(data stored in SCRATCH zone)

SWISSPROT: A0A1R7T3A1_ARATH

ID   A0A1R7T3A1_ARATH        Unreviewed;       544 AA.
AC   A0A1R7T3A1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   30-AUG-2017, entry version 5.
DE   RecName: Full=Laccase {ECO:0000256|RuleBase:RU361119};
DE            EC=1.10.3.2 {ECO:0000256|RuleBase:RU361119};
DE   AltName: Full=Benzenediol:oxygen oxidoreductase {ECO:0000256|RuleBase:RU361119};
DE   AltName: Full=Diphenol oxidase {ECO:0000256|RuleBase:RU361119};
DE   AltName: Full=Urishiol oxidase {ECO:0000256|RuleBase:RU361119};
GN   Name=LAC10 {ECO:0000313|EMBL:ANM71095.1};
GN   Synonyms=laccase 10 {ECO:0000313|EMBL:ANM71095.1};
GN   OrderedLocusNames=At5g01190 {ECO:0000313|EMBL:ANM71095.1};
GN   ORFNames=F7J8.170 {ECO:0000313|EMBL:ANM71095.1}, F7J8_170
GN   {ECO:0000313|EMBL:ANM71095.1};
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 {ECO:0000313|EMBL:ANM71095.1, ECO:0000313|Proteomes:UP000006548};
RN   [1] {ECO:0000313|EMBL:ANM71095.1, ECO:0000313|Proteomes:UP000006548}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX   PubMed=11130714; DOI=10.1038/35048507;
RG   Kazusa DNA Research Institute;
RG   Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG   European Union Arabidopsis Genome Sequencing Consortium;
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., See L.H., Vil D., Baker J.,
RA   Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T.,
RA   Entian K.D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Lankhorst R.K., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.W.,
RA   Bevan M., Fransz P.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:823-826(2000).
RN   [2] {ECO:0000313|EMBL:ANM71095.1, ECO:0000313|Proteomes:UP000006548}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Lignin degradation and detoxification of lignin-derived
CC       products. {ECO:0000256|RuleBase:RU361119}.
CC   -!- CATALYTIC ACTIVITY: 4 benzenediol + O(2) = 4 benzosemiquinone + 2
CC       H(2)O. {ECO:0000256|RuleBase:RU361119}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU361119};
CC       Note=Binds 4 Cu cations per monomer.
CC       {ECO:0000256|RuleBase:RU361119};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|RuleBase:RU361119}.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|RuleBase:RU361119, ECO:0000256|SAAS:SAAS00534212}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002688; ANM71095.1; -; Genomic_DNA.
DR   RefSeq; NP_001332650.1; NM_001342578.1.
DR   SMR; A0A1R7T3A1; -.
DR   EnsemblPlants; AT5G01190.2; AT5G01190.2; AT5G01190.
DR   GeneID; 831697; -.
DR   Gramene; AT5G01190.2; AT5G01190.2; AT5G01190.
DR   Proteomes; UP000006548; Chromosome 5.
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: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   3: Inferred from homology;
DR   PRODOM; A0A1R7T3A1.
DR   SWISS-2DPAGE; A0A1R7T3A1.
KW   Apoplast {ECO:0000256|RuleBase:RU361119};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006548};
KW   Copper {ECO:0000256|RuleBase:RU361119, ECO:0000256|SAAS:SAAS00524507};
KW   Lignin degradation {ECO:0000256|RuleBase:RU361119};
KW   Metal-binding {ECO:0000256|RuleBase:RU361119,
KW   ECO:0000256|SAAS:SAAS00524516};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361119,
KW   ECO:0000256|SAAS:SAAS00643973};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006548};
KW   Repeat {ECO:0000256|RuleBase:RU361119};
KW   Secreted {ECO:0000256|RuleBase:RU361119};
KW   Signal {ECO:0000256|RuleBase:RU361119}.
FT   SIGNAL        1     22       {ECO:0000256|RuleBase:RU361119}.
FT   CHAIN        23    544       Laccase. {ECO:0000256|RuleBase:RU361119}.
FT                                /FTId=PRO_5010005964.
FT   DOMAIN       29    130       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF07732}.
FT   DOMAIN      144    293       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF00394}.
FT   DOMAIN      399    527       Plastocyanin-like. {ECO:0000259|Pfam:
FT                                PF07731}.
SQ   SEQUENCE   544 AA;  59725 MW;  210F2E6E27B87DFF CRC64;
     MVFPIRILVL FALLAFPACV HGAIRKYTFN IVTVNGKFPG PTIYANEDDT ILVNVVNNVK
     YNVSIHWHGI RQLRTGWADG PAYITQCPIK PGHSYVYNFT VTGQRGTLWW HAHVLWLRAT
     VHGAIVILPK LGLPYPFPKP HREEVIILGE WWKSDTETVV NEALKSGLAP NVSDAHVING
     HPGFVPNCPS QGNFKLAVES GKTYMLRLIN AALNEELFFK IAGHRFTVVE VDAVYVKPFN
     TDTILIAPGQ TTTALVSAAR PSGQYLIAAA PFQDSAVVAV DNRTATATVH YSGTLSATPT
     KTTSPPPQNA TSVANTFVNS LRSLNSKTYP ANVPITVDHD LLFTVGLGIN RCHSCKAGNF
     SRVVAAINNI TFKMPKTALL QAHYFNLTGI YTTDFPAKPR RVFDFTGKPP SNLATMKATK
     LYKLPYNSTV QVVLQDTGNV APENHPIHLH GFNFFVVGLG TGNYNSKKDS NKFNLVDPVE
     RNTVGVPSGG WAAIRFRADN PGVWFMHCHL EVHTTWGLKM AFLVENGKGP NQSIRPPPSD
     LPKC
//

If you have problems or comments...

PBIL Back to PBIL home page