ID   LAC6_ARATH              Reviewed;         569 AA.
AC   Q9ZPY2; Q8RY28;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   04-NOV-2026, entry version 155.
DE   RecName: Full=Laccase-6;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 6;
DE   AltName: Full=Diphenol oxidase 6;
DE   AltName: Full=Urishiol oxidase 6;
DE   Flags: Precursor;
GN   Name=LAC6; OrderedLocusNames=At2g46570; ORFNames=F13A10.10;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
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   [6]
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ZPY2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ZPY2-2; Sequence=VSP_024345, VSP_024346, VSP_024347;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the inflorescence stem,
CC       but not in siliques. {ECO:0000269|PubMed:15940465,
CC       ECO:0000269|PubMed:16804053}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR   EMBL; AC006418; AAD20177.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10723.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7038973.1; -; Genomic_DNA.
DR   EMBL; AY078937; AAL84943.1; -; mRNA.
DR   PIR; E84904; E84904.
DR   RefSeq; NP_182180.1; NM_130222.2. [Q9ZPY2-1]
DR   AlphaFoldDB; Q9ZPY2; -.
DR   SMR; Q9ZPY2; -.
DR   STRING; 3702.Q9ZPY2; -.
DR   GlyCosmos; Q9ZPY2; 7 sites, No reported glycans.
DR   GlyGen; Q9ZPY2; 7 sites.
DR   PaxDb; 3702-Q9ZPY2; -.
DR   ProteomicsDB; 237145; -. [Q9ZPY2-1]
DR   GeneID; 819269; -.
DR   KEGG; ath:AT2G46570; -.
DR   Araport; AT2G46570; -.
DR   TAIR; AT2G46570; LAC6.
DR   eggNOG; KOG1263; Eukaryota.
DR   HOGENOM; CLU_006504_6_3_1; -.
DR   InParanoid; Q9ZPY2; -.
DR   OMA; AACPKQQ; -.
DR   PhylomeDB; Q9ZPY2; -.
DR   BioCyc; ARA:AT2G46570-MONOMER; -.
DR   PRO; PR:Q9ZPY2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Proteomes; UP001984100; Chromosome 2.
DR   ExpressionAtlas; Q9ZPY2; 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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:InterPro.
DR   GO; GO:0009625; P:response to insect; IEP:TAIR.
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   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; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
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:SF324; LACCASE-6; 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.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoplast; Copper; Glycoprotein; Lignin degradation;
KW   Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..569
FT                   /note="Laccase-6"
FT                   /id="PRO_0000283634"
FT   DOMAIN          37..153
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          163..315
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          417..553
FT                   /note="Plastocyanin-like 3"
FT   BINDING         87
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         89
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         132
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         134
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         472
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         475
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         477
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="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         533
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         534
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         538
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         543
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        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..235
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_024345"
FT   VAR_SEQ         296..327
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_024346"
FT   VAR_SEQ         528..568
FT                   /note="LWLLHCHFDIHQTWGMSTMFIVKNGKKVQESLPHPPADLPK -> ILLHKTP
FT                   KHHNTYDI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_024347"
SQ   SEQUENCE   569 AA;  63901 MW;  3BA02CB6A0C44238 CRC64;
     MTSSAVPSLF RLSFLLFTLQ VMNIGRIGAA TRFYQFKVQT IRLTRLCQTN EIVTVNKKFP
     GPAISAQEDD RIVIKVINMT PYNTTIHWHG IKQKRSCWYD GPSYITQCPI QSGQSFTYNF
     KVAQQKGTFL WHAHFSWLRA TVYGPLIVYP KASVPYPFKK PFNEHTILLG EYWLKNVVEL
     EQHVLESGGP PPPADAFTIN GQPGPNYNCS SKDVYEIQIV PRKIYLLRLI NAGINMETFF
     TIANHRLTIV EVDGEYTKPY TTERVMLVPG QTMNILVTAD QTVGRYSMAM GPYESAKNVK
     FQNTSAIANF QYIGALPNNV TVPAKLPIFN DNIAVKTVMD GLRSLNAVDV PRNIDAHLFI
     TIGLNVNKCN SENPNNKCQG PRKGRLAASM NNISFIEPKV SILEAYYKQL EGYFTLDFPT
     TPEKAYDFVN GAPNDIANDT QAANGTRAIV FEYGSRIQII FQNTGTLTTE NHPIHLHGHS
     FYVIGYGTGN YDQQTAKFNL EDPPYLNTIG VPVGGWAAIR FVANNPGLWL LHCHFDIHQT
     WGMSTMFIVK NGKKVQESLP HPPADLPKC
//