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Q8RYM9 (LAC2_ORYSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laccase-2
EC=1.10.3.2
Alternative name(s):
Benzenediol:oxygen oxidoreductase 2
Diphenol oxidase 2
Urishiol oxidase 2
Gene names
Name:LAC2
Ordered Locus Names:Os01g0634500, LOC_Os01g44330
ORF Names:OsJ_002637, P0663E10.27
OrganismOryza sativa subsp. japonica (Rice) [Reference proteome]
Taxonomic identifier39947 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza ›

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Ontologies

Keywords
   Biological processLignin degradation
   Cellular componentApoplast
Secreted
   DomainRepeat
Signal
   LigandCopper
Metal-binding
   Molecular functionOxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlignin catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapoplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncopper ion binding

Inferred from electronic annotation. Source: InterPro

hydroquinone:oxygen oxidoreductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 562536Laccase-2
PRO_0000291887

Regions

Domain34 – 150117Plastocyanin-like 1
Domain160 – 312153Plastocyanin-like 2
Domain411 – 546136Plastocyanin-like 3

Sites

Metal binding841Copper 1 By similarity
Metal binding861Copper 2 By similarity
Metal binding1291Copper 2 By similarity
Metal binding1311Copper 3 By similarity
Metal binding4631Copper 4 By similarity
Metal binding4661Copper 1 By similarity
Metal binding4681Copper 3 By similarity
Metal binding5251Copper 3 By similarity
Metal binding5261Copper 4 By similarity
Metal binding5271Copper 2 By similarity
Metal binding5311Copper 4 By similarity

Amino acid modifications

Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1891N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation3001N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Glycosylation3861N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation4451N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1681E → D in EAZ12812. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8RYM9 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 0BF4F84B9E7996A9

FASTA56261,296
        10         20         30         40         50         60 
MASAASSLPL LVSSLLLALF ALGAHADVKR YQFDIVMSNV SRLCHEKAMV TVNGSYPGPT 

        70         80         90        100        110        120 
IYAREGDRVI VNVTNHVKHN MTIHWHGLKQ RRNGWADGPA YVTQCPIGSG GSYVYDFNVT 

       130        140        150        160        170        180 
RQRGTLWWHA HIAWMRATVH GAIVILPAAG VPYPFPKPDD EAEIVLGEWW HADVETVERQ 

       190        200        210        220        230        240 
GSMLGMAPNM SDAHTINGKP GPLVPFCSEK HTYALQVQSG KTYLLRIINA AVNDELFFSI 

       250        260        270        280        290        300 
AGHNMTVVEI DATYTKPFAA STVQLSPGQT MNVLVSADQS PGRYFMVAKP FNDVPIPADN 

       310        320        330        340        350        360 
KTATAILQYA GVPTSVVPAL PQTMPATNST GSVAAFHDKL RSLNSPRYPA DVPLAVDRHL 

       370        380        390        400        410        420 
LYTIGLNIDP CETCLNRSRL AASLNNITFV MPRTALLQAH YYGQKGVFAA DFPDRPPARF 

       430        440        450        460        470        480 
NYTGVPLTAG LGTSLGTRLS KIAYNATVEL VLQDTNLLSV ESHPFHLHGY NFFVVGRGVG 

       490        500        510        520        530        540 
NFDPAKDPAK YNLVDPPERN TVGVPAGGWT AIRFRADNPG VWFLHCHLEV HTSWGLKMAF 

       550        560 
LVEDGSGPDE SVLPPPKDLP KC

« Hide

References

[1]"The genome sequence and structure of rice chromosome 1."
Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y., Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H., Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M. expand/collapse author list , Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S., Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H., Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S., Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y., Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S., Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H., Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.
Nature 420:312-316(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.
[2]"The genomes of Oryza sativa: a history of duplications."
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L. expand/collapse author list , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nipponbare.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP004317 Genomic DNA. Translation: BAB90733.1.
CM000138 Genomic DNA. Translation: EAZ12812.1.

3D structure databases

HSSPHSSP built from PDB template 1GYC based on UniProtKB Q12718.
ProteinModelPortalQ8RYM9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

KEGGdosa:Os01t0634500-00.

Organism-specific databases

GrameneQ8RYM9.

Phylogenomic databases

eggNOGCOG2132.
OMAWHAHIAW.

Family and domain databases

Gene3D2.60.40.420. 3 hits.
InterProIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR002355. Cu_oxidase_Cu_BS.
IPR008972. Cupredoxin.
IPR017761. Laccase.
[Graphical view]
PfamPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 1 hit.
[Graphical view]
SUPFAMSSF49503. Cupredoxin. 3 hits.
TIGRFAMsTIGR03389. laccase. 1 hit.
PROSITEPS00079. MULTICOPPER_OXIDASE1. 1 hit.
PS00080. MULTICOPPER_OXIDASE2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLAC2_ORYSJ
AccessionPrimary (citable) accession number: Q8RYM9
Secondary accession number(s): A2ZVR5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 1, 2002
Last modified: April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Oryza sativa (rice)

Index of Oryza sativa entries and their corresponding gene designations

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents