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Q12542 (LAC2_AGABI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Laccase-2
EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Laccase II
Urishiol oxidase 2
Gene names
Name:lcc2
OrganismAgaricus bisporus (White button mushroom)
Taxonomic identifier5341 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Agaricomycetes › Agaricomycetidae › Agaricales › Agaricaceae › Agaricus

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

hydroquinone:oxygen oxidoreductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 520501Laccase-2
PRO_0000002919

Regions

Domain21 – 145125Plastocyanin-like 1
Domain157 – 305149Plastocyanin-like 2
Domain375 – 488114Plastocyanin-like 3

Sites

Metal binding821Copper 1; type 2 By similarity
Metal binding841Copper 2; type 3 By similarity
Metal binding1271Copper 2; type 3 By similarity
Metal binding1291Copper 3; type 3 By similarity
Metal binding4171Copper 4; type 1 By similarity
Metal binding4201Copper 1; type 2 By similarity
Metal binding4221Copper 3; type 3 By similarity
Metal binding4701Copper 3; type 3 By similarity
Metal binding4711Copper 4; type 1 By similarity
Metal binding4721Copper 2; type 3 By similarity
Metal binding4761Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation1081N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2991N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Glycosylation4921N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q12542 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EF100145F0A697AA

FASTA52057,823
        10         20         30         40         50         60 
MRFSNAFVLV AACISSVLAD TKTFNFDLVN TRLAPDGFER DTVVINGEFP GTLVQVNKGD 

        70         80         90        100        110        120 
SVRIPVNNKL TSSTMRRSVS IHWHGFFQAR TSGQDGPAFV NQCPQPPNTT FTYEFSVADE 

       130        140        150        160        170        180 
SGTFWYHSHL STQYCDGLRG AFVVYDPEDP LGHLYDVDDE TTVITLAEWY HVLAPDINNE 

       190        200        210        220        230        240 
FFSSGIIPVQ DSGLINGKGR FNGGPETPFA VVNVEQGKRY RFRVIAISCR PFFTFSVDNH 

       250        260        270        280        290        300 
NLTFMEADSV EHDPVEIQNV DIYAAQRVSV ILNANQPVDN YWMRAPMTGG NPDRNPNLNI 

       310        320        330        340        350        360 
SLTLAILRYK GAPEVEPTTV NVPGHKLLDQ EMHPIAQEGP GKLGDGPPDK HITLNIAQPN 

       370        380        390        400        410        420 
APFFDINGIS YISPTVPVLL QILSGAKRPE DVLPSEQIFF VPKNSLIEVN IPGEGAHPFH 

       430        440        450        460        470        480 
LHGHNFDVVL ASNDDTFNFV NPPRRDVYPI NGGNTTFRFF TDNPGAWFLH CHIDWHLEAG 

       490        500        510        520 
LAIVFAEAPE DNVSGPQSQI TPQDWLDLCP EYNAIEPEFQ

« Hide

References

[1]"Identification of two laccase genes in the cultivated mushroom Agaricus bisporus."
Perry C.R., Smith M., Britnell C.H., Wood D.A., Thurston C.F.
J. Gen. Microbiol. 139:1209-1218(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: D649.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L10663 mRNA. Translation: AAA17035.1.

3D structure databases

ProteinModelPortalQ12542.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.40.420. 3 hits.
InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 3 hits.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 2 hits.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC2_AGABI
AccessionPrimary (citable) accession number: Q12542
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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