Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9SR40

- LAC7_ARATH

UniProt

Q9SR40 - LAC7_ARATH

Protein

Laccase-7

Gene

LAC7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Lignin degradation and detoxification of lignin-derived products.By similarity

    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 bindingi81 – 811Copper 1; type 2By similarity
    Metal bindingi83 – 831Copper 2; type 3By similarity
    Metal bindingi126 – 1261Copper 2; type 3By similarity
    Metal bindingi128 – 1281Copper 3; type 3By similarity
    Metal bindingi468 – 4681Copper 4; type 1By similarity
    Metal bindingi471 – 4711Copper 1; type 2By similarity
    Metal bindingi473 – 4731Copper 3; type 3By similarity
    Metal bindingi530 – 5301Copper 3; type 3By similarity
    Metal bindingi531 – 5311Copper 4; type 1By similarity
    Metal bindingi532 – 5321Copper 2; type 3By similarity
    Metal bindingi536 – 5361Copper 4; type 1By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. lignin catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Lignin degradation

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G09220-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laccase-7 (EC:1.10.3.2)
    Alternative name(s):
    Benzenediol:oxygen oxidoreductase 7
    Diphenol oxidase 7
    Urishiol oxidase 7
    Gene namesi
    Name:LAC7
    Ordered Locus Names:At3g09220
    ORF Names:F3L24.9
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G09220.

    Subcellular locationi

    GO - Cellular componenti

    1. apoplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Apoplast, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 567544Laccase-7PRO_0000283635Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi386 – 3861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi427 – 4271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi450 – 4501N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9SR40.
    PRIDEiQ9SR40.

    Expressioni

    Tissue specificityi

    Predominantly expressed in tissues other than the inflorescence stem.2 Publications

    Gene expression databases

    GenevestigatoriQ9SR40.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT3G09220.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SR40.
    SMRiQ9SR40. Positions 23-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 147117Plastocyanin-like 1Add
    BLAST
    Domaini157 – 310154Plastocyanin-like 2Add
    BLAST
    Domaini412 – 551140Plastocyanin-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.
    InParanoidiQ9SR40.
    OMAiWHAHASF.
    PhylomeDBiQ9SR40.

    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.
    PROSITEiPS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9SR40-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGVRVPIAC ALILLAISSI TSASIVEHTF NVQNLTVSRL CKRQVITVVN    50
    GSLPGPTIRV KEGDSLVIHV LNHSPHNITI HWHGIFHKLT VWADGPSMIT 100
    QCPIQPGQRY AYRFNITGQE GTLWWHAHAS FLRATVYGAL VIRPKSGHSY 150
    PFPKPHKEVP ILFGEWWNTD VVALEEAAIA TGVPPNNSDA YTINGRPGNL 200
    YPCSKDRMFS LNVVKGKRYL LRIINAAMNI QLFFKIANHR LTVVAADAVY 250
    TAPYVTDVIV IAPGQTIDAL LFADQSVDTS YYMAAHPYAS APAVPFPNTT 300
    TRGVIHYGGA SKTGRSKPVL MPKLPSFFDT LTAYRFYSNL TALVNGPHWV 350
    PVPRYVDEEM LVTIGLGLEA CADNTTCPKF SASMSNHSFV LPKKLSILEA 400
    VFHDVKGIFT ADFPDQPPVK FDYTNPNVTQ TNPGLLFTQK STSAKILKFN 450
    TTVEVVLQNH ALIAAESHPM HLHGFNFHVL AQGFGNYDPS RDRSKLNLVD 500
    PQSRNTLAVP VGGWAVIRFT ANNPGAWIFH CHIDVHLPFG LGMIFVVKNG 550
    PTKSTTLPPP PPDLPKC 567
    Length:567
    Mass (Da):62,403
    Last modified:May 1, 2000 - v1
    Checksum:iBA4EFEAA57734D2B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC011436 Genomic DNA. Translation: AAF14041.1.
    CP002686 Genomic DNA. Translation: AEE74739.1.
    AK117639 mRNA. Translation: BAC42295.1.
    BT004971 mRNA. Translation: AAO50504.1.
    RefSeqiNP_187533.1. NM_111756.2.
    UniGeneiAt.40144.

    Genome annotation databases

    EnsemblPlantsiAT3G09220.1; AT3G09220.1; AT3G09220.
    GeneIDi820078.
    KEGGiath:AT3G09220.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC011436 Genomic DNA. Translation: AAF14041.1 .
    CP002686 Genomic DNA. Translation: AEE74739.1 .
    AK117639 mRNA. Translation: BAC42295.1 .
    BT004971 mRNA. Translation: AAO50504.1 .
    RefSeqi NP_187533.1. NM_111756.2.
    UniGenei At.40144.

    3D structure databases

    ProteinModelPortali Q9SR40.
    SMRi Q9SR40. Positions 23-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT3G09220.1-P.

    Proteomic databases

    PaxDbi Q9SR40.
    PRIDEi Q9SR40.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G09220.1 ; AT3G09220.1 ; AT3G09220 .
    GeneIDi 820078.
    KEGGi ath:AT3G09220.

    Organism-specific databases

    TAIRi AT3G09220.

    Phylogenomic databases

    eggNOGi COG2132.
    HOGENOMi HOG000241916.
    InParanoidi Q9SR40.
    OMAi WHAHASF.
    PhylomeDBi Q9SR40.

    Enzyme and pathway databases

    BioCyci ARA:AT3G09220-MONOMER.

    Gene expression databases

    Genevestigatori Q9SR40.

    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 PS00080. MULTICOPPER_OXIDASE2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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] [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. 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.
      , 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.
    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiLAC7_ARATH
    AccessioniPrimary (citable) accession number: Q9SR40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 94 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