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Reviewed, UniProtKB/Swiss-Prot Q6ID18 (LAC10_ARATH)

Last modified November 25, 2008. Version 35. 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-10
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 10
    Urishiol oxidase 10
    Diphenol oxidase 10
Gene names
Name: LAC10
Ordered Locus Names: At5g01190
ORF Names: F7J8.170
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 length558 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 + 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, with lower levels in siliques. Ref.3

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Sequence caution

The sequence CAB69847.1 differs from that shown. Reason: Erroneous gene model prediction.

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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 – 2222 Potential
Chain23 – 558536Laccase-10
PRO_0000283638

Regions

Domain30 – 146117Plastocyanin-like 1
Domain157 – 308152Plastocyanin-like 2
Domain408 – 542135Plastocyanin-like 3

Sites

Metal binding801Copper 1; type 2 By similarity
Metal binding821Copper 2; type 3 By similarity
Metal binding1251Copper 2; type 3 By similarity
Metal binding1271Copper 3; type 3 By similarity
Metal binding4591Copper 4; type 1 By similarity
Metal binding4621Copper 1; type 2 By similarity
Metal binding4641Copper 3; type 3 By similarity
Metal binding5211Copper 3; type 3 By similarity
Metal binding5221Copper 4; type 1 By similarity
Metal binding5231Copper 2; type 3 By similarity
Metal binding5271Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation761N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation1851N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3731N-linked (GlcNAc...) Potential
Glycosylation3831N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q6ID18-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 4F0CACDA7088ACBA

FASTA55861,298
        10         20         30         40         50         60 
MVFPIRILVL FALLAFPACV HGAIRKYTFN VVTKQVTRIC STKQIVTVNG KFPGPTIYAN 

        70         80         90        100        110        120 
EDDTILVNVV NNVKYNVSIH WHGIRQLRTG WADGPAYITQ CPIKPGHSYV YNFTVTGQRG 

       130        140        150        160        170        180 
TLWWHAHVLW LRATVHGAIV ILPKLGLPYP FPKPHREEVI ILGEWWKSDT ETVVNEALKS 

       190        200        210        220        230        240 
GLAPNVSDAH VINGHPGFVP NCPSQGNFKL AVESGKTYML RLINAALNEE LFFKIAGHRF 

       250        260        270        280        290        300 
TVVEVDAVYV KPFNTDTILI APGQTTTALV SAARPSGQYL IAAAPFQDSA VVAVDNRTAT 

       310        320        330        340        350        360 
ATVHYSGTLS ATPTKTTSPP PQNATSVANT FVNSLRSLNS KTYPANVPIT VDHDLLFTVG 

       370        380        390        400        410        420 
LGINRCHSCK AGNFSRVVAA INNITFKMPK TALLQAHYFN LTGIYTTDFP AKPRRVFDFT 

       430        440        450        460        470        480 
GKPPSNLATM KATKLYKLPY NSTVQVVLQD TGNVAPENHP IHLHGFNFFV VGLGTGNYNS 

       490        500        510        520        530        540 
KKDSNKFNLV DPVERNTVGV PSGGWAAIRF RADNPGVWFM HCHLEVHTTW GLKMAFLVEN 

       550 
GKGPNQSIRP PPSDLPKC

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Arabidopsis ORF clones."
Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[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: TISSUE SPECIFICITY.

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Cross-references

Sequence databases

AL137189 Genomic DNA. Translation: CAB69847.1. Sequence problems.
BT014855 mRNA. Translation: AAT41838.1.
PIRT45959.
RefSeqNP_195739.2.
UniGeneAt.33933

3D structure databases

HSSPHSSP built from PDB template 1A65 based on UniProtKB Q9Y780.
ModBaseSearch...

Genome annotation databases

GeneID831697.
GenomeReviewsGene locus AT5G01190 in contig BA000015_GR.
KEGGath:AT5G01190.

Organism-specific databases

TAIRAt5g01190.

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 nameLAC10_ARATH
AccessionPrimary (citable) accession number: Q6ID18
Secondary accession number(s): Q9LFB7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: November 25, 2008
This is version 35 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