Reviewed, UniProtKB/Swiss-Prot Q12739 (LAC2_PLEOS)

Names and origin

Protein names

Recommended name:
    Laccase-2
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 2
    Urishiol oxidase 2
    Diphenol oxidase 2

Gene names

Name:

POX2

Organism

Pleurotus ostreatus (Oyster mushroom) (White-rot fungus)

Taxonomic identifier

5322 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Pleurotaceae › Pleurotus

Protein attributes

Sequence length	533 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	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.
Post-translational modification	N-glycosylated at Asn-467; contains a high-mannose glycan with a varying number of mannose residues. Ref.1
Miscellaneous	POX2 isozyme is the most abundant laccase of P.ostreatus under various growth conditions.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Lignin degradation
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW laccase 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
	Signal peptide	1 – 23	23
	Chain	24 – 533	510	Laccase-2		PRO_0000002930
Regions
	Domain	25 – 171	147	Plastocyanin-like 1
	Domain	173 – 336	164	Plastocyanin-like 2
	Domain	382 – 501	120	Plastocyanin-like 3
Sites
	Metal binding	98	1	Copper 1; type 2 By similarity
	Metal binding	100	1	Copper 2; type 3 By similarity
	Metal binding	143	1	Copper 2; type 3 By similarity
	Metal binding	145	1	Copper 3; type 3 By similarity
	Metal binding	427	1	Copper 4; type 1 By similarity
	Metal binding	430	1	Copper 1; type 2 By similarity
	Metal binding	432	1	Copper 3; type 3 By similarity
	Metal binding	483	1	Copper 3; type 3 By similarity
	Metal binding	484	1	Copper 4; type 1 By similarity
	Metal binding	485	1	Copper 2; type 3 By similarity
	Metal binding	489	1	Copper 4; type 1 By similarity
Amino acid modifications
	Glycosylation	467	1	N-linked (GlcNAc...) (high mannose) Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q12739-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7233C41D47E19AE6	FASTA	533	56,767
	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

References

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z49075 Genomic DNA. Translation: CAA88895.1. Z34848 mRNA. Translation: CAA84357.1.
PIR	S62371.
3D structure databases
HSSP	HSSP built from PDB template 1GYC based on UniProtKB Q12718.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.10.3.2. 16687.
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]
Gene3D	G3DSA:2.60.40.420. Cupredoxin. 3 hits.
Pfam	PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
PROSITE	PS00079. MULTICOPPER_OXIDASE1. 2 hits. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAC2_PLEOS

Accession

Primary (citable) accession number: Q12739

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)