Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q84J37 (LAC15_ARATH)

Last modified November 25, 2008. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-15
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 15
    Urishiol oxidase 15
    Diphenol oxidase 15
    Protein TRANSPARENT TESTA 10
Gene names
Name: TT10
Synonyms: LAC15
Ordered Locus Names: At5g48100
ORF Names: MDN11.18
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 length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Lignin degradation and detoxification of lignin-derived products By similarity. Involved in lignin synthesis in seed coats, in seed coat permeability, in seed germination, and in root elongation. Required for the seed coat (testa) brown pigmentation by mediating the polymerization of proanthocyanidin (tannin) from its monomer precursor epicatechin. Promotes sligthly seed dormancy.

Catalytic activity

4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secreted › extracellular space › apoplastPotential.

Tissue specificity

Mostly expressed in siliques, particularly in developping seeds. Also detected at low levels in stems, seedlings, and flowers.

Developmental stage

Transcript levels increase during rosette leaves development. In the inflorescence stem, highest levels in the young, developing tip and lowest levels in the basal stem tissues. Strong increase 4 days after fertilization. Specifically localized in developping seed coat (testa). Detected in the endothelium and in the pigment strand at the chalaza zone during early stages of embryo morphogenesis. Later, the activity increased and spread to the outer integument, mostly in the oil penultimate cell layer. Strongly expressed in early aborted seeds and in the transmitting tissue of the silique.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Sequence caution

The sequence BAB11074.1 differs from that shown. Reason: Erroneous gene model prediction.

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-KW

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

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 – 2121 Potential
Chain22 – 565544Laccase-15
PRO_0000283643

Regions

Domain27 – 143117Plastocyanin-like 1
Domain153 – 305153Plastocyanin-like 2
Domain408 – 547140Plastocyanin-like 3

Sites

Metal binding771Copper 1; type 2 By similarity
Metal binding791Copper 2; type 3 By similarity
Metal binding1221Copper 2; type 3 By similarity
Metal binding1241Copper 3; type 3 By similarity
Metal binding4621Copper 4; type 1 By similarity
Metal binding4651Copper 1; type 2 By similarity
Metal binding4671Copper 3; type 3 By similarity
Metal binding5261Copper 3; type 3 By similarity
Metal binding5271Copper 4; type 1 By similarity
Metal binding5281Copper 2; type 3 By similarity
Metal binding5321Copper 4; type 1 By similarity
Metal binding5371Copper 4; type 1 By similarity

Amino acid modifications

Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation1821N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2931N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation3721N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential
Glycosylation4181N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1521D → G in tt10-1; transparent testa; when associated with D-509
Mutagenesis5091G → D in tt10-1; transparent testa; when associated with G-152

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q84J37-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: FDBCBE3D6F10DBA4

FASTA56563,994
        10         20         30         40         50         60 
MSHSFFNLFL ISLFLYNNCI AHHYTFTVRE VPYTKLCSTK AILTVNSQFP GPIIKVHKGD 

        70         80         90        100        110        120 
TIYVNVQNRA SENITMHWHG VEQPRNPWSD GPEYITQCPI RPGSDFLYKV IFSIEDTTVW 

       130        140        150        160        170        180 
WHAHSSWTRA TVHGLIFVYP RPPQILPFPK ADHEVPIILG EWWKRDVREV VEEFVRTGGA 

       190        200        210        220        230        240 
PNVSDALTIN GHPGFLYPCS KSDTFHLTVE KGKTYRIRMV NAAMNLPLFF AIANHSLTVV 

       250        260        270        280        290        300 
SADGHYIKPI KATYITISPG ETLDMLLHAD QDPERTYYMA ARAYQSGNID FNNSTTIGIL 

       310        320        330        340        350        360 
SYTSSCKAKT SSFSGYYPTL PFYNDTSAAF GFFTKIKCLF SGQVPVQISR RIITTVSINL 

       370        380        390        400        410        420 
RMCPQNSCEG PNGSRLAASM NNISFVTPSH VDILKAYYYH IKGVYGTRFP EFPPLIFNFT 

       430        440        450        460        470        480 
AENQPLFLET PRLATEVKVI EFGQVVELVI QGTSLVGGGL DHPMHLHGFS FYVVGVGFGN 

       490        500        510        520        530        540 
YNISEEDPSS RYNLYDPPYK NTMTVPRNGW IAIRFVADNP GVWFMHCHLD RHQTWGMNVV 

       550        560 
FIVKNGREPN QQILPPPDDL PPCYE

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.
DNA Res. 6:183-195(1999) [PubMed: 10470850] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"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.
[3]"Mutations affecting the testa colour in Arabidopsis."
Koornneef M.
Arabidopsis Inf. Serv. 27:1-4(1990)
Cited for: FUNCTION.
[4]"Influence of the testa on seed dormancy, germination, and longevity in Arabidopsis."
Debeaujon I., Leon-Kloosterziel K.M., Koornneef M.
Plant Physiol. 122:403-413(2000) [PubMed: 10677433] [Abstract]
Cited for: FUNCTION.
[5]Erratum
Debeaujon I., Leon-Kloosterziel K.M., Koornneef M.
Plant Physiol. 125:1139-1141(2001)
[6]"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, DEVELOPMENTAL STAGE.
[7]"TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat."
Pourcel L., Routaboul J.-M., Kerhoas L., Caboche M., Lepiniec L., Debeaujon I.
Plant Cell 17:2966-2980(2005) [PubMed: 16243908] [Abstract]
Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-152 AND GLY-509.
[8]"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: FUNCTION, TISSUE SPECIFICITY.
[9]"Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation of Arabidopsis."
Liang M., Davis E., Gardner D., Cai X., Wu Y.
Planta 224:1185-1196(2006) [PubMed: 16779554] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.

Hide | Top

Cross-references

Sequence databases

AB017064 Genomic DNA. Translation: BAB11074.1. Sequence problems.
BT002919 mRNA. Translation: AAO22735.1.
BT005152 mRNA. Translation: AAO50685.1.
RefSeqNP_199621.2.
UniGeneAt.9463

3D structure databases

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

Genome annotation databases

GeneID834862.
GenomeReviewsGene locus AT5G48100 in contig BA000015_GR.
KEGGath:AT5G48100.
NMPDRfig|3702.1.peg.26629.

Organism-specific databases

TAIRAt5g48100.

Gene expression databases

ArrayExpressQ84J37.

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]
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameLAC15_ARATH
AccessionPrimary (citable) accession number: Q84J37
Secondary accession number(s): Q9FI28
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 1, 2003
Last modified: November 25, 2008
This is version 39 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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

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