ELP3_DROME
ID ELP3_DROME Reviewed; 552 AA.
AC Q9VQZ6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Elongator complex protein 3 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9};
DE AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305};
GN Name=Elp3; ORFNames=CG15433;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20626565; DOI=10.1111/j.1471-4159.2010.06892.x;
RA Singh N., Lorbeck M.T., Zervos A., Zimmerman J., Elefant F.;
RT "The histone acetyltransferase Elp3 plays in active role in the control of
RT synaptic bouton expansion and sleep in Drosophila.";
RL J. Neurochem. 115:493-504(2010).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF TYR-531.
RX PubMed=21288872; DOI=10.1534/genetics.110.123893;
RA Walker J., Kwon S.Y., Badenhorst P., East P., McNeill H., Svejstrup J.Q.;
RT "Role of elongator subunit Elp3 in Drosophila melanogaster larval
RT development and immunity.";
RL Genetics 187:1067-1075(2011).
CC -!- FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator
CC complex which is required for multiple tRNA modifications, including
CC mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-
CC methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl
CC uridine) (By similarity). In the elongator complex, acts as a tRNA
CC uridine(34) acetyltransferase by mediating formation of
CC carboxymethyluridine in the wobble base at position 34 in tRNAs (By
CC similarity). Plays a role in the control of synaptic bouton expansion
CC (PubMed:20626565). Required for larval development (PubMed:21288872).
CC {ECO:0000250|UniProtKB:D5VRB9, ECO:0000250|UniProtKB:Q9H9T3,
CC ECO:0000269|PubMed:20626565, ECO:0000269|PubMed:21288872}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + S-adenosyl-L-methionine + uridine(34) in
CC tRNA = 5'-deoxyadenosine + carboxymethyluridine(34) in tRNA + CoA + 2
CC H(+) + L-methionine; Xref=Rhea:RHEA:61020, Rhea:RHEA-COMP:10407,
CC Rhea:RHEA-COMP:11727, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:65315,
CC ChEBI:CHEBI:74882; Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61021;
CC Evidence={ECO:0000250|UniProtKB:D5VRB9};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q02908};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:Q02908};
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q9H9T3}.
CC -!- SUBUNIT: Component of the elongator complex.
CC {ECO:0000250|UniProtKB:Q9H9T3}.
CC -!- DISRUPTION PHENOTYPE: Pronounced larval developmental delay and death
CC at the pupal stage with delayed and reduced ecdysone-induced
CC transcription, developmental of melanotic nodules and up-regulation of
CC stress-induced genes (PubMed:21288872). RNAi-mediated knockdown results
CC in lethality at the late pupal stage (PubMed:20626565). RNAi-mediated
CC knockdown in the central nervous system results in a hyperactive
CC phenotype, sleep loss in adult females, a significant expansion in
CC synaptic bouton number in the larval neuromuscular junction (NMJ),
CC increased larval NMJ axonal length and branching, and misregulation of
CC genes known to be involved in these processes with a marked increase in
CC Hsc70-3 and Syb mRNA levels and a marked decrease in qvr/sss mRNA
CC levels (PubMed:20626565). RNAi-mediated knockdown in hemocytes results
CC in reduced hemocyte numbers and hemocyte aggregation (PubMed:21288872).
CC {ECO:0000269|PubMed:20626565, ECO:0000269|PubMed:21288872}.
CC -!- SIMILARITY: Belongs to the ELP3 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:Q9H9T3}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014134; AAF51012.1; -; Genomic_DNA.
DR EMBL; AY089621; AAL90359.1; -; mRNA.
DR RefSeq; NP_608834.1; NM_134990.3.
DR AlphaFoldDB; Q9VQZ6; -.
DR SMR; Q9VQZ6; -.
DR BioGRID; 59843; 5.
DR IntAct; Q9VQZ6; 1.
DR STRING; 7227.FBpp0077129; -.
DR PaxDb; Q9VQZ6; -.
DR PRIDE; Q9VQZ6; -.
DR DNASU; 33649; -.
DR EnsemblMetazoa; FBtr0077439; FBpp0077129; FBgn0031604.
DR GeneID; 33649; -.
DR KEGG; dme:Dmel_CG15433; -.
DR UCSC; CG15433-RA; d. melanogaster.
DR CTD; 55140; -.
DR FlyBase; FBgn0031604; Elp3.
DR VEuPathDB; VectorBase:FBgn0031604; -.
DR eggNOG; KOG2535; Eukaryota.
DR GeneTree; ENSGT00390000013141; -.
DR HOGENOM; CLU_025983_2_1_1; -.
DR InParanoid; Q9VQZ6; -.
DR OMA; TFETRPD; -.
DR OrthoDB; 320059at2759; -.
DR PhylomeDB; Q9VQZ6; -.
DR BRENDA; 2.3.1.48; 1994.
DR SignaLink; Q9VQZ6; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 33649; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 33649; -.
DR PRO; PR:Q9VQZ6; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0031604; Expressed in egg chamber and 46 other tissues.
DR Genevisible; Q9VQZ6; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0033588; C:elongator holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
DR GO; GO:0008607; F:phosphorylase kinase regulator activity; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106261; F:tRNA uridine(34) acetyltransferase activity; IEA:RHEA.
DR GO; GO:0048789; P:cytoskeletal matrix organization at active zone; IMP:FlyBase.
DR GO; GO:0030097; P:hemopoiesis; IMP:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IMP:FlyBase.
DR GO; GO:0002168; P:instar larval development; IMP:FlyBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:FlyBase.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; IDA:FlyBase.
DR GO; GO:2000289; P:regulation of photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030431; P:sleep; IMP:FlyBase.
DR GO; GO:0050808; P:synapse organization; IMP:FlyBase.
DR GO; GO:0051124; P:synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR039661; ELP3.
DR InterPro; IPR034687; ELP3-like.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032432; Radical_SAM_C.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR11135; PTHR11135; 1.
DR PANTHER; PTHR11135:SF7; PTHR11135:SF7; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF16199; Radical_SAM_C; 1.
DR PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1.
DR SFLD; SFLDF00344; ELP3-like; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR TIGRFAMs; TIGR01211; ELP3; 1.
DR PROSITE; PS51186; GNAT; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Acyltransferase; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW tRNA processing; tRNA-binding.
FT CHAIN 1..552
FT /note="Elongator complex protein 3"
FT /id="PRO_0000283992"
FT DOMAIN 84..374
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 398..552
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q02908"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q02908"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q02908"
FT BINDING 166
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 476..479
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 499..501
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT BINDING 532
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:A0A1C7D1B7"
FT MUTAGEN 531
FT /note="Y->F: Embryonic lethality."
FT /evidence="ECO:0000269|PubMed:21288872"
SQ SEQUENCE 552 AA; 62821 MW; 3CE7D4D46EEE0C1F CRC64;
MKAKKKLGVG LSRQERQVLV IGEIIQELLK AHEAKKDVNL NRMKSLVASK YGLDSSPRLV
DIIAAVPQDA KKILLPKLRA KPIRTASGIA VVAVMCKPHR CPHINMTGNI CVYCPGGPDS
DFEYSTQSYT GYEPTSMRAI RSRYDPFLQT RHRVEQLKQL GHSVDKVEFI VMGGTFMCLP
EEYRDYFIRN LHDALSGHSS ANVAEAVRYS EKSRTKCIGI TIETRPDYCL KRHISDMLSY
GCTRLEIGVQ SVYEDVARDT NRGHTVRAVC ESFQLGKDAG YKIVTHMMPD LPNVDFERDI
EQFIEYFENP AFRSDGLKIY PTLVIRGTGL YELWKTGRYK SYPPSMLVDL VAKILALVPP
WTRVYRVQRD IPMPLVSSGV EHGNLRELAL ARMKDLGTTC RDVRTREVGI QEIHNKVRPY
EIELIRRDYV ANGGWETFLS YEDPEQDILV GLLRLRKCSP DTFRPELKGE CSIVRELHVY
GSVVPVNARD PTKFQHQGFG MLLMEEAERI AREEHGSTKL AVISGVGTRN YYRKMGYQLD
GPYMSKSIEE NN
