ID   LAC9_ARATH              Reviewed;         586 AA.
AC   Q9LFD1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   02-SEP-2026, entry version 136.
DE   RecName: Full=Laccase-9;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 9;
DE   AltName: Full=Diphenol oxidase 9;
DE   AltName: Full=Urishiol oxidase 9;
DE   Flags: Precursor;
GN   Name=LAC9; OrderedLocusNames=At5g01050; ORFNames=F7J8.30;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15940465; DOI=10.1007/s00425-004-1472-6;
RA   McCaig B.C., Meagher R.B., Dean J.F.D.;
RT   "Gene structure and molecular analysis of the laccase-like multicopper
RT   oxidase (LMCO) gene family in Arabidopsis thaliana.";
RL   Planta 221:619-636(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16804053; DOI=10.1093/jxb/erl022;
RA   Cai X., Davis E.J., Ballif J., Liang M., Bushman E., Haroldsen V.,
RA   Torabinejad J., Wu Y.;
RT   "Mutant identification and characterization of the laccase gene family in
RT   Arabidopsis.";
RL   J. Exp. Bot. 57:2563-2569(2006).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 hydroquinone + O2 = 4 benzosemiquinone + 2 H2O;
CC         Xref=Rhea:RHEA:11276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17594, ChEBI:CHEBI:17977; EC=1.10.3.2;
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC       Note=Binds 4 Cu cations per monomer. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in roots.
CC       {ECO:0000269|PubMed:15940465, ECO:0000269|PubMed:16804053}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR   EMBL; AL137189; CAB69833.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90292.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7050580.1; -; Genomic_DNA.
DR   PIR; T45945; T45945.
DR   RefSeq; NP_195725.1; NM_120182.3.
DR   AlphaFoldDB; Q9LFD1; -.
DR   SMR; Q9LFD1; -.
DR   STRING; 3702.Q9LFD1; -.
DR   GlyCosmos; Q9LFD1; 9 sites, No reported glycans.
DR   GlyGen; Q9LFD1; 9 sites.
DR   PaxDb; 3702-Q9LFD1; -.
DR   GeneID; 831812; -.
DR   KEGG; ath:AT5G01050; -.
DR   Araport; AT5G01050; -.
DR   TAIR; AT5G01050; -.
DR   eggNOG; KOG1263; Eukaryota.
DR   HOGENOM; CLU_006504_6_3_1; -.
DR   InParanoid; Q9LFD1; -.
DR   OMA; LYYMTIS; -.
DR   PhylomeDB; Q9LFD1; -.
DR   BioCyc; ARA:AT5G01050-MONOMER; -.
DR   PRO; PR:Q9LFD1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFD1; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; ISM:TAIR.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:InterPro.
DR   CDD; cd13849; CuRO_1_LCC_plant; 1.
DR   CDD; cd13875; CuRO_2_LCC_plant; 1.
DR   CDD; cd13897; CuRO_3_LCC_plant; 1.
DR   FunFam; 2.60.40.420:FF:000135; Laccase; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR001117; Cu-oxidase_2nd.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034288; CuRO_1_LCC.
DR   InterPro; IPR034285; CuRO_2_LCC.
DR   InterPro; IPR034289; CuRO_3_LCC.
DR   InterPro; IPR017761; Laccase.
DR   NCBIfam; TIGR03389; laccase; 1.
DR   PANTHER; PTHR11709:SF251; LACCASE-8-RELATED; 1.
DR   PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 3.
PE   2: Evidence at transcript level;
KW   Apoplast; Copper; Glycoprotein; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..586
FT                   /note="Laccase-9"
FT                   /id="PRO_0000283637"
FT   DOMAIN          33..149
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          159..307
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          411..552
FT                   /note="Plastocyanin-like 3"
FT   BINDING         83
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 2 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         130
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         469
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         472
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 2 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         474
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         531
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         532
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         533
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        79
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        451
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   586 AA;  65589 MW;  84FFF22C99A35451 CRC64;
     MPRVHHSLSN QAFLVLLLFS SIASAAIVEH VLHVKDVVVT PLCKEQMIPI VNGSLPGPTI
     NVREGDTLVV HVINKSTYNV TIHWHGVFQL KSVWMDGANM ITQCPIQPSN NFTYQFDITG
     QEGTLLWHAH VVNLRATIHG ALIIRPRSGR PYPFPKPYKE VPLIFQQWWD TDVRLLELRP
     APVSDAYLIN GLAGDSYPCS KNRMFNLKVV QGKTYLLRII NAALNTHLFF KIANHNVTVV
     AVDAVYTTPY LTDVMILTPG QTIDAILTAD QPIGTYYMAI IPYFSAIGVP ASPDTKPTRG
     LIVYEGATSS SSPTKPWMPP ANDIPTAHRF SSNITSLVGG PHWTPVPRHV DEKMFITMGL
     GLDPCPSNAK CVGPLDQRLA GSLNNRTFMI PERISMQEAY FYNITGVYTD DFPDQPPLKF
     DFTKFEQHPT NSDMEMMFPE RKTSVKTIRF NSTVEIVLQN TGILTPESHP MHLHGFNFYV
     LGYGFGNYDP IRDARKLNLF NPQMHNTVGV PPGGWVVLRF IANNPGIWLF HCHMDAHLPL
     GIMMAFIVQN GPTRETSLPS PPSNLPQCTR DPTIYDSRTT NVDMSY
//