ID   LAC17_ARATH             Reviewed;         577 AA.
AC   Q9FJD5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   02-SEP-2026, entry version 139.
DE   RecName: Full=Laccase-17;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 17;
DE   AltName: Full=Diphenol oxidase 17;
DE   AltName: Full=Urishiol oxidase 17;
DE   Flags: Precursor;
GN   Name=LAC17; OrderedLocusNames=At5g60020; ORFNames=MMN10.27;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
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].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- TISSUE SPECIFICITY: Ubiquitous with higher levels in the inflorescence
CC       stem. {ECO:0000269|PubMed:15940465, ECO:0000269|PubMed:16804053}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR   EMBL; AB015475; BAB08370.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97267.1; -; Genomic_DNA.
DR   EMBL; OZ408687; CAO7057181.1; -; Genomic_DNA.
DR   EMBL; BT015359; AAU05482.1; -; mRNA.
DR   EMBL; BT015890; AAU95426.1; -; mRNA.
DR   RefSeq; NP_200810.1; NM_125395.3.
DR   AlphaFoldDB; Q9FJD5; -.
DR   SMR; Q9FJD5; -.
DR   FunCoup; Q9FJD5; 57.
DR   STRING; 3702.Q9FJD5; -.
DR   GlyCosmos; Q9FJD5; 15 sites, No reported glycans.
DR   GlyGen; Q9FJD5; 15 sites.
DR   PaxDb; 3702-Q9FJD5; -.
DR   ProteomicsDB; 237039; -.
DR   GeneID; 836124; -.
DR   KEGG; ath:AT5G60020; -.
DR   Araport; AT5G60020; -.
DR   TAIR; AT5G60020; LAC17.
DR   eggNOG; KOG1263; Eukaryota.
DR   HOGENOM; CLU_006504_6_3_1; -.
DR   InParanoid; Q9FJD5; -.
DR   OrthoDB; 2121828at2759; -.
DR   PhylomeDB; Q9FJD5; -.
DR   BioCyc; ARA:AT5G60020-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G60020-MONOMER; -.
DR   PRO; PR:Q9FJD5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJD5; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; ISM:TAIR.
DR   GO; GO:0009505; C:plant-type cell wall; IDA: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; IMP:TAIR.
DR   GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR   GO; GO:0046274; P:lignin catabolic process; IEA:InterPro.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IMP: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   FunFam; 2.60.40.420:FF:000049; Laccase; 1.
DR   FunFam; 2.60.40.420:FF:000053; Laccase; 1.
DR   FunFam; 2.60.40.420:FF:000062; 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; 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:SF417; LACCASE-17; 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   Apoplast; Copper; Glycoprotein; Lignin degradation; Metal-binding;
KW   Oxidoreductase; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..577
FT                   /note="Laccase-17"
FT                   /id="PRO_0000283645"
FT   DOMAIN          30..146
FT                   /note="Plastocyanin-like 1"
FT   DOMAIN          156..309
FT                   /note="Plastocyanin-like 2"
FT   DOMAIN          427..561
FT                   /note="Plastocyanin-like 3"
FT   BINDING         80
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         82
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         125
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         127
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         478
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         481
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         483
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         540
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         541
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         542
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         546
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        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        391
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        401
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        437
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        450
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        460
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   577 AA;  63958 MW;  1EE10D890EF6D261 CRC64;
     MALQLLLAVF SCVLLLPQPA FGITRHYTLE IKMQNVTRLC HTKSLVSVNG QFPGPKLIAR
     EGDQVLIKVV NQVPNNISLH WHGIRQLRSG WADGPAYITQ CPIQTGQSYV YNYTIVGQRG
     TLWYHAHISW LRSTVYGPLI ILPKRGVPYP FAKPHKEVPM IFGEWFNADT EAIIRQATQT
     GGGPNVSDAY TINGLPGPLY NCSAKDTFRL RVKPGKTYLL RLINAALNDE LFFSIANHTV
     TVVEADAIYV KPFETETILI APGQTTNVLL KTKSSYPSAS FFMTARPYVT GQGTFDNSTV
     AGILEYEPPK QTKGAHSRTS IKNLQLFKPI LPALNDTNFA TKFSNKLRSL NSKNFPANVP
     LNVDRKFFFT VGLGTNPCNH KNNQTCQGPT NTTMFAASIS NISFTMPTKA LLQSHYSGQS
     HGVYSPKFPW SPIVPFNYTG TPPNNTMVSN GTNLMVLPYN TSVELVMQDT SILGAESHPL
     HLHGFNFFVV GQGFGNFDPN KDPRNFNLVD PIERNTVGVP SGGWAAIRFL ADNPGVWFMH
     CHLEVHTSWG LRMAWLVLDG DKPDQKLLPP PADLPKC
//