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Q93ZR1 (ELP3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processAuxin signaling pathway
Transcription
Transcription regulation
tRNA processing
   Cellular componentNucleus
   LigandIron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA mediated transformation

Inferred from mutant phenotype PubMed 17827277. Source: TAIR

auxin-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from mutant phenotype Ref.1. Source: TAIR

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-templated

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-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentElongator 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

nucleus

Inferred from direct assay PubMed 22404109. Source: TAIR

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 565565Elongator complex protein 3
PRO_0000232128

Regions

Domain414 – 565152N-acetyltransferase

Sites

Metal binding1171Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1271Iron-sulfur (4Fe-4S-S-AdoMet) By similarity
Metal binding1301Iron-sulfur (4Fe-4S-S-AdoMet) By similarity

Experimental info

Mutagenesis2001R → W in east1-1; slow growth associated with pale-green and downwardly curled leaves. Ref.8
Mutagenesis3311D → N in elo3-1; reduced cell proliferation. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q93ZR1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 8F993E4D41CF4B05

FASTA56563,694
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
RefSeqNP_568725.1. NM_124412.2.
UniGeneAt.20657.

3D structure databases

ProteinModelPortalQ93ZR1.
SMRQ93ZR1. Positions 457-561.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid20344. 1 interaction.
IntActQ93ZR1. 1 interaction.
STRING3702.AT5G50320.1-P.

Proteomic databases

PaxDbQ93ZR1.
PRIDEQ93ZR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G50320.1; AT5G50320.1; AT5G50320.
GeneID835098.
KEGGath:AT5G50320.

Organism-specific databases

TAIRAT5G50320.

Phylogenomic databases

eggNOGCOG1243.
HOGENOMHOG000227514.
InParanoidQ93ZR1.
KOK07739.
OMAGYKVVSH.
PhylomeDBQ93ZR1.
ProtClustDBCLSN2689971.

Enzyme and pathway databases

BioCycARA:AT5G50320-MONOMER.

Gene expression databases

GenevestigatorQ93ZR1.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
3.80.30.20. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR006638. Elp3/MiaB/NifB.
IPR000182. GNAT_dom.
IPR005910. Hist_AcTrfase_ELP3.
IPR007197. rSAM.
IPR023404. rSAM_horseshoe.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005669. Hist_AcTrfase_ELP3. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
TIGRFAMsTIGR01211. ELP3. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ93ZR1.

Entry information

Entry nameELP3_ARATH
AccessionPrimary (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: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names