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UniProtKB/Swiss-Prot entry Q84J37


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LAC15_ARATH
Primary accession number Q84J37
Secondary accession number Q9FI28
Integrated into Swiss-Prot on April 3, 2007
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 38)
Name and origin of the protein
Protein name Laccase-15 [Precursor]
Synonyms EC 1.10.3.2
Benzenediol:oxygen oxidoreductase 15
Urishiol oxidase 15
Diphenol oxidase 15
Protein TRANSPARENT TESTA 10
Gene name
Name: TT10
Synonyms: LAC15
OrderedLocusNames: At5g48100
ORFNames: MDN11.18
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1093/dnares/6.3.183; PubMed=10470850 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.;
"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.";
DNA Res. 6:183-195(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[3]
FUNCTION.
Koornneef M.;
"Mutations affecting the testa colour in Arabidopsis.";
Arabidopsis Inf. Serv. 27:1-4(1990).
[4]
FUNCTION.
DOI=10.1104/pp.122.2.403; PubMed=10677433 [NCBI, ExPASy, EBI, Israel, Japan]
Debeaujon I., Leon-Kloosterziel K.M., Koornneef M.;
"Influence of the testa on seed dormancy, germination, and longevity in Arabidopsis.";
Plant Physiol. 122:403-413(2000).
[5]
ERRATUM.
Debeaujon I., Leon-Kloosterziel K.M., Koornneef M.;
Plant Physiol. 125:1139-1141(2001).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
DOI=10.1007/s00425-004-1472-6; PubMed=15940465 [NCBI, ExPASy, EBI, Israel, Japan]
McCaig B.C., Meagher R.B., Dean J.F.D.;
"Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana.";
Planta 221:619-636(2005).
[7]
FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-152 AND GLY-509.
DOI=10.1105/tpc.105.035154; PubMed=16243908 [NCBI, ExPASy, EBI, Israel, Japan]
Pourcel L., Routaboul J.-M., Kerhoas L., Caboche M., Lepiniec L., Debeaujon I.;
"TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative polymerization of flavonoids in Arabidopsis seed coat.";
Plant Cell 17:2966-2980(2005).
[8]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1093/jxb/erl022; PubMed=16804053 [NCBI, ExPASy, EBI, Israel, Japan]
Cai X., Davis E.J., Ballif J., Liang M., Bushman E., Haroldsen V., Torabinejad J., Wu Y.;
"Mutant identification and characterization of the laccase gene family in Arabidopsis.";
J. Exp. Bot. 57:2563-2569(2006).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1007/s00425-006-0300-6; PubMed=16779554 [NCBI, ExPASy, EBI, Israel, Japan]
Liang M., Davis E., Gardner D., Cai X., Wu Y.;
"Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation of Arabidopsis.";
Planta 224:1185-1196(2006).
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 + O2 = 4 benzosemiquinone + 2 H2O.
  • COFACTOR: Binds 4 copper ions per monomer (By similarity).
  • SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast (Potential).
  • 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.
  • SIMILARITY: Belongs to the multicopper oxidase family.
  • SIMILARITY: Contains 3 plastocyanin-like domains.
  • SEQUENCE CAUTION:
    • Sequence=BAB11074.1; Type=Erroneous gene model prediction;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB017064; BAB11074.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT002919; AAO22735.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT005152; AAO50685.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_199621.2; -.
UniGene At.9463
3D structure databases
HSSP P37064; 1AOZ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q84J37.
Organism-specific databases
TAIR At5g48100; -.
Gene expression databases
ArrayExpress Q84J37; -.
Ontologies
GO
GO:0048046; Cellular component: apoplast (inferred from electronic annotation from UniProtKB-KW).
GO:0008471; Molecular function: laccase activity (inferred from electronic annotation from EC).
GO:0046274; Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
IPR017761; Laccase.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.420; Cupredoxin; 3.
Pfam PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.
PROSITE PS00079; MULTICOPPER_OXIDASE1; 1.
PS00080; MULTICOPPER_OXIDASE2; 1.
BLOCKS Q84J37.
ProtoNet Q84J37.
Genome annotation databases
GeneID 834862; -.
GenomeReviews BA000015_GR; AT5G48100.
KEGG ath:AT5G48100; -.
NMPDR fig|3702.1.peg.26629; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoplast; Complete proteome; Copper; Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    21  21     Potential. 
CHAIN   22   565  544     Laccase-15. PRO_0000283643
DOMAIN   27   143  117     Plastocyanin-like 1. 
DOMAIN   153   305  153     Plastocyanin-like 2. 
DOMAIN   408   547  140     Plastocyanin-like 3. 
METAL   77    77        Copper 1; type 2 (By similarity). 
METAL   79    79        Copper 2; type 3 (By similarity). 
METAL   122   122        Copper 2; type 3 (By similarity). 
METAL   124   124        Copper 3; type 3 (By similarity). 
METAL   462   462        Copper 4; type 1 (By similarity). 
METAL   465   465        Copper 1; type 2 (By similarity). 
METAL   467   467        Copper 3; type 3 (By similarity). 
METAL   526   526        Copper 3; type 3 (By similarity). 
METAL   527   527        Copper 4; type 1 (By similarity). 
METAL   528   528        Copper 2; type 3 (By similarity). 
METAL   532   532        Copper 4; type 1 (By similarity). 
METAL   537   537        Copper 4; type 1 (By similarity). 
CARBOHYD   73    73        N-linked (GlcNAc...) (Potential). 
CARBOHYD   182   182        N-linked (GlcNAc...) (Potential). 
CARBOHYD   234   234        N-linked (GlcNAc...) (Potential). 
CARBOHYD   293   293        N-linked (GlcNAc...) (Potential). 
CARBOHYD   324   324        N-linked (GlcNAc...) (Potential). 
CARBOHYD   372   372        N-linked (GlcNAc...) (Potential). 
CARBOHYD   382   382        N-linked (GlcNAc...) (Potential). 
CARBOHYD   418   418        N-linked (GlcNAc...) (Potential). 
CARBOHYD   482   482        N-linked (GlcNAc...) (Potential). 
MUTAGEN   152   152        D->G: In tt10-1; transparent testa; when associated with D-509. 
MUTAGEN   509   509        G->D: In tt10-1; transparent testa; when associated with G-152. 
Sequence information
Length: 565 AA [This is the length of the unprocessed precursor] Molecular weight: 63994 Da [This is the MW of the unprocessed precursor] CRC64: FDBCBE3D6F10DBA4 [This is a checksum on the sequence]
        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 

Q84J37 in FASTA format

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