LAC17_ARATH
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 03-AUG-2022, entry version 125.
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 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 [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: 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; 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 STRING; 3702.AT5G60020.1; -.
DR PaxDb; Q9FJD5; -.
DR PRIDE; Q9FJD5; -.
DR ProteomicsDB; 237039; -.
DR EnsemblPlants; AT5G60020.1; AT5G60020.1; AT5G60020.
DR GeneID; 836124; -.
DR Gramene; AT5G60020.1; AT5G60020.1; AT5G60020.
DR KEGG; ath:AT5G60020; -.
DR Araport; AT5G60020; -.
DR TAIR; locus:2168128; AT5G60020.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR InParanoid; Q9FJD5; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9FJD5; -.
DR BioCyc; ARA:AT5G60020-MON; -.
DR BioCyc; MetaCyc:AT5G60020-MON; -.
DR PRO; PR:Q9FJD5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJD5; baseline and differential.
DR Genevisible; Q9FJD5; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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 Gene3D; 2.60.40.420; -; 3.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
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 PANTHER; PTHR11709; PTHR11709; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR TIGRFAMs; TIGR03389; laccase; 1.
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
