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Reviewed, UniProtKB/Swiss-Prot Q9LMS3 (LAC1_ARATH)

Last modified November 3, 2009. Version 53. 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-1
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 1
    Urishiol oxidase 1
    Diphenol oxidase 1
Gene names
Name: LAC1
Ordered Locus Names: At1g18140
ORF Names: T10F20.14, T10O22.11
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 length581 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

Expressed in roots, stems and flowers. Ref.3

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Sequence caution

The sequence AAF78389.1 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-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 – 581556Laccase-1
PRO_0000283629

Regions

Domain34 – 150117Plastocyanin-like 1
Domain161 – 312152Plastocyanin-like 2
Domain429 – 565137Plastocyanin-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 binding4821Copper 4; type 1 By similarity
Metal binding4851Copper 1; type 2 By similarity
Metal binding4871Copper 3; type 3 By similarity
Metal binding5441Copper 3; type 3 By similarity
Metal binding5451Copper 4; type 1 By similarity
Metal binding5461Copper 2; type 3 By similarity
Metal binding5501Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9LMS3-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EE2071A7673C28AD

FASTA58165,229
        10         20         30         40         50         60 
MENLGFLIIS TFLLLFTTLL PYSSASTTRR FHFNVEWKKV TRLCHTKQLL TVNGQYPGPT 

        70         80         90        100        110        120 
VAVHEGDIVE IKVTNRIAHN TTIHWHGLRQ YRTGWADGPA YITQCPIRSK QSYTYRFKVE 

       130        140        150        160        170        180 
DQRGTLLWHA HHSWQRASVY GAFIIYPRQP YPFSGSHIQS EIPIILGEWW NDDVDNVEKA 

       190        200        210        220        230        240 
MMKTGAGAKV SDAYTLNGLP GPLYPCSTKD TFTATVDAGK TYILRIINAA LNNELFVAVA 

       250        260        270        280        290        300 
NHTLTVVEVD AVYTKPVHTK AIMIAPGQTT TLLLRADQLS GGEFLIAATP YVTSVFPFNN 

       310        320        330        340        350        360 
STTVGFIRYT GKTKPENSVN TRRRRRLTAM STVVALPNML DTKFATKFSD SIKSLGSAKY 

       370        380        390        400        410        420 
PCKVPTKIDK RVITTISLNL QDCPLNQTCD GYAGKRFFAS MNNISFVRPP ISILESYYKK 

       430        440        450        460        470        480 
QSKGVFSLDF PEKPPNRFDF TGVDPVSENM NTEFGTKLFE VEFGSRLEIV FQGTSFLNIE 

       490        500        510        520        530        540 
NHPLHVHGHN FFVVGRGFGN FDPEKDPKRY NLVDPPERNT FAVPTGGWAA IRINADNPGV 

       550        560        570        580 
WFIHCHLEQH TSWGLAMGFI VKDGPLPSQT LLPPPHDLPQ C

« Hide

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References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed: 11130712] [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 (JUL-2006) 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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AC034107 Genomic DNA. Translation: AAF97830.1.
AC069551 Genomic DNA. Translation: AAF78389.1. Sequence problems.
AK227320 mRNA. Translation: BAE99334.1.
IPIIPI00527099.
PIRE86316.
RefSeqNP_173252.2.
UniGeneAt.41805

3D structure databases

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

Proteomic databases

PRIDEQ9LMS3.

Genome annotation databases

GeneID838393.
GenomeReviewsGene locus AT1G18140 in contig CT485782_GR.
KEGGath:AT1G18140.
NMPDRfig|3702.1.peg.2146.

Organism-specific databases

TAIRAt1g18140.

Phylogenomic databases

OMAGEWWNDD.

Enzyme and pathway databases

BRENDA1.10.3.2. 302.

Gene expression databases

GenevestigatorQ9LMS3.

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 nameLAC1_ARATH
AccessionPrimary (citable) accession number: Q9LMS3
Secondary accession number(s): Q9LM34
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 53 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