Reviewed, UniProtKB/Swiss-Prot O80434 (LAC4_ARATH)

Names and origin

Protein names

Recommended name:
    Laccase-4
    EC=1.10.3.2
Alternative name(s):
    Benzenediol:oxygen oxidoreductase 4
    Urishiol oxidase 4
    Diphenol oxidase 4
    Protein IRREGULAR XYLEM 12

Gene names

Name:	IRX12
Synonyms:	LAC4
Ordered Locus Names:	At2g38080
ORF Names:	F16M14.1

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	558 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. Required for secondary xylem cell wall lignification.
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	Ubiquitous, with higher levels in the inflorescence stem. Ref.4 Ref.5
Developmental stage	Transcript levels diminished during rosette leaves development. 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
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 secondary cell wall biogenesis Ref.3 Inferred from mutant phenotype. Source: TAIR
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 – 24	24	Potential
	Chain	25 – 558	534	Laccase-4		PRO_0000283632
Regions
	Domain	32 – 148	117	Plastocyanin-like 1
	Domain	158 – 308	151	Plastocyanin-like 2
	Domain	408 – 542	135	Plastocyanin-like 3
Sites
	Metal binding	82	1	Copper 1; type 2 By similarity
	Metal binding	84	1	Copper 2; type 3 By similarity
	Metal binding	127	1	Copper 2; type 3 By similarity
	Metal binding	129	1	Copper 3; type 3 By similarity
	Metal binding	459	1	Copper 4; type 1 By similarity
	Metal binding	462	1	Copper 1; type 2 By similarity
	Metal binding	464	1	Copper 3; type 3 By similarity
	Metal binding	521	1	Copper 3; type 3 By similarity
	Metal binding	522	1	Copper 4; type 1 By similarity
	Metal binding	523	1	Copper 2; type 3 By similarity
	Metal binding	527	1	Copper 4; type 1 By similarity
Amino acid modifications
	Glycosylation	37	1	N-linked (GlcNAc...) Potential
	Glycosylation	78	1	N-linked (GlcNAc...) Potential
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Glycosylation	187	1	N-linked (GlcNAc...) Potential
	Glycosylation	296	1	N-linked (GlcNAc...) Potential
	Glycosylation	323	1	N-linked (GlcNAc...) Potential
	Glycosylation	330	1	N-linked (GlcNAc...) Potential
	Glycosylation	373	1	N-linked (GlcNAc...) Potential
	Glycosylation	383	1	N-linked (GlcNAc...) Potential
	Glycosylation	400	1	N-linked (GlcNAc...) Potential
	Glycosylation	418	1	N-linked (GlcNAc...) Potential
	Glycosylation	441	1	N-linked (GlcNAc...) Potential
	Glycosylation	479	1	N-linked (GlcNAc...) Potential
	Glycosylation	545	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	O80434-1 [UniParc]. Last modified June 1, 2002. Version 2. Checksum: C3BA6184D88E87DC	FASTA	558	61,527
	10 20 30 40 50 60 MGSHMVWFLF LVSFFSVFPA PSESMVRHYK FNVVMKNVTR LCSSKPTVTV NGRYPGPTIY 70 80 90 100 110 120 AREDDTLLIK VVNHVKYNVS IHWHGVRQVR TGWADGPAYI TQCPIQPGQV YTYNYTLTGQ 130 140 150 160 170 180 RGTLWWHAHI LWLRATVYGA LVILPKRGVP YPFPKPDNEK VIVLGEWWKS DTENIINEAL 190 200 210 220 230 240 KSGLAPNVSD SHMINGHPGP VRNCPSQGYK LSVENGKTYL LRLVNAALNE ELFFKVAGHI 250 260 270 280 290 300 FTVVEVDAVY VKPFKTDTVL IAPGQTTNVL LTASKSAGKY LVTASPFMDA PIAVDNVTAT 310 320 330 340 350 360 ATVHYSGTLS SSPTILTLPP PQNATSIANN FTNSLRSLNS KKYPALVPTT IDHHLFFTVG 370 380 390 400 410 420 LGLNACPTCK AGNGSRVVAS INNVTFIMPK TALLPAHYFN TSGVFTTDFP KNPPHVFNYS 430 440 450 460 470 480 GGSVTNMATE TGTRLYKLPY NATVQLVLQD TGVIAPENHP VHLHGFNFFE VGRGLGNFNS 490 500 510 520 530 540 TKDPKNFNLV DPVERNTIGV PSGGWVVIRF RADNPGVWFM HCHLEVHTTW GLKMAFLVEN 550 GKGPNQSILP PPKDLPKC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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.
[3]	"Identification of novel genes in Arabidopsis involved in secondary cell wall formation using expression profiling and reverse genetics." Brown D.M., Zeef L.A.H., Ellis J., Goodacre R., Turner S.R. Plant Cell 17:2281-2295(2005) [PubMed: 15980264] [Abstract] Cited for: FUNCTION.
[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: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC003028 Genomic DNA. Translation: AAC27158.2. AY052669 mRNA. Translation: AAK96573.1. AY063730 mRNA. Translation: AAL36080.1. AY065187 mRNA. Translation: AAL38363.1. AY114636 mRNA. Translation: AAM47955.1.
IPI	IPI00522344.
PIR	T01240.
RefSeq	NP_565881.1.
UniGene	At.12454
3D structure databases
HSSP	HSSP built from PDB template 1HFU based on UniProtKB Q9Y780.
ModBase	Search...
Proteomic databases
PRIDE	O80434.
Genome annotation databases
GeneID	818386.
GenomeReviews	Gene locus AT2G38080 in contig CT485783_GR.
KEGG	ath:AT2G38080.
NMPDR	fig|3702.1.peg.10916.
Organism-specific databases
TAIR	At2g38080.
Phylogenomic databases
OMA	O80434. YAREDDT.
Enzyme and pathway databases
BRENDA	1.10.3.2. 302.
Gene expression databases
ArrayExpress	O80434.
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. 1 hit. PS00080. MULTICOPPER_OXIDASE2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LAC4_ARATH

Accession

Primary (citable) accession number: O80434
Secondary accession number(s): Q940U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)