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Reviewed, UniProtKB/Swiss-Prot Q339K6 (LAC15_ORYSJ)

Last modified June 16, 2009. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Laccase-15
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 15
    Urishiol oxidase 15
    Diphenol oxidase 15
Gene names
Name: LAC15
Ordered Locus Names: Os10g0346300, LOC_Os10g20610
ORF Names: OSJNBa0045C13.15
OrganismOryza sativa subsp. japonica (Rice)
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

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Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Lignin degradation and detoxification of lignin-derived products By similarity.

Catalytic activity

4 benzenediol + O2 = 4 benzosemiquinone + 2 H2O.

Cofactor

Binds 4 copper ions per monomer By similarity.

Subcellular location

Secreted › extracellular space › apoplast Potential.

Sequence similarities

Belongs to the multicopper oxidase family.

Contains 3 plastocyanin-like domains.

Sequence caution

The sequence AAK92654.1 differs from that shown. Reason: Erroneous gene model prediction.

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Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentApoplast
Secreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncopper ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

laccase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 599570Laccase-15
PRO_0000291899

Regions

Domain46 – 162117Plastocyanin-like 1
Domain173 – 328156Plastocyanin-like 2
Domain444 – 586143Plastocyanin-like 3

Sites

Metal binding961Copper 1 By similarity
Metal binding981Copper 2 By similarity
Metal binding1411Copper 2 By similarity
Metal binding1431Copper 3 By similarity
Metal binding5031Copper 4 Potential
Metal binding5061Copper 1 By similarity
Metal binding5081Copper 3 By similarity
Metal binding5651Copper 3 By similarity
Metal binding5661Copper 4 Potential
Metal binding5671Copper 2 By similarity
Metal binding5711Copper 4 Potential
Metal binding5761Copper 4 Potential

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2731T → A in AK110474. Ref.4
Sequence conflict3111D → N in AK110474. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
Q339K6-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 7E10A0E08196CFDF

FASTA59965,670
        10         20         30         40         50         60 
MKRCQSSRPT AAVAAVVAAV SMIIVLVSGT AIPSAAAAAA VEHTFVVSQV NMTHLCKEMA 

        70         80         90        100        110        120 
FTVVNGQLPG PTIEVTEGDS VTVHVVNKSP YNLTIHWHGV YQLLNCWNDG VPMITQRPIQ 

       130        140        150        160        170        180 
PNHNFTYRFN VAGQEGTLWW HAHDAFLRGT VHGALIIRPR HGAASYPFPR PHREVPIIIG 

       190        200        210        220        230        240 
EWWEKDLPQV DRNMTNGYFD DYSSGSTING KLGDLFNCSG VLEDGYVLDV EPGKTYLLRI 

       250        260        270        280        290        300 
INAALFSEYF LKIAGHRFTV VASDANYLTP YSTDVVVIAP GETLDAIVVA DAPPSGRYYI 

       310        320        330        340        350        360 
AAQPIQAPPP DTQTPEYATR GTLQYSSNSR NSSAAAMPEM PHQHDTMRSF YFRGNLTAGA 

       370        380        390        400        410        420 
RLHRHGRRRV PARADESLFV TLGLGSVCRH GGASCKRGGN LKESIVVANV NNVSFHIPAA 

       430        440        450        460        470        480 
AATPILEAHY YHRLHAGAGE EEEELAERPP RAYNYTDQAL TPFGPEEMRL EATSRAVVTR 

       490        500        510        520        530        540 
RFRHGATVDV VFQSTAMLQG DSNPMHLHGH DVFLLAQGIG IYDAARDEGK FNLVNPPRKN 

       550        560        570        580        590 
TVLVPNLGWA AVRFVADNPG AWLMHCHFEF HLSMGMAAVF IVEDGPTVDT SLPPPPEDF

« Hide

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References

« Hide 'large scale' references
[1]"In-depth view of structure, activity, and evolution of rice chromosome 10."
Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. expand/collapse author list , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.
Science 300:1566-1569(2003) [PubMed: 12791992] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[2]"The map-based sequence of the rice genome."
International rice genome sequencing project (IRGSP)
Nature 436:793-800(2005) [PubMed: 16100779] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[3]"Curated genome annotation of Oryza sativa ssp. japonica and comparative genome analysis with Arabidopsis thaliana."
The rice annotation project (RAP)
Genome Res. 17:175-183(2007) [PubMed: 17210932] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: cv. Nipponbare.
[4]"Collection, mapping, and annotation of over 28,000 cDNA clones from japonica rice."
The rice full-length cDNA consortium
Science 301:376-379(2003) [PubMed: 12869764] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Nipponbare.

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Cross-references

Sequence databases

AC079634 Genomic DNA. Translation: AAK92654.1. Sequence problems.
DP000086 Genomic DNA. Translation: ABB47271.1.
AP008216 Genomic DNA. Translation: BAF26313.1.
AK110474 mRNA. No translation available.
RefSeqNP_001064399.1.
UniGeneOs.46813

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4348374.
KEGGosa:4348374.

Organism-specific databases

GrameneQ339K6.

Family and domain databases

InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 3 hits.
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLAC15_ORYSJ
AccessionPrimary (citable) accession number: Q339K6
Secondary accession number(s): Q94HD6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: December 6, 2005
Last modified: June 16, 2009
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents