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Reviewed, UniProtKB/Swiss-Prot Q9FLB5 (LAC12_ARATH)

Last modified February 9, 2010. Version 55. 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-12
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 12
    Urishiol oxidase 12
    Diphenol oxidase 12
Gene names
Name: LAC12
Ordered Locus Names: At5g05390
ORF Names: K18I23.20
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 length565 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

Predominantly expressed in the inflorescence stem. Ref.2 Ref.3

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 – 2424 Potential
Chain25 – 565541Laccase-12
PRO_0000283640

Regions

Domain32 – 148117Plastocyanin-like 1
Domain158 – 310153Plastocyanin-like 2
Domain413 – 549137Plastocyanin-like 3

Sites

Metal binding821Copper 1; type 2 By similarity
Metal binding841Copper 2; type 3 By similarity
Metal binding1271Copper 2; type 3 By similarity
Metal binding1291Copper 3; type 3 By similarity
Metal binding4661Copper 4; type 1 By similarity
Metal binding4691Copper 1; type 2 By similarity
Metal binding4711Copper 3; type 3 By similarity
Metal binding5281Copper 3; type 3 By similarity
Metal binding5291Copper 4; type 1 By similarity
Metal binding5301Copper 2; type 3 By similarity
Metal binding5341Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
Q9FLB5-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 15DA9DDD5CA8932E

FASTA56562,734
        10         20         30         40         50         60 
MTTVHTFSIL LFFCSLFSAS LIIAKVQHHD FVIQETPVKR LCKTRNAITV NGMFPGPTLE 

        70         80         90        100        110        120 
VNNGDTLEVK VHNRARYNIT IHWHGVRQIR TGWADGPEFV TQCPIRPGKS YTYRFTIQGQ 

       130        140        150        160        170        180 
EGTLWWHAHS SWLRATVYGA LIIHPTPGSS FPFPKPDRQT ALMLGEWWNA NPVDVINQAT 

       190        200        210        220        230        240 
RTGAAPNISD AYTINGQPGD LYNCSTKETV VVPINSGETS LLRVINAALN QPLFFTVANH 

       250        260        270        280        290        300 
KLTVVGADAS YLKPFTTKVL MLGPGQTTDV LLTADQPPKR YYIAARAYQS AQNAPFDNTT 

       310        320        330        340        350        360 
TTAILQYKKT TTTSKPIMPV LPAFNDTNTV TSFSRKFKSL RNVVVPKTID DNLFFTIGLG 

       370        380        390        400        410        420 
LDNCPKKFPK SRCQGLNGTR FTASMNNVSF VLPSNFSLLQ AHSNGIPGVF TTDFPSKPPV 

       430        440        450        460        470        480 
KFDYTGNNIS RALFQPVKGT KLYKLKYGSR VQVVLQDTNI VTSENHPIHL HGYDFYIVGE 

       490        500        510        520        530        540 
GFGNFNPKKD TSKFNLVDPP LRNTVAVPVN GWAVIRFVAD NPGVWLMHCH LDVHIKWGLA 

       550        560 
MAFLVDNGVG ELETLEAPPH DLPIC

« Hide

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References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
DNA Res. 5:131-145(1998) [PubMed: 9679202] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[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

EMBL
GenBank
DDBJ		AB010692 Genomic DNA. Translation: BAB09982.1.
IPIIPI00530693.
RefSeqNP_196158.1.
UniGeneAt.54730

3D structure databases

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

Genome annotation databases

GeneID830421.
GenomeReviewsGene locus AT5G05390 in contig BA000015_GR.
KEGGath:AT5G05390.
NMPDRfig|3702.1.peg.22645.

Organism-specific databases

TAIRAt5g05390.

Phylogenomic databases

eggNOGKOG1263.
HOGENOMHBG749556.
InParanoidQ9FLB5.
OMADLETHEA.
PhylomeDBQ9FLB5.

Enzyme and pathway databases

BRENDA1.10.3.2. 302.

Gene expression databases

GenevestigatorQ9FLB5.

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 nameLAC12_ARATH
AccessionPrimary (citable) accession number: Q9FLB5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2001
Last modified: February 9, 2010
This is version 55 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