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Q9SR40 (LAC7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laccase-7
EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 7
Diphenol oxidase 7
Urishiol oxidase 7
Gene names
Name:LAC7
Ordered Locus Names:At3g09220
ORF Names:F3L24.9
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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 tissues other than the inflorescence stem. Ref.5 Ref.6

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentApoplast
Secreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processlignin catabolic process

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: InterPro

hydroquinone:oxygen oxidoreductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 567544Laccase-7
PRO_0000283635

Regions

Domain31 – 147117Plastocyanin-like 1
Domain157 – 310154Plastocyanin-like 2
Domain412 – 551140Plastocyanin-like 3

Sites

Metal binding811Copper 1; type 2 By similarity
Metal binding831Copper 2; type 3 By similarity
Metal binding1261Copper 2; type 3 By similarity
Metal binding1281Copper 3; type 3 By similarity
Metal binding4681Copper 4; type 1 By similarity
Metal binding4711Copper 1; type 2 By similarity
Metal binding4731Copper 3; type 3 By similarity
Metal binding5301Copper 3; type 3 By similarity
Metal binding5311Copper 4; type 1 By similarity
Metal binding5321Copper 2; type 3 By similarity
Metal binding5361Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation341N-linked (GlcNAc...) Potential
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential
Glycosylation4501N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SR40 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: BA4EFEAA57734D2B

FASTA56762,403
        10         20         30         40         50         60 
MEGVRVPIAC ALILLAISSI TSASIVEHTF NVQNLTVSRL CKRQVITVVN GSLPGPTIRV 

        70         80         90        100        110        120 
KEGDSLVIHV LNHSPHNITI HWHGIFHKLT VWADGPSMIT QCPIQPGQRY AYRFNITGQE 

       130        140        150        160        170        180 
GTLWWHAHAS FLRATVYGAL VIRPKSGHSY PFPKPHKEVP ILFGEWWNTD VVALEEAAIA 

       190        200        210        220        230        240 
TGVPPNNSDA YTINGRPGNL YPCSKDRMFS LNVVKGKRYL LRIINAAMNI QLFFKIANHR 

       250        260        270        280        290        300 
LTVVAADAVY TAPYVTDVIV IAPGQTIDAL LFADQSVDTS YYMAAHPYAS APAVPFPNTT 

       310        320        330        340        350        360 
TRGVIHYGGA SKTGRSKPVL MPKLPSFFDT LTAYRFYSNL TALVNGPHWV PVPRYVDEEM 

       370        380        390        400        410        420 
LVTIGLGLEA CADNTTCPKF SASMSNHSFV LPKKLSILEA VFHDVKGIFT ADFPDQPPVK 

       430        440        450        460        470        480 
FDYTNPNVTQ TNPGLLFTQK STSAKILKFN TTVEVVLQNH ALIAAESHPM HLHGFNFHVL 

       490        500        510        520        530        540 
AQGFGNYDPS RDRSKLNLVD PQSRNTLAVP VGGWAVIRFT ANNPGAWIFH CHIDVHLPFG 

       550        560 
LGMIFVVKNG PTKSTTLPPP PPDLPKC

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. expand/collapse author list , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
Nature 408:820-822(2000) [PubMed: 11130713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed: 11910074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"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.
[6]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AC011436 Genomic DNA. Translation: AAF14041.1.
CP002686 Genomic DNA. Translation: AEE74739.1.
AK117639 mRNA. Translation: BAC42295.1.
BT004971 mRNA. Translation: AAO50504.1.
IPIIPI00528510.
RefSeqNP_187533.1. NM_111756.2.
UniGeneAt.40144.

3D structure databases

HSSPHSSP built from PDB template 1AOZ based on UniProtKB P37064.
ProteinModelPortalQ9SR40.
SMRQ9SR40. Positions 24-567.
ModBaseSearch...

Proteomic databases

PRIDEQ9SR40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G09220.1; AT3G09220.1; AT3G09220.
GeneID820078.
GenomeReviewsGene locus AT3G09220 in contig BA000014_GR.
KEGGath:AT3G09220.
NMPDRfig|3702.1.peg.12936.

Organism-specific databases

TAIRAt3g09220.

Phylogenomic databases

eggNOGKOG1263.
GeneTreeEPGT00050000000260.
HOGENOMHBG749556.
InParanoidQ9SR40.
OMAWHAHASF.
PhylomeDBQ9SR40.
ProtClustDBCLSN2685122.

Gene expression databases

ArrayExpressQ9SR40.
GenevestigatorQ9SR40.

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.
PANTHERPTHR11709:SF9. PTHR11709:SF9. 1 hit.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 3 hits.
TIGRFAMsTIGR03389. Laccase. 1 hit.
PROSITEPS00079. MULTICOPPER_OXIDASE1. False negative.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC7_ARATH
AccessionPrimary (citable) accession number: Q9SR40
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 1, 2000
Last modified: November 16, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents