LAC12_ARATH
ID LAC12_ARATH Reviewed; 565 AA.
AC Q9FLB5;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Laccase-12;
DE EC=1.10.3.2;
DE AltName: Full=Benzenediol:oxygen oxidoreductase 12;
DE AltName: Full=Diphenol oxidase 12;
DE AltName: Full=Urishiol oxidase 12;
DE Flags: Precursor;
GN Name=LAC12; OrderedLocusNames=At5g05390; ORFNames=K18I23.20;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(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 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 [4]
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: Predominantly expressed in the inflorescence stem.
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; AB010692; BAB09982.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90868.1; -; Genomic_DNA.
DR RefSeq; NP_196158.1; NM_120621.2.
DR AlphaFoldDB; Q9FLB5; -.
DR SMR; Q9FLB5; -.
DR STRING; 3702.AT5G05390.1; -.
DR PaxDb; Q9FLB5; -.
DR PRIDE; Q9FLB5; -.
DR ProteomicsDB; 250770; -.
DR EnsemblPlants; AT5G05390.1; AT5G05390.1; AT5G05390.
DR GeneID; 830421; -.
DR Gramene; AT5G05390.1; AT5G05390.1; AT5G05390.
DR KEGG; ath:AT5G05390; -.
DR Araport; AT5G05390; -.
DR TAIR; locus:2153469; AT5G05390.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR InParanoid; Q9FLB5; -.
DR OMA; WNANPVD; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q9FLB5; -.
DR BioCyc; ARA:AT5G05390-MON; -.
DR PRO; PR:Q9FLB5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLB5; baseline and differential.
DR Genevisible; Q9FLB5; 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 GO; GO:1990641; P:response to iron ion starvation; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..565
FT /note="Laccase-12"
FT /id="PRO_0000283640"
FT DOMAIN 32..148
FT /note="Plastocyanin-like 1"
FT DOMAIN 158..310
FT /note="Plastocyanin-like 2"
FT DOMAIN 413..549
FT /note="Plastocyanin-like 3"
FT BINDING 82
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 84
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="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="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 466
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 469
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 471
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 528
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="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 530
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 534
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 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 565 AA; 62734 MW; 15DA9DDD5CA8932E CRC64;
MTTVHTFSIL LFFCSLFSAS LIIAKVQHHD FVIQETPVKR LCKTRNAITV NGMFPGPTLE
VNNGDTLEVK VHNRARYNIT IHWHGVRQIR TGWADGPEFV TQCPIRPGKS YTYRFTIQGQ
EGTLWWHAHS SWLRATVYGA LIIHPTPGSS FPFPKPDRQT ALMLGEWWNA NPVDVINQAT
RTGAAPNISD AYTINGQPGD LYNCSTKETV VVPINSGETS LLRVINAALN QPLFFTVANH
KLTVVGADAS YLKPFTTKVL MLGPGQTTDV LLTADQPPKR YYIAARAYQS AQNAPFDNTT
TTAILQYKKT TTTSKPIMPV LPAFNDTNTV TSFSRKFKSL RNVVVPKTID DNLFFTIGLG
LDNCPKKFPK SRCQGLNGTR FTASMNNVSF VLPSNFSLLQ AHSNGIPGVF TTDFPSKPPV
KFDYTGNNIS RALFQPVKGT KLYKLKYGSR VQVVLQDTNI VTSENHPIHL HGYDFYIVGE
GFGNFNPKKD TSKFNLVDPP LRNTVAVPVN GWAVIRFVAD NPGVWLMHCH LDVHIKWGLA
MAFLVDNGVG ELETLEAPPH DLPIC
