LAC15_ARATH
ID LAC15_ARATH Reviewed; 565 AA.
AC Q84J37; Q9FI28;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Laccase-15;
DE EC=1.10.3.2;
DE AltName: Full=Benzenediol:oxygen oxidoreductase 15;
DE AltName: Full=Diphenol oxidase 15;
DE AltName: Full=Protein TRANSPARENT TESTA 10;
DE AltName: Full=Urishiol oxidase 15;
DE Flags: Precursor;
GN Name=TT10; Synonyms=LAC15; OrderedLocusNames=At5g48100; ORFNames=MDN11.18;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(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].
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 FUNCTION.
RA Koornneef M.;
RT "Mutations affecting the testa colour in Arabidopsis.";
RL Arabidopsis Inf. Serv. 27:1-4(1990).
RN [5]
RP FUNCTION.
RX PubMed=10677433; DOI=10.1104/pp.122.2.403;
RA Debeaujon I., Leon-Kloosterziel K.M., Koornneef M.;
RT "Influence of the testa on seed dormancy, germination, and longevity in
RT Arabidopsis.";
RL Plant Physiol. 122:403-413(2000).
RN [6]
RP ERRATUM OF PUBMED:10677433.
RA Debeaujon I., Leon-Kloosterziel K.M., Koornneef M.;
RL Plant Physiol. 125:1139-1141(2001).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [8]
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-152 AND GLY-509.
RX PubMed=16243908; DOI=10.1105/tpc.105.035154;
RA Pourcel L., Routaboul J.-M., Kerhoas L., Caboche M., Lepiniec L.,
RA Debeaujon I.;
RT "TRANSPARENT TESTA10 encodes a laccase-like enzyme involved in oxidative
RT polymerization of flavonoids in Arabidopsis seed coat.";
RL Plant Cell 17:2966-2980(2005).
RN [9]
RP FUNCTION, AND 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).
RN [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16779554; DOI=10.1007/s00425-006-0300-6;
RA Liang M., Davis E., Gardner D., Cai X., Wu Y.;
RT "Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation
RT of Arabidopsis.";
RL Planta 224:1185-1196(2006).
RN [11]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC products (By similarity). Involved in lignin synthesis in seed coats,
CC in seed coat permeability, in seed germination, and in root elongation.
CC Required for the seed coat (testa) brown pigmentation by mediating the
CC polymerization of proanthocyanidin (tannin) from its monomer precursor
CC epicatechin. Slightly promotes seed dormancy. {ECO:0000250,
CC ECO:0000269|PubMed:10677433, ECO:0000269|PubMed:16243908,
CC ECO:0000269|PubMed:16779554, ECO:0000269|PubMed:16804053,
CC ECO:0000269|Ref.4}.
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 siliques, particularly in
CC developing seeds. Also detected at low levels in stems, seedlings, and
CC flowers. {ECO:0000269|PubMed:15940465, ECO:0000269|PubMed:16243908,
CC ECO:0000269|PubMed:16779554, ECO:0000269|PubMed:16804053}.
CC -!- DEVELOPMENTAL STAGE: Transcript levels increase during rosette leaves
CC development. In the inflorescence stem, highest levels in the young,
CC developing tip and lowest levels in the basal stem tissues. Strong
CC increase 4 days after fertilization. Specifically localized in
CC developing seed coat (testa). Detected in the endothelium and in the
CC pigment strand at the chalaza zone during early stages of embryo
CC morphogenesis. Later, the activity increased and spread to the outer
CC integument, mostly in the oil penultimate cell layer. Strongly
CC expressed in early aborted seeds and in the transmitting tissue of the
CC silique. {ECO:0000269|PubMed:15940465, ECO:0000269|PubMed:16243908}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11074.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB017064; BAB11074.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95619.1; -; Genomic_DNA.
DR EMBL; BT002919; AAO22735.1; -; mRNA.
DR EMBL; BT005152; AAO50685.1; -; mRNA.
DR RefSeq; NP_199621.2; NM_124184.2.
DR AlphaFoldDB; Q84J37; -.
DR SMR; Q84J37; -.
DR STRING; 3702.AT5G48100.1; -.
DR PaxDb; Q84J37; -.
DR PRIDE; Q84J37; -.
DR ProteomicsDB; 250749; -.
DR EnsemblPlants; AT5G48100.1; AT5G48100.1; AT5G48100.
DR GeneID; 834862; -.
DR Gramene; AT5G48100.1; AT5G48100.1; AT5G48100.
DR KEGG; ath:AT5G48100; -.
DR Araport; AT5G48100; -.
DR TAIR; locus:2162677; AT5G48100.
DR eggNOG; KOG1263; Eukaryota.
DR HOGENOM; CLU_006504_6_3_1; -.
DR InParanoid; Q84J37; -.
DR OMA; CHTAWHA; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; Q84J37; -.
DR BioCyc; ARA:AT5G48100-MON; -.
DR PRO; PR:Q84J37; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84J37; baseline and differential.
DR Genevisible; Q84J37; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; ISS:TAIR.
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:0009813; P:flavonoid biosynthetic process; 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:0010023; P:proanthocyanidin biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Apoplast; Copper; Glycoprotein; Lignin degradation; Metal-binding;
KW Oxidoreductase; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..565
FT /note="Laccase-15"
FT /id="PRO_0000283643"
FT DOMAIN 27..143
FT /note="Plastocyanin-like 1"
FT DOMAIN 153..305
FT /note="Plastocyanin-like 2"
FT DOMAIN 408..547
FT /note="Plastocyanin-like 3"
FT BINDING 77
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 79
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 122
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 124
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 462
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 465
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 467
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 526
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 527
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 528
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 532
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 537
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 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 152
FT /note="D->G: In tt10-1; transparent testa; when associated
FT with D-509."
FT /evidence="ECO:0000269|PubMed:16243908"
FT MUTAGEN 509
FT /note="G->D: In tt10-1; transparent testa; when associated
FT with G-152."
FT /evidence="ECO:0000269|PubMed:16243908"
SQ SEQUENCE 565 AA; 63994 MW; FDBCBE3D6F10DBA4 CRC64;
MSHSFFNLFL ISLFLYNNCI AHHYTFTVRE VPYTKLCSTK AILTVNSQFP GPIIKVHKGD
TIYVNVQNRA SENITMHWHG VEQPRNPWSD GPEYITQCPI RPGSDFLYKV IFSIEDTTVW
WHAHSSWTRA TVHGLIFVYP RPPQILPFPK ADHEVPIILG EWWKRDVREV VEEFVRTGGA
PNVSDALTIN GHPGFLYPCS KSDTFHLTVE KGKTYRIRMV NAAMNLPLFF AIANHSLTVV
SADGHYIKPI KATYITISPG ETLDMLLHAD QDPERTYYMA ARAYQSGNID FNNSTTIGIL
SYTSSCKAKT SSFSGYYPTL PFYNDTSAAF GFFTKIKCLF SGQVPVQISR RIITTVSINL
RMCPQNSCEG PNGSRLAASM NNISFVTPSH VDILKAYYYH IKGVYGTRFP EFPPLIFNFT
AENQPLFLET PRLATEVKVI EFGQVVELVI QGTSLVGGGL DHPMHLHGFS FYVVGVGFGN
YNISEEDPSS RYNLYDPPYK NTMTVPRNGW IAIRFVADNP GVWFMHCHLD RHQTWGMNVV
FIVKNGREPN QQILPPPDDL PPCYE
