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Reviewed, UniProtKB/Swiss-Prot Q9LYQ2 (LAC13_ARATH)

Last modified February 9, 2010. Version 52. 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-13
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 13
    Urishiol oxidase 13
    Diphenol oxidase 13
Gene names
Name: LAC13
Ordered Locus Names: At5g07130
ORF Names: T28J14.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

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Protein attributes

Sequence length569 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. Also detected in leaves, stems and flowers but not in siliques. Ref.2

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 – 2121 Potential
Chain22 – 569548Laccase-13
PRO_0000283641

Regions

Domain29 – 145117Plastocyanin-like 1
Domain157 – 308152Plastocyanin-like 2
Domain418 – 553136Plastocyanin-like 3

Sites

Metal binding791Copper 1; type 2 By similarity
Metal binding811Copper 2; type 3 By similarity
Metal binding1241Copper 2; type 3 By similarity
Metal binding1261Copper 3; type 3 By similarity
Metal binding4701Copper 4; type 1 By similarity
Metal binding4731Copper 1; type 2 By similarity
Metal binding4751Copper 3; type 3 By similarity
Metal binding5321Copper 3; type 3 By similarity
Metal binding5331Copper 4; type 1 By similarity
Metal binding5341Copper 2; type 3 By similarity
Metal binding5381Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation3911N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9LYQ2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DB618A13E0E2881B

FASTA56963,145
        10         20         30         40         50         60 
MEQLRPFFLL LAIFVASLVN AEVHFHEFVI QETPVKRLCR VHNSITVNGQ FPGPTLEVRN 

        70         80         90        100        110        120 
GDSLVITAIN KARYNISLHW HGIRQMRNPW ADGPEYITQC PIQPGGSYTY RFTMEDQEGT 

       130        140        150        160        170        180 
LWWHAHSRWL RATVYGALII RPPLSSPHYP FPVIPKREIT LLLGEWWDRN PMDVLNLAQF 

       190        200        210        220        230        240 
TGAAPNISDA FTINGQPGDL YRCSSQETLR FLVGSGEIVL LRVINSALNQ ELFFGVANHK 

       250        260        270        280        290        300 
LTVVAADASY TKPFSTNVIM LGPGQTTDVL LTADQPPAHY YMAAHAYNSA NAAFDNTTTT 

       310        320        330        340        350        360 
AILKYKDASC VTLQAKSQAR AIPAQLPGFN DTATAAAFTA QMKSPSKVKV PLEIDENLFF 

       370        380        390        400        410        420 
TVGLGLFNCP TPNTQRCQGP NGTRFTASIN NVSFVFPKQN SIMQAYYQGT PTGVFTTDFP 

       430        440        450        460        470        480 
PTPPVTFDYT GNVSRGLWQP TRGTKAYKLK FNSQVQIILQ DTSIVTTENH PMHLHGYEFY 

       490        500        510        520        530        540 
VVGTGVGNFN PNTDTSSFNL IDPPRRNTIG TPPGGWVAIR FVANNPGAWL MHCHIDSHIF 

       550        560 
WGLAMVFLVE NGEGHLQSVQ SPPLDLPQC

« Hide

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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]"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

EMBL
GenBank
DDBJ		AL163652 Genomic DNA. Translation: CAB87269.1.
IPIIPI00521305.
PIRT48484.
RefSeqNP_196330.3.
UniGeneAt.5043

3D structure databases

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

Genome annotation databases

GeneID830604.
GenomeReviewsGene locus AT5G07130 in contig BA000015_GR.
KEGGath:AT5G07130.
NMPDRfig|3702.1.peg.22849.

Organism-specific databases

TAIRAt5g07130.

Phylogenomic databases

eggNOGKOG1263.
HOGENOMHBG749556.
InParanoidQ9LYQ2.
PhylomeDBQ9LYQ2.

Enzyme and pathway databases

BRENDA1.10.3.2. 302.

Gene expression databases

GenevestigatorQ9LYQ2.

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 nameLAC13_ARATH
AccessionPrimary (citable) accession number: Q9LYQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 52 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