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Reviewed, UniProtKB/Swiss-Prot Q56YT0 (LAC3_ARATH)

Last modified November 3, 2009. Version 41. 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-3
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 3
    Urishiol oxidase 3
    Diphenol oxidase 3
Gene names
Name: LAC3
Ordered Locus Names: At2g30210
ORF Names: T9D9.2
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 length570 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.

Catalytic activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secreted › extracellular space › apoplast Potential.

Tissue specificity

Mostly expressed in roots and siliques. Ref.3 Ref.4

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-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 2525 Potential
Chain26 – 570545Laccase-3
PRO_0000283631

Regions

Domain33 – 149117Plastocyanin-like 1
Domain159 – 310152Plastocyanin-like 2
Domain419 – 554136Plastocyanin-like 3

Sites

Metal binding831Copper 1; type 2 By similarity
Metal binding851Copper 2; type 3 By similarity
Metal binding1281Copper 2; type 3 By similarity
Metal binding1301Copper 3; type 3 By similarity
Metal binding4711Copper 4; type 1 By similarity
Metal binding4741Copper 1; type 2 By similarity
Metal binding4761Copper 3; type 3 By similarity
Metal binding5331Copper 3; type 3 By similarity
Metal binding5341Copper 4; type 1 By similarity
Metal binding5351Copper 2; type 3 By similarity
Metal binding5391Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1881N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3321N-linked (GlcNAc...) Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Glycosylation4331N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q56YT0-1 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 48520C684D7B2DA3

FASTA57064,027
        10         20         30         40         50         60 
MESFRRFSLL SFIALLAYFA FLASAEHHVH QFVITPTPVK RLCRTHQSIT VNGQYPGPTL 

        70         80         90        100        110        120 
VVRNGDSLAI TVINRARYNI SIHWHGIRQL RNPWADGPEY ITQCPIRPGQ TYTYRFKIED 

       130        140        150        160        170        180 
QEGTLWWHAH SRWLRATVYG ALIIYPRLGS PYPFSMPKRD IPILLGEWWD RNPMDVLKQA 

       190        200        210        220        230        240 
QFTGAAANVS DAYTINGQPG DLYRCSRAGT IRFPIFPGET VQLRVINAGM NQELFFSVAN 

       250        260        270        280        290        300 
HQFTVVETDS AYTKPFTTNV IMIGPGQTTN VLLTANQRPG RYYMAARAYN SANAPFDNTT 

       310        320        330        340        350        360 
TTAILQYVNA PTRRGRGRGQ IAPVFPVLPG FNDTATATAF TNRLRYWKRA PVPQQVDENL 

       370        380        390        400        410        420 
FFTVGLGLIN CANPNSPRCQ GPNGTRFAAS MNNMSFVLPR SNSVMQAYYQ GTPGIFTTDF 

       430        440        450        460        470        480 
PPVPPVQFDY TGNVSRGLWQ PIKGTKAYKL KYKSNVQIVL QDTSIVTPEN HPMHLHGYQF 

       490        500        510        520        530        540 
YVVGSGFGNF NPRTDPARFN LFDPPERNTI GTPPGGWVAI RFVADNPGAW FMHCHIDSHL 

       550        560        570 
GWGLAMVFLV ENGRGQLQSV QAPPLDLPRC

« Hide

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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]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-570.
Strain: cv. Columbia.
[3]"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.
[4]"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: TISSUE SPECIFICITY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AC002338 Genomic DNA. Translation: AAC16927.1.
AC004165 Genomic DNA. Translation: AAM14916.1.
AK221241 mRNA. Translation: BAD93858.1.
IPIIPI00543063.
PIRT00579.
RefSeqNP_180580.1.
UniGeneAt.27864

3D structure databases

HSSPHSSP built from PDB template 1KYA based on UniProtKB Q96UT7.
ModBaseSearch...

Proteomic databases

PRIDEQ56YT0.

Genome annotation databases

GeneID817571.
GenomeReviewsGene locus AT2G30210 in contig CT485783_GR.
KEGGath:AT2G30210.
NMPDRfig|3702.1.peg.10073.

Organism-specific databases

TAIRAt2g30210.

Phylogenomic databases

OMAMAARAYN.

Enzyme and pathway databases

BRENDA1.10.3.2. 302.

Gene expression databases

GenevestigatorQ56YT0.

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]
TIGRFAMsTIGR03389. laccase. 1 hit.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLAC3_ARATH
AccessionPrimary (citable) accession number: Q56YT0
Secondary accession number(s): O22917
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: November 3, 2009
This is version 41 of the entry and version 2 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