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Reviewed, UniProtKB/Swiss-Prot O81081 (LAC2_ARATH)

Last modified November 25, 2008. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Laccase-2
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 2
    Urishiol oxidase 2
    Diphenol oxidase 2
Gene names
Name: LAC2
Ordered Locus Names: At2g29130
ORF Names: T9I4.21
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length573 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Lignin degradation and detoxification of lignin-derived products By similarity. Required for root elongation in dehydration conditions.

Catalytic activity

4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secreted › extracellular space › apoplastPotential.

Tissue specificity

Ubiquitous and constitutive.

Induction

By NaCl and 20% PEG.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

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Ontologies

Keywords

   Biological processLignin degradation
   Cellular componentApoplast
Secreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentapoplast

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 573547Laccase-2
PRO_0000283630

Regions

Domain35 – 151117Plastocyanin-like 1
Domain161 – 314154Plastocyanin-like 2
Domain423 – 557135Plastocyanin-like 3

Sites

Metal binding851Copper 1; type 2 By similarity
Metal binding871Copper 2; type 3 By similarity
Metal binding1301Copper 2; type 3 By similarity
Metal binding1321Copper 3; type 3 By similarity
Metal binding4741Copper 4; type 1 By similarity
Metal binding4771Copper 1; type 2 By similarity
Metal binding4791Copper 3; type 3 By similarity
Metal binding5361Copper 3; type 3 By similarity
Metal binding5371Copper 4; type 1 By similarity
Metal binding5381Copper 2; type 3 By similarity
Metal binding5421Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Potential
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation2421N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
O81081-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 1FC2D2C5B3D9E64A

FASTA57363,832
        10         20         30         40         50         60 
MVTWVLNYLL VAFLFAISYN IDAASAGITR HYQFDIQLKN ITRLCKTKTI VTVNGKFPGP 

        70         80         90        100        110        120 
RVTAREGDNL QIKVVNHVSN NISIHWHGIR QLRSGWADGP SYVTQCPIRM GQSYVYNFTV 

       130        140        150        160        170        180 
TGQRGTLWWH AHIQWMRATV YGPLIILPKL HQPYPFPKPY KQVPILFGEW FNADPQAVVQ 

       190        200        210        220        230        240 
QALQTGAGPN ASDAHTFNGL PGPLYNCSTK DTYKLMVKPG KTYLLRLINA ALNDELFFTI 

       250        260        270        280        290        300 
ANHTLTVVEA DACYVKPFQT NIVLLGPGQT TNVLLKTKPI YPNATFYMLA RPYFTGQGTI 

       310        320        330        340        350        360 
DNTTVAGILQ YQHHTKSSKN LSIIKPSLPP INSTSYAANF TKMFRSLASS TFPANVPKVV 

       370        380        390        400        410        420 
DKQYFFAIGL GTNPCPKNQT CQGPTNTTKF AASINNVSFI LPNKTSLLQS YFVGKSKNVF 

       430        440        450        460        470        480 
MTDFPTAPII PFNYTGTPPN NTMVSRGTKV VVLKYKTTVE LVLQGTSILG IEAHPIHLHG 

       490        500        510        520        530        540 
FNFYVVGQGF GNFNPARDPK HYNLVDPVER NTINIPSGGW VAIRFLADNP GVWLMHCHIE 

       550        560        570 
IHLSWGLTMA WVVLDGDLPN QKLLPPPSDF PKC

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed: 10617197] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana."
McCaig B.C., Meagher R.B., Dean J.F.D.
Planta 221:619-636(2005) [PubMed: 15940465] [Abstract]
Cited for: TISSUE SPECIFICITY.
[3]"Mutant identification and characterization of the laccase gene family in Arabidopsis."
Cai X., Davis E.J., Ballif J., Liang M., Bushman E., Haroldsen V., Torabinejad J., Wu Y.
J. Exp. Bot. 57:2563-2569(2006) [PubMed: 16804053] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.

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Cross-references

Sequence databases

AC005315 Genomic DNA. Translation: AAC33238.1.
PIRT02743.
RefSeqNP_180477.1.
UniGeneAt.13041

3D structure databases

HSSPHSSP built from PDB template 1AOZ based on UniProtKB P37064.
ModBaseSearch...

Genome annotation databases

GeneID817462.
GenomeReviewsGene locus AT2G29130 in contig CT485783_GR.
KEGGath:AT2G29130.
NMPDRfig|3702.1.peg.9961.

Organism-specific databases

TAIRAt2g29130.

Gene expression databases

ArrayExpressO81081.

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR017761. Laccase.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLAC2_ARATH
AccessionPrimary (citable) accession number: O81081
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: November 1, 1998
Last modified: November 25, 2008
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents