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UniProtKB/Swiss-Prot entry Q9LFD1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LAC9_ARATH
Primary accession number Q9LFD1
Secondary accession numbers None
Integrated into Swiss-Prot on April 3, 2007
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 37)
Name and origin of the protein
Protein name Laccase-9 [Precursor]
Synonyms EC 1.10.3.2
Benzenediol:oxygen oxidoreductase 9
Urishiol oxidase 9
Diphenol oxidase 9
Gene name
Name: LAC9
OrderedLocusNames: At5g01050
ORFNames: F7J8.30
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[2]
TISSUE SPECIFICITY.
DOI=10.1007/s00425-004-1472-6; PubMed=15940465 [NCBI, ExPASy, EBI, Israel, Japan]
McCaig B.C., Meagher R.B., Dean J.F.D.;
"Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana.";
Planta 221:619-636(2005).
[3]
TISSUE SPECIFICITY.
DOI=10.1093/jxb/erl022; PubMed=16804053 [NCBI, ExPASy, EBI, Israel, Japan]
Cai X., Davis E.J., Ballif J., Liang M., Bushman E., Haroldsen V., Torabinejad J., Wu Y.;
"Mutant identification and characterization of the laccase gene family in Arabidopsis.";
J. Exp. Bot. 57:2563-2569(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AL137189; CAB69833.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T45945; T45945.
RefSeq NP_195725.1; -.
UniGene At.33978
3D structure databases
HSSP P37064; 1AOZ. [HSSP ENTRY / PDB]
ModBase Q9LFD1.
Organism-specific databases
TAIR At5g01050; -.
Family and domain databases
InterPro IPR001117; Cu-oxidase.
IPR011706; Cu-oxidase_2.
IPR011707; Cu-oxidase_3.
IPR002355; Cu_oxidase_Cu_BS.
IPR008972; Cupredoxin.
IPR017761; Laccase.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.420; Cupredoxin; 3.
Pfam PF00394; Cu-oxidase; 1.
PF07731; Cu-oxidase_2; 1.
PF07732; Cu-oxidase_3; 1.
Pfam graphical view of domain structure.
PROSITE PS00079; MULTICOPPER_OXIDASE1; FALSE_NEG.
PS00080; MULTICOPPER_OXIDASE2; FALSE_NEG.
BLOCKS Q9LFD1.
Genome annotation databases
GeneID 831812; -.
GenomeReviews BA000015_GR; AT5G01050.
KEGG ath:AT5G01050; -.
NMPDR fig|3702.1.peg.22166; -.
Other
ProtoNet Q9LFD1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoplast; Complete proteome; Copper; Glycoprotein; Lignin degradation; Metal-binding; Oxidoreductase; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25     Potential. 
CHAIN   26   586  561     Laccase-9. PRO_0000283637
DOMAIN   33   149  117     Plastocyanin-like 1. 
DOMAIN   159   307  149     Plastocyanin-like 2. 
DOMAIN   411   552  142     Plastocyanin-like 3. 
METAL   83    83        Copper 1; type 2 (By similarity). 
METAL   85    85        Copper 2; type 3 (By similarity). 
METAL   128   128        Copper 2; type 3 (By similarity). 
METAL   130   130        Copper 3; type 3 (By similarity). 
METAL   469   469        Copper 4; type 1 (By similarity). 
METAL   472   472        Copper 1; type 2 (By similarity). 
METAL   474   474        Copper 3; type 3 (By similarity). 
METAL   531   531        Copper 3; type 3 (By similarity). 
METAL   532   532        Copper 4; type 1 (By similarity). 
METAL   533   533        Copper 2; type 3 (By similarity). 
METAL   537   537        Copper 4; type 1 (By similarity). 
CARBOHYD   52    52        N-linked (GlcNAc...) (Potential). 
CARBOHYD   74    74        N-linked (GlcNAc...) (Potential). 
CARBOHYD   79    79        N-linked (GlcNAc...) (Potential). 
CARBOHYD   111   111        N-linked (GlcNAc...) (Potential). 
CARBOHYD   236   236        N-linked (GlcNAc...) (Potential). 
CARBOHYD   333   333        N-linked (GlcNAc...) (Potential). 
CARBOHYD   385   385        N-linked (GlcNAc...) (Potential). 
CARBOHYD   403   403        N-linked (GlcNAc...) (Potential). 
CARBOHYD   451   451        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 586 AA [This is the length of the unprocessed precursor] Molecular weight: 65589 Da [This is the MW of the unprocessed precursor] CRC64: 84FFF22C99A35451 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPRVHHSLSN QAFLVLLLFS SIASAAIVEH VLHVKDVVVT PLCKEQMIPI VNGSLPGPTI 

        70         80         90        100        110        120 
NVREGDTLVV HVINKSTYNV TIHWHGVFQL KSVWMDGANM ITQCPIQPSN NFTYQFDITG 

       130        140        150        160        170        180 
QEGTLLWHAH VVNLRATIHG ALIIRPRSGR PYPFPKPYKE VPLIFQQWWD TDVRLLELRP 

       190        200        210        220        230        240 
APVSDAYLIN GLAGDSYPCS KNRMFNLKVV QGKTYLLRII NAALNTHLFF KIANHNVTVV 

       250        260        270        280        290        300 
AVDAVYTTPY LTDVMILTPG QTIDAILTAD QPIGTYYMAI IPYFSAIGVP ASPDTKPTRG 

       310        320        330        340        350        360 
LIVYEGATSS SSPTKPWMPP ANDIPTAHRF SSNITSLVGG PHWTPVPRHV DEKMFITMGL 

       370        380        390        400        410        420 
GLDPCPSNAK CVGPLDQRLA GSLNNRTFMI PERISMQEAY FYNITGVYTD DFPDQPPLKF 

       430        440        450        460        470        480 
DFTKFEQHPT NSDMEMMFPE RKTSVKTIRF NSTVEIVLQN TGILTPESHP MHLHGFNFYV 

       490        500        510        520        530        540 
LGYGFGNYDP IRDARKLNLF NPQMHNTVGV PPGGWVVLRF IANNPGIWLF HCHMDAHLPL 

       550        560        570        580 
GIMMAFIVQN GPTRETSLPS PPSNLPQCTR DPTIYDSRTT NVDMSY 

Q9LFD1 in FASTA format

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