Q93ZR1 (ELP3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongator complex protein 3
Short name=AtELP3
EC=2.3.1.48

Alternative name(s):
Elongator component 3
Protein ELONGATA 3
Protein ENHANCER-OF-ASYMMETRIC-LEAVES-TWO1

Gene names

Name:	HAG3
Synonyms:	EAST1, ELO3, ELP3
Ordered Locus Names:	At5g50320
ORF Names:	MXI22.3

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone acetyltransferase component of the large multiprotein complex Elongator that is involved in the regulation of transcription initiation and elongation. May also have a methyltransferase activity. Promotes organs development by modulating cell division rate. Required for auxin distribution or signaling. Involved in tRNA wobble uridine modification. Mediates the establishment of leaf polarity independently of AS2 and the ta-siRNA-related pathway. Ref.6 Ref.7 Ref.8
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Cofactor	Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Subunit structure	Component of the RNA polymerase II elongator complex (Elongator) made of at least six subunits, ELP1/ELO2, ELP2, ELP3/ELO3, ELP4/ELO1, ELP5, and ELP6. Ref.7
Subcellular location	Nucleus. Note: Localized in euchromatin during interphase. Ref.7
Tissue specificity	Expressed in meristematic tissues of in roots, leaves, seedlings, cotyledons, floral buds and shoot apices. Ref.1 Ref.7
Disruption phenotype	Slow growing rate associated with pale-green and downwardly curled narrow leaves and reduced root growth that results from a decreased cell division rate and a reduced apical dominance. Defect in tRNA wobble uridine modification. Filamentous leaves with abaxialized epidermis in AS2 defective plants. Ref.1 Ref.6 Ref.7 Ref.8
Sequence similarities	Belongs to the ELP3 family. Contains 1 N-acetyltransferase domain.
Sequence caution	The sequence AAL06951.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Auxin signaling pathway Transcription Transcription regulation tRNA processing
Cellular component	Nucleus
Ligand	Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA mediated transformation Inferred from mutant phenotype PubMed 17827277. Source: TAIR auxin mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Inferred from mutant phenotype Ref.1. Source: TAIR histone acetylation Inferred from electronic annotation. Source: GOC organ growth Inferred from mutant phenotype Ref.1. Source: TAIR regulation of auxin mediated signaling pathway Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of leaf formation Inferred from mutant phenotype Ref.8. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW specification of organ axis polarity Inferred from mutant phenotype Ref.8. Source: UniProtKB tRNA wobble uridine modification Inferred from mutant phenotype Ref.6. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Elongator holoenzyme complex Inferred from direct assay Ref.7. Source: UniProtKB cytosol Inferred from direct assay PubMed 21166475PubMed 22404109. Source: TAIR nuclear euchromatin Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC iron-sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 565	565	Elongator complex protein 3		PRO_0000232128
Regions
	Domain	414 – 565	152	N-acetyltransferase
Sites
	Metal binding	117	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	127	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
	Metal binding	130	1	Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Experimental info
	Mutagenesis	200	1	R → W in east1-1; slow growth associated with pale-green and downwardly curled leaves. Ref.8
	Mutagenesis	331	1	D → N in elo3-1; reduced cell proliferation. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q93ZR1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 8F993E4D41CF4B05	FASTA	565	63,694
	10 20 30 40 50 60 MATAVVMNGE LKKQPRPGKG GYQGRGLTEE EARVRAISEI VSTMIERSHR NENVDLNAIK 70 80 90 100 110 120 TAACRKYGLA RAPKLVEMIA ALPDSERETL LPKLRAKPVR TASGIAVVAV MSKPHRCPHI 130 140 150 160 170 180 ATTGNICVYC PGGPDSDFEY STQSYTGYEP TSMRAIRARY NPYVQARSRI DQLKRLGHSV 190 200 210 220 230 240 DKVEFILMGG TFMSLPAEYR DFFIRNLHDA LSGHTSANVE EAVAYSEHSA TKCIGMTIET 250 260 270 280 290 300 RPDYCLGPHL RQMLIYGCTR LEIGVQSTYE DVARDTNRGH TVAAVADCFC LAKDAGFKVV 310 320 330 340 350 360 AHMMPDLPNV GVERDMESFK EFFESPSFRA DGLKIYPTLV IRGTGLYELW KTGRYRNYPP 370 380 390 400 410 420 EQLVDIVARI LSMVPPWTRV YRVQRDIPMP LVTSGVEKGN LRELALARMD DLGLKCRDVR 430 440 450 460 470 480 TREAGIQDIH HKIKPEQVEL VRRDYTANEG WETFLSYEDT RQDILVGLLR LRKCGKNVTC 490 500 510 520 530 540 PELMGKCSVV RELHVYGTAV PVHGRDADKL QHQGYGTLLM EEAERIARRE HRSNKIGVIS 550 560 GVGTRHYYRK LGYELEGPYM VKHLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The elongata mutants identify a functional Elongator complex in plants with a role in cell proliferation during organ growth." Nelissen H., Fleury D., Bruno L., Robles P., de Veylder L., Traas J., Micol J., Van Montagu M., Inze D., Van Lijsebettens M. Proc. Natl. Acad. Sci. U.S.A. 102:7754-7759(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF ASP-331, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY. Strain: cv. Landsberg erecta. Tissue: Seedling.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones." Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S. DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes." Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S., Richards E.J., Bender J., Mount D.W., Jorgensen R.A. Nucleic Acids Res. 30:5036-5055(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE.
[6]	"Elongator function in tRNA wobble uridine modification is conserved between yeast and plants." Mehlgarten C., Jablonowski D., Wrackmeyer U., Tschitschmann S., Sondermann D., Jaeger G., Gong Z., Bystroem A.S., Schaffrath R., Breunig K.D. Mol. Microbiol. 76:1082-1094(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]	"Plant Elongator regulates auxin-related genes during RNA polymerase II transcription elongation." Nelissen H., De Groeve S., Fleury D., Neyt P., Bruno L., Bitonti M.B., Vandenbussche F., Van der Straeten D., Yamaguchi T., Tsukaya H., Witters E., De Jaeger G., Houben A., Van Lijsebettens M. Proc. Natl. Acad. Sci. U.S.A. 107:1678-1683(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[8]	"Asymmetric leaves2 and Elongator, a histone acetyltransferase complex, mediate the establishment of polarity in leaves of Arabidopsis thaliana." Kojima S., Iwasaki M., Takahashi H., Imai T., Matsumura Y., Fleury D., Van Lijsebettens M., Machida Y., Machida C. Plant Cell Physiol. 52:1259-1273(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ARG-200, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ964958 mRNA. Translation: CAI79647.1. AB012248 Genomic DNA. Translation: BAB09451.1. CP002688 Genomic DNA. Translation: AED95925.1. AY054293 mRNA. Translation: AAL06951.1. Different initiation. AY056323 mRNA. Translation: AAL07172.1. AY133528 mRNA. Translation: AAM91358.1.
IPI	IPI00539057.
RefSeq	NP_568725.1. NM_124412.2.
UniGene	At.20657.
3D structure databases
ProteinModelPortal	Q93ZR1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q93ZR1. 1 interaction.
STRING	3702.AT5G50320.1-P.
Proteomic databases
PaxDb	Q93ZR1.
PRIDE	Q93ZR1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G50320.1; AT5G50320.1; AT5G50320.
GeneID	835098.
KEGG	ath:AT5G50320.
Organism-specific databases
TAIR	At5g50320.
Phylogenomic databases
eggNOG	COG1243.
HOGENOM	HOG000227514.
InParanoid	Q93ZR1.
KO	K07739.
OMA	EWQHRGY.
PhylomeDB	Q93ZR1.
ProtClustDB	CLSN2689971.
Gene expression databases
Genevestigator	Q93ZR1.
GermOnline	AT5G50320. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.630.30. 1 hit. 3.80.30.20. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR006638. Elp3/MiaB/NifB. IPR000182. GNAT_dom. IPR005910. Hist_AcTrfase_ELP3. IPR007197. rSAM. IPR023404. rSAM_horseshoe. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMs	TIGR01211. ELP3. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ELP3_ARATH

Accession

Primary (citable) accession number: Q93ZR1
Secondary accession number(s): Q9FK40

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program