Reviewed, UniProtKB/Swiss-Prot Q2R0L2 (LAC19_ORYSJ)

Names and origin

Protein names

Recommended name:
    Laccase-19
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 19
    Urishiol oxidase 19
    Diphenol oxidase 19

Gene names

Name:	LAC19
Ordered Locus Names:	Os11g0641500, LOC_Os11g42200
ORF Names:	OsJ_033252

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	590 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Lignin degradation and detoxification of lignin-derived products By similarity.
Catalytic activity	4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O.
Cofactor	Binds 4 copper ions per monomer By similarity.
Subcellular location	Secreted › extracellular space › apoplastPotential.
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.
Sequence caution	The sequence AK103094 differs from that shown. Reason: Frameshift at position 318. The sequence EAZ19043.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Lignin degradation
Cellular component	Apoplast Secreted
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	apoplast Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: InterPro laccase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 590	562	Laccase-19		PRO_0000291905
Regions
	Domain	36 – 152	117	Plastocyanin-like 1
	Domain	161 – 315	155	Plastocyanin-like 2
	Domain	424 – 566	143	Plastocyanin-like 3
Sites
	Metal binding	86	1	Copper 1 By similarity
	Metal binding	88	1	Copper 2 By similarity
	Metal binding	131	1	Copper 2 By similarity
	Metal binding	133	1	Copper 3 By similarity
	Metal binding	483	1	Copper 4 Potential
	Metal binding	486	1	Copper 1 By similarity
	Metal binding	488	1	Copper 3 By similarity
	Metal binding	545	1	Copper 3 By similarity
	Metal binding	546	1	Copper 4 Potential
	Metal binding	547	1	Copper 2 By similarity
	Metal binding	551	1	Copper 4 Potential
	Metal binding	556	1	Copper 4 Potential
Amino acid modifications
	Glycosylation	41	1	N-linked (GlcNAc...) Potential
	Glycosylation	47	1	N-linked (GlcNAc...) Potential
	Glycosylation	120	1	N-linked (GlcNAc...) Potential
	Glycosylation	205	1	N-linked (GlcNAc...) Potential
	Glycosylation	344	1	N-linked (GlcNAc...) Potential
	Glycosylation	378	1	N-linked (GlcNAc...) Potential
	Glycosylation	397	1	N-linked (GlcNAc...) Potential
	Glycosylation	434	1	N-linked (GlcNAc...) Potential
	Glycosylation	465	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	501	1	N → K in EAZ19043. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q2R0L2-1 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: 451C018F129BD2E5	FASTA	590	65,848
	10 20 30 40 50 60 MEKLSMVTSL LCAITVAVLA VAVVSGEAAV VEHTFVVHEM NATHLCNTTK IYVVNGQFPG 70 80 90 100 110 120 PTVDVTEGDT VVVHVINKLP FGLTIHWHGV RQMRSCWADG AGFVTECPIP PGNEHTYRFN 130 140 150 160 170 180 VTGQVGTLWW HAHVTCLRAT INGAFIVRPR DGKYPFPTPA KDVPIIIGEW WELDLIELDR 190 200 210 220 230 240 RMMDGNFDDN PLSATINGKL GDLSNCSRMV EESFILDVKH GESYLLRVIN TALFSEYYFR 250 260 270 280 290 300 VAGHTFTVVG ADGNYLTPFK TDMVTVAPGE AIDVIMVADA PPAHYHMIAL ANQPPEPDPQ 310 320 330 340 350 360 IPVFTSRGLV RYAGTTANNN GLPVPMPIMP NQHNTMPSYY FHANLTGLAH PERHRVPMHV 370 380 390 400 410 420 DERLFVTLGL GSICRGQNTT CKRRRSPETI VVATMNNVSF AHPKTTALLE RYYDGTSKGV 430 440 450 460 470 480 YTEDFPIRPP RPFNYTNRDL IPPGPLEEAL EPTFKATKLK RFKYNTSVEI IFQSTTLMQS 490 500 510 520 530 540 DSNPMHLHGY DVFLLAQGLG NFNAKRDVRK FNYHNPQLRN TVQVPRGGWA AIRFVTDNPG 550 560 570 580 590 MWYLHCHFEF HIIMGMATAF IVEDGPTPET SLPPPPPEFK RCGNNGLSQP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The sequence of rice chromosomes 11 and 12, rich in disease resistance genes and recent gene duplications." The rice chromosomes 11 and 12 sequencing consortia BMC Biol. 3:20-20(2005) [PubMed: 16188032] [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]	"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. , 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: 15685292] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[5]	"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DP000010 Genomic DNA. Translation: ABA95017.1. AP008217 Genomic DNA. Translation: BAF28716.1. CM000148 Genomic DNA. Translation: EAZ19043.1. Sequence problems. AK103094 mRNA. No translation available.
RefSeq	NP_001068353.1.
UniGene	Os.54291
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4351005.
KEGG	osa:4351005.
Organism-specific databases
Gramene	Q2R0L2.
Family and domain databases
InterPro	IPR001117. Cu-oxidase. IPR011706. Cu-oxidase_2. IPR011707. Cu-oxidase_3. IPR002355. Cu_oxidase_Cu_BS. IPR008972. Cupredoxin. [Graphical view]
Gene3D	G3DSA:2.60.40.420. Cupredoxin. 3 hits.
Pfam	PF00394. Cu-oxidase. 1 hit. PF07731. Cu-oxidase_2. 1 hit. PF07732. Cu-oxidase_3. 1 hit. [Graphical view]
PROSITE	PS00079. MULTICOPPER_OXIDASE1. 1 hit. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAC19_ORYSJ

Accession

Primary (citable) accession number: Q2R0L2
Secondary accession number(s): A3CD80

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	January 24, 2006
Last modified:	November 25, 2008
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)