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Q84J37

- LAC15_ARATH

UniProt

Q84J37 - LAC15_ARATH

Protein

Laccase-15

Gene

TT10

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    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.By similarity5 Publications

    Catalytic activityi

    4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

    Cofactori

    Binds 4 copper ions per monomer.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi77 – 771Copper 1; type 2By similarity
    Metal bindingi79 – 791Copper 2; type 3By similarity
    Metal bindingi122 – 1221Copper 2; type 3By similarity
    Metal bindingi124 – 1241Copper 3; type 3By similarity
    Metal bindingi462 – 4621Copper 4; type 1By similarity
    Metal bindingi465 – 4651Copper 1; type 2By similarity
    Metal bindingi467 – 4671Copper 3; type 3By similarity
    Metal bindingi526 – 5261Copper 3; type 3By similarity
    Metal bindingi527 – 5271Copper 4; type 1By similarity
    Metal bindingi528 – 5281Copper 2; type 3By similarity
    Metal bindingi532 – 5321Copper 4; type 1By similarity
    Metal bindingi537 – 5371Copper 4; type 1By similarity

    GO - Molecular functioni

    1. copper ion binding Source: TAIR
    2. hydroquinone:oxygen oxidoreductase activity Source: UniProtKB-EC

    GO - Biological processi

    1. lignin biosynthetic process Source: TAIR
    2. lignin catabolic process Source: UniProtKB-KW
    3. proanthocyanidin biosynthetic process Source: TAIR
    4. response to copper ion Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin degradation

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G48100-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laccase-15 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase 15
    Diphenol oxidase 15
    Protein TRANSPARENT TESTA 10
    Urishiol oxidase 15
    Gene namesi
    Name:TT10
    Synonyms:LAC15
    Ordered Locus Names:At5g48100
    ORF Names:MDN11.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G48100.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apoplast, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi152 – 1521D → G in tt10-1; transparent testa; when associated with D-509. 1 Publication
    Mutagenesisi509 – 5091G → D in tt10-1; transparent testa; when associated with G-152. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 565544Laccase-15PRO_0000283643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi372 – 3721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ84J37.
    PRIDEiQ84J37.

    Expressioni

    Tissue specificityi

    Mostly expressed in siliques, particularly in developing seeds. Also detected at low levels in stems, seedlings, and flowers.4 Publications

    Developmental stagei

    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 developing 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.2 Publications

    Gene expression databases

    GenevestigatoriQ84J37.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT5G48100.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ84J37.
    SMRiQ84J37. Positions 23-553.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 143117Plastocyanin-like 1Add
    BLAST
    Domaini153 – 305153Plastocyanin-like 2Add
    BLAST
    Domaini408 – 547140Plastocyanin-like 3Add
    BLAST

    Sequence similaritiesi

    Belongs to the multicopper oxidase family.Curated
    Contains 3 plastocyanin-like domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2132.
    HOGENOMiHOG000241916.
    InParanoidiQ84J37.
    OMAiASENITM.
    PhylomeDBiQ84J37.

    Family and domain databases

    Gene3Di2.60.40.420. 3 hits.
    InterProiIPR001117. Cu-oxidase.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    IPR017761. Laccase.
    [Graphical view]
    PfamiPF00394. Cu-oxidase. 1 hit.
    PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49503. SSF49503. 4 hits.
    TIGRFAMsiTIGR03389. laccase. 1 hit.
    PROSITEiPS00079. MULTICOPPER_OXIDASE1. 1 hit.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q84J37-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHSFFNLFL ISLFLYNNCI AHHYTFTVRE VPYTKLCSTK AILTVNSQFP    50
    GPIIKVHKGD TIYVNVQNRA SENITMHWHG VEQPRNPWSD GPEYITQCPI 100
    RPGSDFLYKV IFSIEDTTVW WHAHSSWTRA TVHGLIFVYP RPPQILPFPK 150
    ADHEVPIILG EWWKRDVREV VEEFVRTGGA PNVSDALTIN GHPGFLYPCS 200
    KSDTFHLTVE KGKTYRIRMV NAAMNLPLFF AIANHSLTVV SADGHYIKPI 250
    KATYITISPG ETLDMLLHAD QDPERTYYMA ARAYQSGNID FNNSTTIGIL 300
    SYTSSCKAKT SSFSGYYPTL PFYNDTSAAF GFFTKIKCLF SGQVPVQISR 350
    RIITTVSINL RMCPQNSCEG PNGSRLAASM NNISFVTPSH VDILKAYYYH 400
    IKGVYGTRFP EFPPLIFNFT AENQPLFLET PRLATEVKVI EFGQVVELVI 450
    QGTSLVGGGL DHPMHLHGFS FYVVGVGFGN YNISEEDPSS RYNLYDPPYK 500
    NTMTVPRNGW IAIRFVADNP GVWFMHCHLD RHQTWGMNVV FIVKNGREPN 550
    QQILPPPDDL PPCYE 565
    Length:565
    Mass (Da):63,994
    Last modified:June 1, 2003 - v1
    Checksum:iFDBCBE3D6F10DBA4
    GO

    Sequence cautioni

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017064 Genomic DNA. Translation: BAB11074.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED95619.1.
    BT002919 mRNA. Translation: AAO22735.1.
    BT005152 mRNA. Translation: AAO50685.1.
    RefSeqiNP_199621.2. NM_124184.2.
    UniGeneiAt.9463.

    Genome annotation databases

    EnsemblPlantsiAT5G48100.1; AT5G48100.1; AT5G48100.
    GeneIDi834862.
    KEGGiath:AT5G48100.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017064 Genomic DNA. Translation: BAB11074.1 . Sequence problems.
    CP002688 Genomic DNA. Translation: AED95619.1 .
    BT002919 mRNA. Translation: AAO22735.1 .
    BT005152 mRNA. Translation: AAO50685.1 .
    RefSeqi NP_199621.2. NM_124184.2.
    UniGenei At.9463.

    3D structure databases

    ProteinModelPortali Q84J37.
    SMRi Q84J37. Positions 23-553.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT5G48100.1-P.

    Proteomic databases

    PaxDbi Q84J37.
    PRIDEi Q84J37.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G48100.1 ; AT5G48100.1 ; AT5G48100 .
    GeneIDi 834862.
    KEGGi ath:AT5G48100.

    Organism-specific databases

    TAIRi AT5G48100.

    Phylogenomic databases

    eggNOGi COG2132.
    HOGENOMi HOG000241916.
    InParanoidi Q84J37.
    OMAi ASENITM.
    PhylomeDBi Q84J37.

    Enzyme and pathway databases

    BioCyci ARA:AT5G48100-MONOMER.

    Gene expression databases

    Genevestigatori Q84J37.

    Family and domain databases

    Gene3Di 2.60.40.420. 3 hits.
    InterProi IPR001117. Cu-oxidase.
    IPR011706. Cu-oxidase_2.
    IPR011707. Cu-oxidase_3.
    IPR002355. Cu_oxidase_Cu_BS.
    IPR008972. Cupredoxin.
    IPR017761. Laccase.
    [Graphical view ]
    Pfami PF00394. Cu-oxidase. 1 hit.
    PF07731. Cu-oxidase_2. 1 hit.
    PF07732. Cu-oxidase_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49503. SSF49503. 4 hits.
    TIGRFAMsi TIGR03389. laccase. 1 hit.
    PROSITEi PS00079. MULTICOPPER_OXIDASE1. 1 hit.
    PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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. "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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "Mutations affecting the testa colour in Arabidopsis."
      Koornneef M.
      Arabidopsis Inf. Serv. 27:1-4(1990)
      Cited for: FUNCTION.
    5. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. Erratum
      Debeaujon I., Leon-Kloosterziel K.M., Koornneef M.
      Plant Physiol. 125:1139-1141(2001)
    7. "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] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    8. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, MUTAGENESIS OF ASP-152 AND GLY-509.
    9. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
      Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
      Plant Physiol. Biochem. 0:0-0(2013)
      Cited for: REVIEW, NOMENCLATURE.

    Entry informationi

    Entry nameiLAC15_ARATH
    AccessioniPrimary (citable) accession number: Q84J37
    Secondary accession number(s): Q9FI28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3