	1	Substrate By similarity
	Site	378 – 379	2	Cleavage Probable
Amino acid modifications
	Cross-link	79 ↔ 81		2'-(S-cysteinyl)-histidine (Cys-His) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O42713 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: DE10827A209895DA	FASTA	556	63,927
	10 20 30 40 50 60 MSLIATVGPT GGVKNRLNIV DFVKNEKFFT LYVRSLELLQ AKEQHDYSSF FQLAGIHGLP 70 80 90 100 110 120 FTEWAKERPS MNLYKAGYCT HGQVLFPTWH RTYLSVLEQI LQGAAIEVAK KFTSNQTDWV 130 140 150 160 170 180 QAAQDLRQPY WDWGFELMPP DEVIKNEEVN ITNYDGKKIS VKNPILRYHF HPIDPSFKPY 190 200 210 220 230 240 GDFATWRTTV RNPDRNRRED IPGLIKKMRL EEGQIREKTY NMLKFNDAWE RFSNHGISDD 250 260 270 280 290 300 QHANSLESVH DDIHVMVGYG KIEGHMDHPF FAAFDPIFWL HHTNVDRLLS LWKAINPDVW 310 320 330 340 350 360 VTSGRNRDGT MGIAPNAQIN SETPLEPFYQ SGDKVWTSAS LADTARLGYS YPDFDKLVGG 370 380 390 400 410 420 TKELIRDAID DLIDERYGSK PSSGARNTAF DLLADFKGIT KEHKEDLKMY DWTIHVAFKK 430 440 450 460 470 480 FELKESFSLL FYFASDGGDY DQENCFVGSI NAFRGTAPET CANCQDNENL IQEGFIHLNH 490 500 510 520 530 540 YLARDLESFE PQDVHKFLKE KGLSYKLYSR GDKPLTSLSV KIEGRPLHLP PGEHRPKYDH 550 TQARVVFDDV AVHVIN

References

[1]	"Cloning, expression and characterisation of two tyrosinase cDNAs from Agaricus bisporus." Wichers H., Recourt K., Hendriks M., Ebbelaar C.E.M., Biancone G., Hoeberichts F., Mooibroek H., Soler-Rivas C. Appl. Microbiol. Biotechnol. 61:336-341(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Horst U1.
[2]	"Characterization of a fruiting body-expressed gene encoding a putative polyphenol oxidase of Agaricus bisporus." Ebbelar C.E.M., Wichers H.J., Van Den Bosch T., Oyevaar J.I., Recourt K. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-556. Strain: Horst U1.
[3]	"Expression of phenol oxidase and heat-shock genes during the development of Agaricus bisporus fruiting bodies, healthy and infected by Lecanicillium fungicola." Largeteau M.L., Latapy C., Minvielle N., Regnault-Roger C., Savoie J.M. Appl. Microbiol. Biotechnol. 85:1499-1507(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ223816 mRNA. Translation: CAA11562.1. X89382 mRNA. Translation: CAA61562.1. Frameshift.
3D structure databases
ProteinModelPortal	O42713.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
SABIO-RK	O42713.
Family and domain databases
Gene3D	1.10.1280.10. 1 hit.
InterPro	IPR016216. Monophenol_mOase_fun. IPR002227. Tyrosinase. IPR008922. Unchr_di-copper_centre. [Graphical view]
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PIRSF	PIRSF000340. MPO_fungal. 1 hit.
PRINTS	PR00092. TYROSINASE.
SUPFAM	SSF48056. Di-copper_centre. 1 hit.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O42713.
ChEMBL	CHEMBL3318.

Entry information

Entry name

PPO2_AGABI

Accession

Primary (citable) accession number: O42713
Secondary accession number(s): Q12543

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	April 3, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program