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Reviewed, UniProtKB/Swiss-Prot Q9SIY8 (LAC5_ARATH)

Last modified June 16, 2009. Version 50. 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-5
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 5
    Urishiol oxidase 5
    Diphenol oxidase 5
Gene names
Name: LAC5
Synonyms: LAC1
Ordered Locus Names: At2g40370
ORF Names: T3G21.14
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 length580 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

Ubiquitous and constitutive. 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

extracellular space

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 – 580555Laccase-5
PRO_0000283633

Regions

Domain34 – 150117Plastocyanin-like 1
Domain160 – 312153Plastocyanin-like 2
Domain428 – 564137Plastocyanin-like 3

Sites

Metal binding841Copper 1; type 2 By similarity
Metal binding861Copper 2; type 3 By similarity
Metal binding1291Copper 2; type 3 By similarity
Metal binding1311Copper 3; type 3 By similarity
Metal binding4811Copper 4; type 1 By similarity
Metal binding4841Copper 1; type 2 By similarity
Metal binding4861Copper 3; type 3 By similarity
Metal binding5431Copper 3; type 3 By similarity
Metal binding5441Copper 4; type 1 By similarity
Metal binding5451Copper 2; type 3 By similarity
Metal binding5491Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9SIY8-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: EFD565D79AD887CE

FASTA58064,133
        10         20         30         40         50         60 
MDVTKSLLCF ISFVAFLLFS SVAEANKAHH HEFIIQATKV KRLCETHNSI TVNGMFPGPM 

        70         80         90        100        110        120 
LVVNNGDTLV VKVINRARYN ITIHWHGVRQ MRTGWADGPE FVTQCPIRPG SSYTYRFTIQ 

       130        140        150        160        170        180 
GQEGTLWWHA HSSWLRATVY GSLLVFPPAG SSYPFTKPHR NVPLLLGEWW DANPVDVLRE 

       190        200        210        220        230        240 
SIRTGGAPNN SDAYTINGQP GDLYKCSSQD TTVVPINVGE TILLRVINSA LNQPLFFTVA 

       250        260        270        280        290        300 
NHKLTVVGAD ASYLKPFTTN VIVLGPGQTT DVLITGDQPP NRYYMAARAY QSAQNAPFGN 

       310        320        330        340        350        360 
TTTTAILQYK SAPCCGVGGG SGTKKGNSFK PIMPILPAYN DTNTVTRFSQ SFRSLRRAEV 

       370        380        390        400        410        420 
PTEIDENLFV TIGLGLNNCP KNFRSRRCQG PNGTRFTASM NNVSFALPSN YSLLQAHHHG 

       430        440        450        460        470        480 
IPGVFTTDFP AKPPVKFDYT GNNISRSLYQ PDRGTKLYKL KYGSRVQIVL QDTGIVTPEN 

       490        500        510        520        530        540 
HPIHLHGYDF YIIAEGFGNF NPKKDTAKFN LEDPPLRNTV GVPVNGWAVI RFIADNPGVW 

       550        560        570        580 
IMHCHLDAHI SWGLAMAFLV ENGNGVLQTI EQPPHDLPVC

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning, characterization, and expression of a cDNA clone encoding laccase from Arabidopsis thaliana."
Gaynor J.J.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"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.
[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.

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Cross-references

Sequence databases

AF506030 mRNA. Translation: AAM77221.1.
AC007020 Genomic DNA. Translation: AAD25671.1.
IPIIPI00545945.
PIRF84828.
RefSeqNP_181568.1.
UniGeneAt.37061

3D structure databases

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

Proteomic databases

PRIDEQ9SIY8.

Genome annotation databases

GeneID818630.
GenomeReviewsGene locus AT2G40370 in contig CT485783_GR.
KEGGath:AT2G40370.
NMPDRfig|3702.1.peg.11166.

Organism-specific databases

TAIRAt2g40370.

Phylogenomic databases

OMAQ9SIY8. DLYKCSS.

Enzyme and pathway databases

BRENDA1.10.3.2. 302.

Gene expression databases

ArrayExpressQ9SIY8.

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 nameLAC5_ARATH
AccessionPrimary (citable) accession number: Q9SIY8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 50 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