(data stored in ACNUC13479 zone)

SWISSPROT: LAC10_ARATH

ID   LAC10_ARATH             Reviewed;         558 AA.
AC   Q6ID18; Q9LFB7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   07-JUN-2017, entry version 97.
DE   RecName: Full=Laccase-10;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 10;
DE   AltName: Full=Diphenol oxidase 10;
DE   AltName: Full=Urishiol oxidase 10;
DE   Flags: Precursor;
GN   Name=LAC10; OrderedLocusNames=At5g01190; ORFNames=F7J8.170;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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
RT   in 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: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
CC       H(2)O.
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, with lower levels in siliques.
CC       {ECO:0000269|PubMed:16804053}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB69847.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL137189; CAB69847.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED90308.1; -; Genomic_DNA.
DR   EMBL; BT014855; AAT41838.1; -; mRNA.
DR   PIR; T45959; T45959.
DR   RefSeq; NP_195739.2; NM_120197.4.
DR   UniGene; At.33933; -.
DR   UniGene; At.67929; -.
DR   ProteinModelPortal; Q6ID18; -.
DR   SMR; Q6ID18; -.
DR   STRING; 3702.AT5G01190.1; -.
DR   PaxDb; Q6ID18; -.
DR   PRIDE; Q6ID18; -.
DR   EnsemblPlants; AT5G01190.1; AT5G01190.1; AT5G01190.
DR   GeneID; 831697; -.
DR   Gramene; AT5G01190.1; AT5G01190.1; AT5G01190.
DR   KEGG; ath:AT5G01190; -.
DR   Araport; AT5G01190; -.
DR   TAIR; locus:2150139; AT5G01190.
DR   eggNOG; KOG1263; Eukaryota.
DR   eggNOG; COG2132; LUCA.
DR   HOGENOM; HOG000241916; -.
DR   InParanoid; Q6ID18; -.
DR   KO; K05909; -.
DR   OMA; HDFAILA; -.
DR   OrthoDB; EOG093605NS; -.
DR   PhylomeDB; Q6ID18; -.
DR   BioCyc; ARA:AT5G01190-MONOMER; -.
DR   PRO; PR:Q6ID18; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q6ID18; 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:0016722; F:oxidoreductase activity, oxidizing metal ions; 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_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
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   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;
DR   PRODOM; Q6ID18.
DR   SWISS-2DPAGE; Q6ID18.
KW   Apoplast; Complete proteome; Copper; Glycoprotein; Lignin degradation;
KW   Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   CHAIN        23    558       Laccase-10.
FT                                /FTId=PRO_0000283638.
FT   DOMAIN       30    146       Plastocyanin-like 1.
FT   DOMAIN      157    308       Plastocyanin-like 2.
FT   DOMAIN      408    542       Plastocyanin-like 3.
FT   METAL        80     80       Copper 1; type 2. {ECO:0000250}.
FT   METAL        82     82       Copper 2; type 3. {ECO:0000250}.
FT   METAL       125    125       Copper 2; type 3. {ECO:0000250}.
FT   METAL       127    127       Copper 3; type 3. {ECO:0000250}.
FT   METAL       459    459       Copper 4; type 1. {ECO:0000250}.
FT   METAL       462    462       Copper 1; type 2. {ECO:0000250}.
FT   METAL       464    464       Copper 3; type 3. {ECO:0000250}.
FT   METAL       521    521       Copper 3; type 3. {ECO:0000250}.
FT   METAL       522    522       Copper 4; type 1. {ECO:0000250}.
FT   METAL       523    523       Copper 2; type 3. {ECO:0000250}.
FT   METAL       527    527       Copper 4; type 1. {ECO:0000250}.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    112    112       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    185    185       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    296    296       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    323    323       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    373    373       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    383    383       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    400    400       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    441    441       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    545    545       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   558 AA;  61298 MW;  4F0CACDA7088ACBA CRC64;
     MVFPIRILVL FALLAFPACV HGAIRKYTFN VVTKQVTRIC STKQIVTVNG KFPGPTIYAN
     EDDTILVNVV NNVKYNVSIH WHGIRQLRTG WADGPAYITQ CPIKPGHSYV YNFTVTGQRG
     TLWWHAHVLW LRATVHGAIV ILPKLGLPYP FPKPHREEVI ILGEWWKSDT ETVVNEALKS
     GLAPNVSDAH VINGHPGFVP NCPSQGNFKL AVESGKTYML RLINAALNEE LFFKIAGHRF
     TVVEVDAVYV KPFNTDTILI APGQTTTALV SAARPSGQYL IAAAPFQDSA VVAVDNRTAT
     ATVHYSGTLS ATPTKTTSPP PQNATSVANT FVNSLRSLNS KTYPANVPIT VDHDLLFTVG
     LGINRCHSCK AGNFSRVVAA INNITFKMPK TALLQAHYFN LTGIYTTDFP AKPRRVFDFT
     GKPPSNLATM KATKLYKLPY NSTVQVVLQD TGNVAPENHP IHLHGFNFFV VGLGTGNYNS
     KKDSNKFNLV DPVERNTVGV PSGGWAAIRF RADNPGVWFM HCHLEVHTTW GLKMAFLVEN
     GKGPNQSIRP PPSDLPKC
//

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