LAC6_ARATH
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 03-AUG-2022, entry version 140.
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 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 [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 -!- 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; 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.AT2G46570.1; -.
DR PaxDb; Q9ZPY2; -.
DR PRIDE; Q9ZPY2; -.
DR ProteomicsDB; 237145; -. [Q9ZPY2-1]
DR EnsemblPlants; AT2G46570.1; AT2G46570.1; AT2G46570. [Q9ZPY2-1]
DR GeneID; 819269; -.
DR Gramene; AT2G46570.1; AT2G46570.1; AT2G46570. [Q9ZPY2-1]
DR KEGG; ath:AT2G46570; -.
DR Araport; AT2G46570; -.
DR TAIR; locus:2039944; AT2G46570.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR InParanoid; Q9ZPY2; -.
DR OMA; QKCHSKT; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9ZPY2; -.
DR BioCyc; ARA:AT2G46570-MON; -.
DR PRO; PR:Q9ZPY2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPY2; baseline and differential.
DR Genevisible; Q9ZPY2; 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 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
