Reviewed, UniProtKB/Swiss-Prot Q9SR40 (LAC7_ARATH)

Names and origin

Protein names

Recommended name:
    Laccase-7
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 7
    Urishiol oxidase 7
    Diphenol oxidase 7

Gene names

Name:	LAC7
Ordered Locus Names:	At3g09220
ORF Names:	F3L24.9

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	567 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 + 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. Ref.4 Ref.5
Sequence similarities	Belongs to the multicopper oxidase family. Contains 3 plastocyanin-like domains.

Ontologies

Keywords
Biological process	Lignin degradation
Cellular component	Apoplast Secreted
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
Cellular component	apoplast Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular space 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 567	544	Laccase-7		PRO_0000283635
Regions
	Domain	31 – 147	117	Plastocyanin-like 1
	Domain	157 – 310	154	Plastocyanin-like 2
	Domain	412 – 551	140	Plastocyanin-like 3
Sites
	Metal binding	81	1	Copper 1; type 2 By similarity
	Metal binding	83	1	Copper 2; type 3 By similarity
	Metal binding	126	1	Copper 2; type 3 By similarity
	Metal binding	128	1	Copper 3; type 3 By similarity
	Metal binding	468	1	Copper 4; type 1 By similarity
	Metal binding	471	1	Copper 1; type 2 By similarity
	Metal binding	473	1	Copper 3; type 3 By similarity
	Metal binding	530	1	Copper 3; type 3 By similarity
	Metal binding	531	1	Copper 4; type 1 By similarity
	Metal binding	532	1	Copper 2; type 3 By similarity
	Metal binding	536	1	Copper 4; type 1 By similarity
Amino acid modifications
	Glycosylation	34	1	N-linked (GlcNAc...) Potential
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	77	1	N-linked (GlcNAc...) Potential
	Glycosylation	115	1	N-linked (GlcNAc...) Potential
	Glycosylation	186	1	N-linked (GlcNAc...) Potential
	Glycosylation	298	1	N-linked (GlcNAc...) Potential
	Glycosylation	339	1	N-linked (GlcNAc...) Potential
	Glycosylation	374	1	N-linked (GlcNAc...) Potential
	Glycosylation	386	1	N-linked (GlcNAc...) Potential
	Glycosylation	427	1	N-linked (GlcNAc...) Potential
	Glycosylation	450	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9SR40-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: BA4EFEAA57734D2B	FASTA	567	62,403
	10 20 30 40 50 60 MEGVRVPIAC ALILLAISSI TSASIVEHTF NVQNLTVSRL CKRQVITVVN GSLPGPTIRV 70 80 90 100 110 120 KEGDSLVIHV LNHSPHNITI HWHGIFHKLT VWADGPSMIT QCPIQPGQRY AYRFNITGQE 130 140 150 160 170 180 GTLWWHAHAS FLRATVYGAL VIRPKSGHSY PFPKPHKEVP ILFGEWWNTD VVALEEAAIA 190 200 210 220 230 240 TGVPPNNSDA YTINGRPGNL YPCSKDRMFS LNVVKGKRYL LRIINAAMNI QLFFKIANHR 250 260 270 280 290 300 LTVVAADAVY TAPYVTDVIV IAPGQTIDAL LFADQSVDTS YYMAAHPYAS APAVPFPNTT 310 320 330 340 350 360 TRGVIHYGGA SKTGRSKPVL MPKLPSFFDT LTAYRFYSNL TALVNGPHWV PVPRYVDEEM 370 380 390 400 410 420 LVTIGLGLEA CADNTTCPKF SASMSNHSFV LPKKLSILEA VFHDVKGIFT ADFPDQPPVK 430 440 450 460 470 480 FDYTNPNVTQ TNPGLLFTQK STSAKILKFN TTVEVVLQNH ALIAAESHPM HLHGFNFHVL 490 500 510 520 530 540 AQGFGNYDPS RDRSKLNLVD PQSRNTLAVP VGGWAVIRFT ANNPGAWIFH CHIDVHLPFG 550 560 LGMIFVVKNG PTKSTTLPPP PPDLPKC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [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]. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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.
[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: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC011436 Genomic DNA. Translation: AAF14041.1. AK117639 mRNA. Translation: BAC42295.1. BT004971 mRNA. Translation: AAO50504.1.
IPI	IPI00528510.
RefSeq	NP_187533.1.
UniGene	At.40144
3D structure databases
HSSP	HSSP built from PDB template 1AOZ based on UniProtKB P37064.
ModBase	Search...
Proteomic databases
PRIDE	Q9SR40.
Genome annotation databases
GeneID	820078.
GenomeReviews	Gene locus AT3G09220 in contig BA000014_GR.
KEGG	ath:AT3G09220.
NMPDR	fig|3702.1.peg.12936.
Organism-specific databases
TAIR	At3g09220.
Phylogenomic databases
OMA	Q9SR40. PTIVATE.
Enzyme and pathway databases
BRENDA	1.10.3.2. 302.
Gene expression databases
ArrayExpress	Q9SR40.
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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAC7_ARATH

Accession

Primary (citable) accession number: Q9SR40

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)