(data stored in ACNUC13479 zone)

SWISSPROT: LAC9_ARATH

ID   LAC9_ARATH              Reviewed;         586 AA.
AC   Q9LFD1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   07-JUN-2017, entry version 103.
DE   RecName: Full=Laccase-9;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 9;
DE   AltName: Full=Diphenol oxidase 9;
DE   AltName: Full=Urishiol oxidase 9;
DE   Flags: Precursor;
GN   Name=LAC9; OrderedLocusNames=At5g01050; ORFNames=F7J8.30;
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   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
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: Predominantly expressed in roots.
CC       {ECO:0000269|PubMed:15940465, ECO:0000269|PubMed:16804053}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000305}.
DR   EMBL; AL137189; CAB69833.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90292.1; -; Genomic_DNA.
DR   PIR; T45945; T45945.
DR   RefSeq; NP_195725.1; NM_120182.3.
DR   UniGene; At.33978; -.
DR   ProteinModelPortal; Q9LFD1; -.
DR   SMR; Q9LFD1; -.
DR   STRING; 3702.AT5G01050.1; -.
DR   PaxDb; Q9LFD1; -.
DR   PRIDE; Q9LFD1; -.
DR   EnsemblPlants; AT5G01050.1; AT5G01050.1; AT5G01050.
DR   GeneID; 831812; -.
DR   Gramene; AT5G01050.1; AT5G01050.1; AT5G01050.
DR   KEGG; ath:AT5G01050; -.
DR   Araport; AT5G01050; -.
DR   TAIR; locus:2150049; AT5G01050.
DR   eggNOG; KOG1263; Eukaryota.
DR   eggNOG; COG2132; LUCA.
DR   HOGENOM; HOG000241916; -.
DR   InParanoid; Q9LFD1; -.
DR   KO; K05909; -.
DR   OMA; YKEVPLI; -.
DR   OrthoDB; EOG093605LR; -.
DR   PhylomeDB; Q9LFD1; -.
DR   BioCyc; ARA:AT5G01050-MONOMER; -.
DR   PRO; PR:Q9LFD1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LFD1; baseline and differential.
DR   Genevisible; Q9LFD1; 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; 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; 4.
DR   TIGRFAMs; TIGR03389; laccase; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9LFD1.
DR   SWISS-2DPAGE; Q9LFD1.
KW   Apoplast; Complete proteome; Copper; Glycoprotein; Lignin degradation;
KW   Metal-binding; Oxidoreductase; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    586       Laccase-9.
FT                                /FTId=PRO_0000283637.
FT   DOMAIN       33    149       Plastocyanin-like 1.
FT   DOMAIN      159    307       Plastocyanin-like 2.
FT   DOMAIN      411    552       Plastocyanin-like 3.
FT   METAL        83     83       Copper 1; type 2. {ECO:0000250}.
FT   METAL        85     85       Copper 2; type 3. {ECO:0000250}.
FT   METAL       128    128       Copper 2; type 3. {ECO:0000250}.
FT   METAL       130    130       Copper 3; type 3. {ECO:0000250}.
FT   METAL       469    469       Copper 4; type 1. {ECO:0000250}.
FT   METAL       472    472       Copper 1; type 2. {ECO:0000250}.
FT   METAL       474    474       Copper 3; type 3. {ECO:0000250}.
FT   METAL       531    531       Copper 3; type 3. {ECO:0000250}.
FT   METAL       532    532       Copper 4; type 1. {ECO:0000250}.
FT   METAL       533    533       Copper 2; type 3. {ECO:0000250}.
FT   METAL       537    537       Copper 4; type 1. {ECO:0000250}.
FT   CARBOHYD     52     52       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     74     74       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    236    236       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    385    385       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    403    403       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    451    451       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   586 AA;  65589 MW;  84FFF22C99A35451 CRC64;
     MPRVHHSLSN QAFLVLLLFS SIASAAIVEH VLHVKDVVVT PLCKEQMIPI VNGSLPGPTI
     NVREGDTLVV HVINKSTYNV TIHWHGVFQL KSVWMDGANM ITQCPIQPSN NFTYQFDITG
     QEGTLLWHAH VVNLRATIHG ALIIRPRSGR PYPFPKPYKE VPLIFQQWWD TDVRLLELRP
     APVSDAYLIN GLAGDSYPCS KNRMFNLKVV QGKTYLLRII NAALNTHLFF KIANHNVTVV
     AVDAVYTTPY LTDVMILTPG QTIDAILTAD QPIGTYYMAI IPYFSAIGVP ASPDTKPTRG
     LIVYEGATSS SSPTKPWMPP ANDIPTAHRF SSNITSLVGG PHWTPVPRHV DEKMFITMGL
     GLDPCPSNAK CVGPLDQRLA GSLNNRTFMI PERISMQEAY FYNITGVYTD DFPDQPPLKF
     DFTKFEQHPT NSDMEMMFPE RKTSVKTIRF NSTVEIVLQN TGILTPESHP MHLHGFNFYV
     LGYGFGNYDP IRDARKLNLF NPQMHNTVGV PPGGWVVLRF IANNPGIWLF HCHMDAHLPL
     GIMMAFIVQN GPTRETSLPS PPSNLPQCTR DPTIYDSRTT NVDMSY
//

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