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UniProtKB/Swiss-Prot entry Q9FY79


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

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Entry information
Entry name LAC14_ARATH
Primary accession number Q9FY79
Secondary accession number Q1PDY2
Integrated into Swiss-Prot on April 3, 2007
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 42)
Name and origin of the protein
Protein name Laccase-14 [Precursor]
Synonyms EC 1.10.3.2
Benzenediol:oxygen oxidoreductase 14
Urishiol oxidase 14
Diphenol oxidase 14
Gene name
Name: LAC14
OrderedLocusNames: At5g09360
ORFNames: T5E8.160
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1111/j.1467-7652.2006.00183.x; PubMed=17147637 [NCBI, ExPASy, EBI, Israel, Japan]
Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
"Simultaneous high-throughput recombinational cloning of open reading frames in closed and open configurations.";
Plant Biotechnol. J. 4:317-324(2006).
[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
AL391712; CAC05462.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ446936; ABE66147.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_196498.1; -.
UniGene At.54782
3D structure databases
HSSP P37064; 1AOZ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
ModBase Q9FY79.
Organism-specific databases
TAIR At5g09360; -.
Ontologies
GO
GO:0048046; Cellular component: apoplast (inferred from electronic annotation from UniProtKB-KW).
GO:0005507; Molecular function: copper ion binding (inferred from electronic annotation from InterPro).
GO:0008471; Molecular function: laccase activity (inferred from electronic annotation from EC).
GO:0046274; Biological process: lignin catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
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; 1.
PS00080; MULTICOPPER_OXIDASE2; 1.
ProtoNet Q9FY79.
Genome annotation databases
GeneID 830795; -.
GenomeReviews BA000015_GR; AT5G09360.
KEGG ath:AT5G09360; -.
NMPDR fig|3702.1.peg.23056; -.
Other
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    33  33     Potential. 
CHAIN   34   569  536     Laccase-14. PRO_0000283642
DOMAIN   41   157  117     Plastocyanin-like 1. 
DOMAIN   167   320  154     Plastocyanin-like 2. 
DOMAIN   420   553  134     Plastocyanin-like 3. 
METAL   91    91        Copper 1; type 2 (By similarity). 
METAL   93    93        Copper 2; type 3 (By similarity). 
METAL   136   136        Copper 2; type 3 (By similarity). 
METAL   138   138        Copper 3; type 3 (By similarity). 
METAL   470   470        Copper 4; type 1 (By similarity). 
METAL   473   473        Copper 1; type 2 (By similarity). 
METAL   475   475        Copper 3; type 3 (By similarity). 
METAL   532   532        Copper 3; type 3 (By similarity). 
METAL   533   533        Copper 4; type 1 (By similarity). 
METAL   534   534        Copper 2; type 3 (By similarity). 
METAL   538   538        Copper 4; type 1 (By similarity). 
METAL   543   543        Copper 4; type 1 (By similarity). 
CARBOHYD   87    87        N-linked (GlcNAc...) (Potential). 
CARBOHYD   190   190        N-linked (GlcNAc...) (Potential). 
CARBOHYD   249   249        N-linked (GlcNAc...) (Potential). 
CARBOHYD   336   336        N-linked (GlcNAc...) (Potential). 
CARBOHYD   374   374        N-linked (GlcNAc...) (Potential). 
CARBOHYD   395   395        N-linked (GlcNAc...) (Potential). 
CARBOHYD   430   430        N-linked (GlcNAc...) (Potential). 
CARBOHYD   452   452        N-linked (GlcNAc...) (Potential). 
CONFLICT   463   469        TVWASNI -> NVLASDN (in Ref. 2; ABE66147). 
Sequence information
Length: 569 AA [This is the length of the unprocessed precursor] Molecular weight: 64878 Da [This is the MW of the unprocessed precursor] CRC64: FE8E2C1F8A329188 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEFKLNIPNT IIKTLQTIVF FLFVLLAFQI AEAEIHHHTF KIKSKAYTRL CNTNKILTVN 

        70         80         90        100        110        120 
GEFPGPTLKA YRGDKLIVNV INNANYNITL HWHGARQIRN PWSDGPEYVT QCPIRPGESY 

       130        140        150        160        170        180 
VYRIDLKVEE GTIWWHAHSQ WARATVHGAF IVYPKRGSSY PFPKPHREIP LILGEWWKKE 

       190        200        210        220        230        240 
NIMHIPGKAN KTGGEPAISD SYTINGQPGY LYPCSKPETF KITVVRGRRY LLRIINAVMD 

       250        260        270        280        290        300 
EELFFAIANH TLTVVAKDGF YLKHFKSDYL MITPGQSMDV LLHANQRPNH YFVAARAYSS 

       310        320        330        340        350        360 
AFGAGFDKTT TTAILQYKGD TLNRIKPILP YLPPYNRTEA STRFTNQFRS QRPVNVPVKI 

       370        380        390        400        410        420 
NTRLLYAISV NLMNCSDDRP CTGPFGKRFS SSINNISFVN PSVDILRAYY RHIGGVFQED 

       430        440        450        460        470        480 
FPRNPPTKFN YTGENLPFPT RFGTKVVVLD YNSSVELILQ GTTVWASNIH PIHLHGYNFY 

       490        500        510        520        530        540 
VVGSGFGNFD RRKDPLRYNL VDPPEETTVG VPRNGWTAVR FVANNPGVWL LHCHIERHAT 

       550        560 
WGMNTVFIVK DGPTKSSRMV KPPPDLPSC 

Q9FY79 in FASTA format

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