Reviewed, UniProtKB/Swiss-Prot Q9LFD2 (LAC8_ARATH)

Names and origin

Protein names

Recommended name:
    Laccase-8
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 8
    Urishiol oxidase 8
    Diphenol oxidase 8

Gene names

Name:	LAC8
Ordered Locus Names:	At5g01040
ORF Names:	F7J8.20

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	584 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. Involved in the flowering time inhibition.
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.
Tissue specificity	Predominantly expressed in tissues other than the inflorescence stem, especially in roots. Ref.4 Ref.5
Developmental stage	Expressed along a developmental gradient in the inflorescence stem, with higher levels in olders organs and low levels in young tissues. Ref.4
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Lignin degradation
Cellular component	Apoplast Secreted
Coding sequence diversity	Alternative splicing
Domain	Repeat Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lignin catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW vegetative to reproductive phase transition Ref.5 Inferred from mutant phenotype. Source: TAIR
Cellular component	apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW laccase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9LFD2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9LFD2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     203-234: RMFNLKVVQGKTYLLRIVNAALNTHLFFKIAN → SNTHSLLESKVTFYCKLFTKNRINFYFYFWLW
     235-584: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Chain	26 – 584	559	Laccase-8		PRO_0000283636
Regions
	Domain	33 – 149	117	Plastocyanin-like 1
	Domain	159 – 306	148	Plastocyanin-like 2
	Domain	410 – 550	141	Plastocyanin-like 3
Sites
	Metal binding	83	1	Copper 1; type 2 By similarity
	Metal binding	85	1	Copper 2; type 3 By similarity
	Metal binding	128	1	Copper 2; type 3 By similarity
	Metal binding	130	1	Copper 3; type 3 By similarity
	Metal binding	467	1	Copper 4; type 1 By similarity
	Metal binding	470	1	Copper 1; type 2 By similarity
	Metal binding	472	1	Copper 3; type 3 By similarity
	Metal binding	529	1	Copper 3; type 3 By similarity
	Metal binding	530	1	Copper 4; type 1 By similarity
	Metal binding	531	1	Copper 2; type 3 By similarity
	Metal binding	535	1	Copper 4; type 1 By similarity
Amino acid modifications
	Glycosylation	52	1	N-linked (GlcNAc...) Potential
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Glycosylation	332	1	N-linked (GlcNAc...) Potential
	Glycosylation	384	1	N-linked (GlcNAc...) Potential
	Glycosylation	402	1	N-linked (GlcNAc...) Potential
	Glycosylation	449	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	203 – 234	32	RMFNL…FKIAN → SNTHSLLESKVTFYCKLFTK NRINFYFYFWLW in isoform 2.		VSP_024348
	Alternative sequence	235 – 584	350	Missing in isoform 2.		VSP_024349

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E83C308696325898	FASTA	584	65,282
	10 20 30 40 50 60 MPRLHHYLSN QAFLVLLLFS SIASAAVVEH VLHIQDVVVK PLCKEQIIPA ANGSLPGPTI 70 80 90 100 110 120 NVREGDTLVV NVINNSTYNV TIHWHGVFQL KSVWMDGANM ITQCPIQPGY NFTYQFDITG 130 140 150 160 170 180 QEGTLLWHAH VVNLRATLHG ALVIRPRSGR PYPFPKPYKE VPIVFQQWWD TDVRLLQLRP 190 200 210 220 230 240 APVSDAYLIN GLAGDSYPCS ENRMFNLKVV QGKTYLLRIV NAALNTHLFF KIANHNVTVV 250 260 270 280 290 300 AVDAVYSTPY LTDVMILTPG QTVDALLTAD QAIGKYYMAT LPYISAIGIP TPDIKPTRGL 310 320 330 340 350 360 IVYQGATSSS SPAEPLMPVP NDMSTAHRFT SNITSLVGGP HWTPVPRHVD EKMFITMGLG 370 380 390 400 410 420 LDPCPAGTKC IGPLGQRYAG SLNNRTFMIP ERISMQEAYF YNISGIYTDD FPNQPPLKFD 430 440 450 460 470 480 YTKFEQRTNN DMKMMFPERK TSVKKIRFNS TVEIVLQNTA IISPESHPMH LHGFNFYVLG 490 500 510 520 530 540 YGFGNYDPIR DARKLNLFNP QMHNTVGVPP GGWVVLRFIA NNPGVWLFHC HMDAHLPYGI 550 560 570 580 MSAFIVQNGP TPETSLPSPP SNLPQCTRDP TIYDSRTTNI DLSY
	Isoform 2. Checksum: 75498B1972496DA1	FASTA	234	26,727
	10 20 30 40 50 60 MPRLHHYLSN QAFLVLLLFS SIASAAVVEH VLHIQDVVVK PLCKEQIIPA ANGSLPGPTI 70 80 90 100 110 120 NVREGDTLVV NVINNSTYNV TIHWHGVFQL KSVWMDGANM ITQCPIQPGY NFTYQFDITG 130 140 150 160 170 180 QEGTLLWHAH VVNLRATLHG ALVIRPRSGR PYPFPKPYKE VPIVFQQWWD TDVRLLQLRP 190 200 210 220 230 APVSDAYLIN GLAGDSYPCS ENSNTHSLLE SKVTFYCKLF TKNRINFYFY FWLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." 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. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: cv. Columbia.
[3]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-499 (ISOFORM 1). Strain: cv. Columbia.
[4]	"Gene structure and molecular analysis of the laccase-like multicopper oxidase (LMCO) gene family in Arabidopsis thaliana." McCaig B.C., Meagher R.B., Dean J.F.D. Planta 221:619-636(2005) [PubMed: 15940465] [Abstract] Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]	"Mutant identification and characterization of the laccase gene family in Arabidopsis." Cai X., Davis E.J., Ballif J., Liang M., Bushman E., Haroldsen V., Torabinejad J., Wu Y. J. Exp. Bot. 57:2563-2569(2006) [PubMed: 16804053] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL137189 Genomic DNA. Translation: CAB69832.1. AK117360 mRNA. Translation: BAC42030.1. AK176457 mRNA. Translation: BAD44220.1.
IPI	IPI00526470. IPI00845130.
PIR	T45944.
RefSeq	NP_195724.1.
UniGene	At.27905
3D structure databases
HSSP	HSSP built from PDB template 1AOZ based on UniProtKB P37064.
ModBase	Search...
Genome annotation databases
GeneID	831877.
GenomeReviews	Gene locus AT5G01040 in contig BA000015_GR.
KEGG	ath:AT5G01040.
NMPDR	fig|3702.1.peg.22165.
Organism-specific databases
TAIR	At5g01040.
Phylogenomic databases
OMA	NSEDTEA.
Enzyme and pathway databases
BRENDA	1.10.3.2. 302.
Gene expression databases
Genevestigator	Q9LFD2.
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]
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]
TIGRFAMs	TIGR03389. laccase. 1 hit.
PROSITE	PS00079. MULTICOPPER_OXIDASE1. False negative. PS00080. MULTICOPPER_OXIDASE2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAC8_ARATH

Accession

Primary (citable) accession number: Q9LFD2
Secondary accession number(s): Q67YL1, Q8GYV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)