ELP3_XENLA
ID ELP3_XENLA Reviewed; 549 AA.
AC Q5HZM6;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Elongator complex protein 3 {ECO:0000250|UniProtKB:Q9H9T3};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:D5VRB9};
DE AltName: Full=tRNA uridine(34) acetyltransferase {ECO:0000305};
GN Name=elp3 {ECO:0000250|UniProtKB:Q9H9T3};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, INTERACTION WITH SNAI1 AND SNAI2, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=27189455; DOI=10.1038/srep26238;
RA Yang X., Li J., Zeng W., Li C., Mao B.;
RT "Elongator Protein 3 (Elp3) stabilizes Snail1 and regulates neural crest
RT migration in Xenopus.";
RL Sci. Rep. 6:26238-26238(2016).
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). Stabilizes transcriptional repressor snai1 by inhibiting
CC its ubiquitination which promotes neural crest cell migration
CC (PubMed:27189455). {ECO:0000250|UniProtKB:D5VRB9,
CC ECO:0000250|UniProtKB:Q9H9T3, ECO:0000269|PubMed:27189455}.
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 (By similarity). Interacts
CC with transcriptional repressors snai1 and snai2; interaction with snai1
CC inhibits snai1 ubiquitination and promotes snai1 stability
CC (PubMed:27189455). {ECO:0000250|UniProtKB:Q9H9T3,
CC ECO:0000269|PubMed:27189455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H9T3}. Nucleus
CC {ECO:0000250|UniProtKB:Q9H9T3}.
CC -!- TISSUE SPECIFICITY: In the embryo, detected at the animal pole at stage
CC 6.5. At stage 15, expressed at the anterior neural plate and its
CC border. At late neurulation, most abundant in the cranial neural crest.
CC At the tailbud stage, mainly expressed in the branchial arches and
CC eyes. {ECO:0000269|PubMed:27189455}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in inhibition of
CC neural crest cell migration and reduced expression of N-cadherin.
CC {ECO:0000269|PubMed:27189455}.
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}.
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DR EMBL; BC088956; AAH88956.1; -; mRNA.
DR RefSeq; NP_001088974.1; NM_001095505.1.
DR AlphaFoldDB; Q5HZM6; -.
DR SMR; Q5HZM6; -.
DR BioGRID; 106434; 1.
DR IntAct; Q5HZM6; 1.
DR DNASU; 496354; -.
DR GeneID; 496354; -.
DR KEGG; xla:496354; -.
DR CTD; 496354; -.
DR Xenbase; XB-GENE-957353; elp3.L.
DR OMA; TFETRPD; -.
DR OrthoDB; 320059at2759; -.
DR UniPathway; UPA00988; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 496354; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; ISS:UniProtKB.
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:SF0; PTHR11135:SF0; 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 SFLD; SFLDS00029; Radical_SAM; 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; Cytoplasm; Iron; Iron-sulfur; Metal-binding;
KW Nucleus; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..549
FT /note="Elongator complex protein 3"
FT /id="PRO_0000283990"
FT DOMAIN 84..374
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 398..549
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"
SQ SEQUENCE 549 AA; 62577 MW; 3DBC66E707E42063 CRC64;
MKPDRGMRGN MSQAELMMMT VADVIKQLVE AHEQGKDVNL NKLKTKTSAK YGLSAQPRLV
DIIAAVPPQY RKILVPKLKA KPIRTASGIA VVAVMCKPHR CPHINFTGNI CVYCPGGPDS
DFEYSTQSYT GYEPTSMRAI RARYDPYLQT RHRVEQLKQL GHNVDKVEFI VMGGTFMALP
EDYRDFFIRN LHDALSGHTS NSVSEAVRYS ERSNTKCVGI TIETRPDYCL KRHLSDMLCY
GCTRLEIGVQ SVYEDVARDT NRGHTVKAVC ESFHLSKDAG FKVVSHMMPD LPNMGLERDI
EQFIEFFENP AFRPDGMKLY PTLVIRGTGL YELWKTGRYR SYSPSTLVDL VARILALVPP
WTRVYRVQRD IPMPLVSSGV EHGNLRELAL ARMKDLGTEC RDVRTREVGI QEIHHKVRPY
QVELIRRDYV ANGGWETFLS YEDPEQDILI GLLRLRKCSE ESFRPELKGG VSIVRELHVY
GSVVPISSRD PSKFQHQGFG MLLMEEAERI ARDEHGSWKI AVISGVGTRN YYRKIGYELE
GPYMVKRLD
