LAC5_ARATH
ID LAC5_ARATH Reviewed; 580 AA.
AC Q9SIY8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Laccase-5;
DE EC=1.10.3.2;
DE AltName: Full=Benzenediol:oxygen oxidoreductase 5;
DE AltName: Full=Diphenol oxidase 5;
DE AltName: Full=Urishiol oxidase 5;
DE Flags: Precursor;
GN Name=LAC5; Synonyms=LAC1; OrderedLocusNames=At2g40370; ORFNames=T3G21.14;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Gaynor J.J.;
RT "Molecular cloning, characterization, and expression of a cDNA clone
RT encoding laccase from Arabidopsis thaliana.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [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 and constitutive.
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; AF506030; AAM77221.1; -; mRNA.
DR EMBL; AC007020; AAD25671.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09819.1; -; Genomic_DNA.
DR PIR; F84828; F84828.
DR RefSeq; NP_181568.1; NM_129597.4.
DR AlphaFoldDB; Q9SIY8; -.
DR SMR; Q9SIY8; -.
DR STRING; 3702.AT2G40370.1; -.
DR PaxDb; Q9SIY8; -.
DR PRIDE; Q9SIY8; -.
DR ProteomicsDB; 237054; -.
DR EnsemblPlants; AT2G40370.1; AT2G40370.1; AT2G40370.
DR GeneID; 818630; -.
DR Gramene; AT2G40370.1; AT2G40370.1; AT2G40370.
DR KEGG; ath:AT2G40370; -.
DR Araport; AT2G40370; -.
DR TAIR; locus:2063109; AT2G40370.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR InParanoid; Q9SIY8; -.
DR OMA; MIIDGPA; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9SIY8; -.
DR BioCyc; ARA:AT2G40370-MON; -.
DR PRO; PR:Q9SIY8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIY8; baseline and differential.
DR Genevisible; Q9SIY8; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0048226; C:Casparian strip; 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; IBA:GO_Central.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046688; P:response to copper ion; 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; -; 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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..580
FT /note="Laccase-5"
FT /id="PRO_0000283633"
FT DOMAIN 34..150
FT /note="Plastocyanin-like 1"
FT DOMAIN 160..312
FT /note="Plastocyanin-like 2"
FT DOMAIN 428..564
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 481
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 484
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 486
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 543
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 544
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 545
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 549
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 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
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 340
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 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 580 AA; 64133 MW; EFD565D79AD887CE CRC64;
MDVTKSLLCF ISFVAFLLFS SVAEANKAHH HEFIIQATKV KRLCETHNSI TVNGMFPGPM
LVVNNGDTLV VKVINRARYN ITIHWHGVRQ MRTGWADGPE FVTQCPIRPG SSYTYRFTIQ
GQEGTLWWHA HSSWLRATVY GSLLVFPPAG SSYPFTKPHR NVPLLLGEWW DANPVDVLRE
SIRTGGAPNN SDAYTINGQP GDLYKCSSQD TTVVPINVGE TILLRVINSA LNQPLFFTVA
NHKLTVVGAD ASYLKPFTTN VIVLGPGQTT DVLITGDQPP NRYYMAARAY QSAQNAPFGN
TTTTAILQYK SAPCCGVGGG SGTKKGNSFK PIMPILPAYN DTNTVTRFSQ SFRSLRRAEV
PTEIDENLFV TIGLGLNNCP KNFRSRRCQG PNGTRFTASM NNVSFALPSN YSLLQAHHHG
IPGVFTTDFP AKPPVKFDYT GNNISRSLYQ PDRGTKLYKL KYGSRVQIVL QDTGIVTPEN
HPIHLHGYDF YIIAEGFGNF NPKKDTAKFN LEDPPLRNTV GVPVNGWAVI RFIADNPGVW
IMHCHLDAHI SWGLAMAFLV ENGNGVLQTI EQPPHDLPVC
