Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9FY79 (LAC14_ARATH)

Last modified June 16, 2009. Version 48. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Laccase-14
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 14
    Urishiol oxidase 14
    Diphenol oxidase 14
Gene names
Name: LAC14
Ordered Locus Names: At5g09360
ORF Names: T5E8.160
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

Hide | Top

Protein attributes

Sequence length569 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

Hide | Top

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 at low levels in flowers and siliques. Ref.3

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Hide | Top

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...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 569536Laccase-14
PRO_0000283642

Regions

Domain41 – 157117Plastocyanin-like 1
Domain167 – 320154Plastocyanin-like 2
Domain420 – 553134Plastocyanin-like 3

Sites

Metal binding911Copper 1; type 2 By similarity
Metal binding931Copper 2; type 3 By similarity
Metal binding1361Copper 2; type 3 By similarity
Metal binding1381Copper 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
Metal binding5431Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Glycosylation4301N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict463 – 4697TVWASNI → NVLASDN in ABE66147. Ref.2

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q9FY79-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: FE8E2C1F8A329188

FASTA56964,878
        10         20         30         40         50         60 
MEFKLNIPNT IIKTLQTIVF FLFVLLAFQI AEAEIHHHTF KIKSKAYTRL CNTNKILTVN 

        70         80         90        100        110        120 
GEFPGPTLKA YRGDKLIVNV INNANYNITL HWHGARQIRN PWSDGPEYVT QCPIRPGESY 

       130        140        150        160        170        180 
VYRIDLKVEE GTIWWHAHSQ WARATVHGAF IVYPKRGSSY PFPKPHREIP LILGEWWKKE 

       190        200        210        220        230        240 
NIMHIPGKAN KTGGEPAISD SYTINGQPGY LYPCSKPETF KITVVRGRRY LLRIINAVMD 

       250        260        270        280        290        300 
EELFFAIANH TLTVVAKDGF YLKHFKSDYL MITPGQSMDV LLHANQRPNH YFVAARAYSS 

       310        320        330        340        350        360 
AFGAGFDKTT TTAILQYKGD TLNRIKPILP YLPPYNRTEA STRFTNQFRS QRPVNVPVKI 

       370        380        390        400        410        420 
NTRLLYAISV NLMNCSDDRP CTGPFGKRFS SSINNISFVN PSVDILRAYY RHIGGVFQED 

       430        440        450        460        470        480 
FPRNPPTKFN YTGENLPFPT RFGTKVVVLD YNSSVELILQ GTTVWASNIH PIHLHGYNFY 

       490        500        510        520        530        540 
VVGSGFGNFD RRKDPLRYNL VDPPEETTVG VPRNGWTAVR FVANNPGVWL LHCHIERHAT 

       550        560 
WGMNTVFIVK DGPTKSSRMV KPPPDLPSC

« Hide

Hide | Top

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]"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations."
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.
Plant Biotechnol. J. 4:317-324(2006) [PubMed: 17147637] [Abstract]
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.

Hide | Top

Cross-references

Sequence databases

AL391712 Genomic DNA. Translation: CAC05462.1.
DQ446936 mRNA. Translation: ABE66147.1.
IPIIPI00539110.
RefSeqNP_196498.1.
UniGeneAt.54782

3D structure databases

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

Proteomic databases

PRIDEQ9FY79.

Genome annotation databases

GeneID830795.
GenomeReviewsGene locus AT5G09360 in contig BA000015_GR.
KEGGath:AT5G09360.
NMPDRfig|3702.1.peg.23056.

Organism-specific databases

TAIRAt5g09360.

Phylogenomic databases

OMAQ9FY79. RAYSSAF.

Enzyme and pathway databases

BRENDA1.10.3.2. 302.

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...

Hide | Top

Entry information

Entry nameLAC14_ARATH
AccessionPrimary (citable) accession number: Q9FY79
Secondary accession number(s): Q1PDY2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 1, 2001
Last modified: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Hide | Top

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