LAC16_ARATH
ID LAC16_ARATH Reviewed; 566 AA.
AC Q1PDH6; A0MFQ5; F4KGE3; Q3E893;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Laccase-16;
DE EC=1.10.3.2;
DE AltName: Full=Benzenediol:oxygen oxidoreductase 16;
DE AltName: Full=Diphenol oxidase 16;
DE AltName: Full=Urishiol oxidase 16;
DE Flags: Precursor;
GN Name=LAC16; OrderedLocusNames=At5g58910; ORFNames=K19M22.11;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(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] OF 37-566.
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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: Mostly expressed in roots at low level.
CC {ECO:0000269|PubMed:15940465, ECO:0000269|PubMed:16804053}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28766.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=AED97116.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED97116.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM68673.1; -; Genomic_DNA.
DR EMBL; DQ447092; ABE66261.1; -; mRNA.
DR EMBL; DQ653381; ABK28766.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001330401.1; NM_001345329.1.
DR RefSeq; NP_200699.1; NM_125281.1.
DR AlphaFoldDB; Q1PDH6; -.
DR SMR; Q1PDH6; -.
DR STRING; 3702.AT5G58910.1; -.
DR PaxDb; Q1PDH6; -.
DR PRIDE; Q1PDH6; -.
DR ProteomicsDB; 237038; -.
DR EnsemblPlants; AT5G58910.3; AT5G58910.3; AT5G58910.
DR GeneID; 836008; -.
DR Gramene; AT5G58910.3; AT5G58910.3; AT5G58910.
DR KEGG; ath:AT5G58910; -.
DR Araport; AT5G58910; -.
DR TAIR; locus:2154518; AT5G58910.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR InParanoid; Q1PDH6; -.
DR PhylomeDB; Q1PDH6; -.
DR PRO; PR:Q1PDH6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q1PDH6; baseline and differential.
DR Genevisible; Q1PDH6; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..566
FT /note="Laccase-16"
FT /id="PRO_0000283644"
FT DOMAIN 37..150
FT /note="Plastocyanin-like 1"
FT DOMAIN 160..312
FT /note="Plastocyanin-like 2"
FT DOMAIN 414..550
FT /note="Plastocyanin-like 3"
FT BINDING 84
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 86
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 129
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 131
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 467
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 470
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 472
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 529
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 530
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 531
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 535
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 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 566 AA; 62373 MW; 4BCFEEC24628B5FB CRC64;
MEIPRRFCIC VLTFFVFVLL SPTTVHSIIR HYKFNVMTNT TKLCSSKPIV TVNGQFPGPT
IVAREGDTIL IKVVNHVKYN VSIHWHGIRQ LRTGWADGPA YITQCPIQPG QNYLHNFTLT
GQRGTLWWHA HILWLRATVH GAIVILPKLG VPYPFPKPYK EKTIVLSEWW KSDVEELINE
ASRIGTAPSA SDAHTINGHS GSISNCPSQS SYGLPVRAGK TYMLRIINAA LNEELFFKIA
GHVLTVVEVD AVYTKPYKTD TVFIAPGQTT NVLLTANANA GSNYMVAATT FTDAHIPYDN
VTATATLHYI GHTSTVSTSK KTVLASLPPQ NATWVATKFT RSLRSLNSLE YPARVPTTVE
HSLFFTVGLG ANPCQSCNNG VRLVAGINNV TFTMPKTALL QAHFFNISGV FTDDFPAKPS
NPYDYTAPVK LGVNAATMKG TKLYRLPYNA TVQIVLQNTA MILSDNHPFH LHGFNFFEVG
RGLGNFNPEK DPKAFNLVDP VERNTVGVPA GGWTAIRFIA DNPGVWFMHC HLELHTTWGL
KMAFVVDNGH GPDQSLLPPP ADLPKC
