[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], GLYCOSYLATION AT ASN-467, AND MASS SPECTROMETRY. TISSUE=Mycelium; PubMed=8654395 [NCBI, ExPASy, EBI, Israel, Japan] Giardina P., Aurilia V., Cannio R., Marzullo L., Amoresano A., Siciliano R., Pucci P., Sannia G.; "The gene, protein and glycan structures of laccase from Pleurotus ostreatus."; Eur. J. Biochem. 235:508-515(1996).
[2]	CHARACTERIZATION. STRAIN=Florida; TISSUE=Mycelium; DOI=10.1007/BF00205066; PubMed=7763931 [NCBI, ExPASy, EBI, Israel, Japan] Palmieri G., Giardina P., Marzullo L., Desiderio B., Nitti G., Cannio R., Sannia G.; "Stability and activity of a phenol oxidase from the ligninolytic fungus Pleurotus ostreatus."; Appl. Microbiol. Biotechnol. 39:632-636(1993).

Comments

FUNCTION: Lignin degradation and detoxification of lignin-derived products (By similarity).
CATALYTIC ACTIVITY: 4 benzenediol + O₂ = 4 benzosemiquinone + 2 H₂O.
COFACTOR: Binds 4 copper ions per monomer (By similarity).
SUBCELLULAR LOCATION: Secreted.
PTM: N-glycosylated at Asn-467; contains a high-mannose glycan with a varying number of mannose residues.
MISCELLANEOUS: POX2 isozyme is the most abundant laccase of P.ostreatus under various growth conditions.
SIMILARITY: Belongs to the multicopper oxidase family.
SIMILARITY: Contains 3 plastocyanin-like domains.

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

Z49075; CAA88895.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z34848; CAA84357.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S62371; S62371.

3D structure databases

HSSP

Q12718; 1GYC. [HSSP ENTRY / PDB]

ModBase

Q12739.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0008471;	Molecular function: laccase activity (inferred from electronic annotation from EC).
GO:0046274;	Biological process: lignin catabolic process (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

IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.420; Cupredoxin; 3.

Pfam

PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.

PROSITE

PS00079; MULTICOPPER_OXIDASE1; 2.
PS00080; MULTICOPPER_OXIDASE2; 1.

Other

ProtoNet

Q12739.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Copper; Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 533`	`510`	`Laccase-2.`	`PRO_0000002930`
`DOMAIN`	`25 171`	`147`	`Plastocyanin-like 1.`
`DOMAIN`	`173 336`	`164`	`Plastocyanin-like 2.`
`DOMAIN`	`382 501`	`120`	`Plastocyanin-like 3.`
`METAL`	`98 98`		`Copper 1; type 2 (By similarity).`
`METAL`	`100 100`		`Copper 2; type 3 (By similarity).`
`METAL`	`143 143`		`Copper 2; type 3 (By similarity).`
`METAL`	`145 145`		`Copper 3; type 3 (By similarity).`
`METAL`	`427 427`		`Copper 4; type 1 (By similarity).`
`METAL`	`430 430`		`Copper 1; type 2 (By similarity).`
`METAL`	`432 432`		`Copper 3; type 3 (By similarity).`
`METAL`	`483 483`		`Copper 3; type 3 (By similarity).`
`METAL`	`484 484`		`Copper 4; type 1 (By similarity).`
`METAL`	`485 485`		`Copper 2; type 3 (By similarity).`
`METAL`	`489 489`		`Copper 4; type 1 (By similarity).`
`CARBOHYD`	`467 467`		`N-linked (GlcNAc...) (high mannose).`

Sequence information

Length: 533 AA [This is the length of the unprocessed precursor]

Molecular weight: 56767 Da [This is the MW of the unprocessed precursor]

CRC64: 7233C41D47E19AE6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFPGARILAT LTLALHLLHG AHAAIGPAGN MYIVNEDVSP DGFARSAVVA RSVPATDPTP 

        70         80         90        100        110        120 
ATASIPGVLV QGNKGDNFQL NVVNQLSDTT MLKTTSIHWH GFFQAGSSWA DGPAFVTQCP 

       130        140        150        160        170        180 
VASGDSFLYN FNVPDQAGTF WYHSHLSTQY CDGLRGPFVV YDPSDPHLSL YDIDNADTVI 

       190        200        210        220        230        240 
TLEDWYHIVA PQNAAIPTPD STLINGKGRY AGGPTSPLAI INVESNKRYR FRLVSMSCDP 

       250        260        270        280        290        300 
NFTFSIDGHS LLVIEADAVN IVPITVDSIQ IFAGQRYSFV LTANQAVDNY WIRANPNLGS 

       310        320        330        340        350        360 
TGFVGGINSA ILRYAGATED DPTTTSSTST PLLETNLVPL ENPGAPGPPV PGGADININL 

       370        380        390        400        410        420 
AMAFDFTTFE LTINGVPFLP PTAPVLLQIL SGASTAASLL PSGSIYELEA NKVVEISMPA 

       430        440        450        460        470        480 
LAVGGPHPFH LHGHTFDVIR SAGSTTYNFD TPARRDVVNT GTGANDNVTI RFVTDNPGPW 

       490        500        510        520        530 
FLHCHIDWHL EIGLAVVFAE DVTSISAPPA AWDDLCPIYN ALSDNDKGGI VPS

Q12739 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools