(data stored in ACNUC13479 zone)

SWISSPROT: LAC8_ARATH

ID   LAC8_ARATH              Reviewed;         584 AA.
AC   Q9LFD2; Q67YL1; Q8GYV9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   30-AUG-2017, entry version 107.
DE   RecName: Full=Laccase-8;
DE            EC=1.10.3.2;
DE   AltName: Full=Benzenediol:oxygen oxidoreductase 8;
DE   AltName: Full=Diphenol oxidase 8;
DE   AltName: Full=Urishiol oxidase 8;
DE   Flags: Precursor;
GN   Name=LAC8; OrderedLocusNames=At5g01040; ORFNames=F7J8.20;
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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-499 (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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
RT   in Arabidopsis.";
RL   J. Exp. Bot. 57:2563-2569(2006).
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products (By similarity). Involved in the flowering time
CC       inhibition. {ECO:0000250, ECO:0000269|PubMed:16804053}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9LFD2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9LFD2-2; Sequence=VSP_024348, VSP_024349;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in tissues other than
CC       the inflorescence stem, especially in roots.
CC       {ECO:0000269|PubMed:15940465, ECO:0000269|PubMed:16804053}.
CC   -!- DEVELOPMENTAL STAGE: Expressed along a developmental gradient in
CC       the inflorescence stem, with higher levels in olders organs and
CC       low levels in young tissues. {ECO:0000269|PubMed:15940465}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000305}.
DR   EMBL; AL137189; CAB69832.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90291.1; -; Genomic_DNA.
DR   EMBL; AK117360; BAC42030.1; -; mRNA.
DR   EMBL; AK176457; BAD44220.1; -; mRNA.
DR   PIR; T45944; T45944.
DR   RefSeq; NP_195724.1; NM_120181.5. [Q9LFD2-1]
DR   UniGene; At.27863; -.
DR   UniGene; At.27905; -.
DR   ProteinModelPortal; Q9LFD2; -.
DR   STRING; 3702.AT5G01040.1; -.
DR   PaxDb; Q9LFD2; -.
DR   EnsemblPlants; AT5G01040.1; AT5G01040.1; AT5G01040. [Q9LFD2-1]
DR   GeneID; 831877; -.
DR   Gramene; AT5G01040.1; AT5G01040.1; AT5G01040.
DR   KEGG; ath:AT5G01040; -.
DR   Araport; AT5G01040; -.
DR   TAIR; locus:2150039; AT5G01040.
DR   eggNOG; KOG1263; Eukaryota.
DR   eggNOG; COG2132; LUCA.
DR   HOGENOM; HOG000241916; -.
DR   InParanoid; Q9LFD2; -.
DR   KO; K05909; -.
DR   OMA; RYYMAIS; -.
DR   OrthoDB; EOG093605LR; -.
DR   PhylomeDB; Q9LFD2; -.
DR   BioCyc; ARA:AT5G01040-MONOMER; -.
DR   PRO; PR:Q9LFD2; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; Q9LFD2; 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   GO; GO:0046688; P:response to copper ion; IEP:TAIR.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP: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_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; Q9LFD2.
DR   SWISS-2DPAGE; Q9LFD2.
KW   Alternative splicing; Apoplast; Complete proteome; Copper;
KW   Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     25       {ECO:0000255}.
FT   CHAIN        26    584       Laccase-8.
FT                                /FTId=PRO_0000283636.
FT   DOMAIN       33    149       Plastocyanin-like 1.
FT   DOMAIN      159    306       Plastocyanin-like 2.
FT   DOMAIN      410    550       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       467    467       Copper 4; type 1. {ECO:0000250}.
FT   METAL       470    470       Copper 1; type 2. {ECO:0000250}.
FT   METAL       472    472       Copper 3; type 3. {ECO:0000250}.
FT   METAL       529    529       Copper 3; type 3. {ECO:0000250}.
FT   METAL       530    530       Copper 4; type 1. {ECO:0000250}.
FT   METAL       531    531       Copper 2; type 3. {ECO:0000250}.
FT   METAL       535    535       Copper 4; type 1. {ECO:0000250}.
FT   CARBOHYD     52     52       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     75     75       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    332    332       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    384    384       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    402    402       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    449    449       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ     203    234       RMFNLKVVQGKTYLLRIVNAALNTHLFFKIAN -> SNTHS
FT                                LLESKVTFYCKLFTKNRINFYFYFWLW (in isoform
FT                                2). {ECO:0000303|PubMed:11910074}.
FT                                /FTId=VSP_024348.
FT   VAR_SEQ     235    584       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11910074}.
FT                                /FTId=VSP_024349.
SQ   SEQUENCE   584 AA;  65282 MW;  E83C308696325898 CRC64;
     MPRLHHYLSN QAFLVLLLFS SIASAAVVEH VLHIQDVVVK PLCKEQIIPA ANGSLPGPTI
     NVREGDTLVV NVINNSTYNV TIHWHGVFQL KSVWMDGANM ITQCPIQPGY NFTYQFDITG
     QEGTLLWHAH VVNLRATLHG ALVIRPRSGR PYPFPKPYKE VPIVFQQWWD TDVRLLQLRP
     APVSDAYLIN GLAGDSYPCS ENRMFNLKVV QGKTYLLRIV NAALNTHLFF KIANHNVTVV
     AVDAVYSTPY LTDVMILTPG QTVDALLTAD QAIGKYYMAT LPYISAIGIP TPDIKPTRGL
     IVYQGATSSS SPAEPLMPVP NDMSTAHRFT SNITSLVGGP HWTPVPRHVD EKMFITMGLG
     LDPCPAGTKC IGPLGQRYAG SLNNRTFMIP ERISMQEAYF YNISGIYTDD FPNQPPLKFD
     YTKFEQRTNN DMKMMFPERK TSVKKIRFNS TVEIVLQNTA IISPESHPMH LHGFNFYVLG
     YGFGNYDPIR DARKLNLFNP QMHNTVGVPP GGWVVLRFIA NNPGVWLFHC HMDAHLPYGI
     MSAFIVQNGP TPETSLPSPP SNLPQCTRDP TIYDSRTTNI DLSY
//

If you have problems or comments...

PBIL Back to PBIL home page