ELP1_DROME
ID ELP1_DROME Reviewed; 1252 AA.
AC Q9VGK7; Q8MRJ9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Elongator complex protein 1;
DE Short=ELP1;
GN Name=Elp1; ORFNames=CG10535;
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=Ovary;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1094, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine) (By similarity). The elongator complex
CC catalyzes formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (By similarity). ELP1 binds to tRNA, mediating
CC interaction of the elongator complex with tRNA (By similarity).
CC {ECO:0000250|UniProtKB:O95163, ECO:0000250|UniProtKB:Q06706}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:O95163}.
CC -!- SUBUNIT: Homodimer. Component of the elongator complex.
CC {ECO:0000250|UniProtKB:O95163}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95163}. Nucleus
CC {ECO:0000250|UniProtKB:O95163}.
CC -!- SIMILARITY: Belongs to the ELP1/IKA1 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:O95163}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50216.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF54670.2; -; Genomic_DNA.
DR EMBL; AY119562; AAM50216.1; ALT_INIT; mRNA.
DR RefSeq; NP_650098.1; NM_141841.2.
DR AlphaFoldDB; Q9VGK7; -.
DR SMR; Q9VGK7; -.
DR BioGRID; 66527; 8.
DR IntAct; Q9VGK7; 2.
DR STRING; 7227.FBpp0081896; -.
DR iPTMnet; Q9VGK7; -.
DR PaxDb; Q9VGK7; -.
DR EnsemblMetazoa; FBtr0082420; FBpp0081896; FBgn0037926.
DR GeneID; 41399; -.
DR KEGG; dme:Dmel_CG10535; -.
DR UCSC; CG10535-RA; d. melanogaster.
DR CTD; 8518; -.
DR FlyBase; FBgn0037926; Elp1.
DR VEuPathDB; VectorBase:FBgn0037926; -.
DR eggNOG; KOG1920; Eukaryota.
DR GeneTree; ENSGT00390000013344; -.
DR InParanoid; Q9VGK7; -.
DR PhylomeDB; Q9VGK7; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 41399; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 41399; -.
DR PRO; PR:Q9VGK7; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037926; Expressed in oviduct (Drosophila) and 37 other tissues.
DR ExpressionAtlas; Q9VGK7; baseline and differential.
DR Genevisible; Q9VGK7; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033588; C:elongator holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0009047; P:dosage compensation by hyperactivation of X chromosome; IGI:FlyBase.
DR GO; GO:0002926; P:tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006849; Elp1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR12747; PTHR12747; 1.
DR Pfam; PF04762; IKI3; 1.
DR PIRSF; PIRSF017233; IKAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..1252
FT /note="Elongator complex protein 1"
FT /id="PRO_0000283999"
FT REGION 814..1252
FT /note="Mediates dimerization"
FT /evidence="ECO:0000250|UniProtKB:O95163"
FT REGION 1097..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1129
FT /note="Required for binding to tRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06706"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 77
FT /note="V -> A (in Ref. 3; AAM50216)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="T -> A (in Ref. 3; AAM50216)"
FT /evidence="ECO:0000305"
FT CONFLICT 614..616
FT /note="QLD -> RLV (in Ref. 3; AAM50216)"
FT /evidence="ECO:0000305"
FT CONFLICT 1106
FT /note="R -> G (in Ref. 3; AAM50216)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1252 AA; 142814 MW; E511D1DE81DE5AC5 CRC64;
MRNLKLRYCK ELNAVAHPQH LLLQPELNGG ASDIYFVVAD NKIYAVQESG DVRLKVIADL
PDIVGVEFLQ LDNAICVASG AGEVILVDPQ TGATSEGTFC DVGIESMAWS PNQEVVAFVT
RTHNVVLMTS TFDVIAEQPL DAELDPDQQF VNVGWGKKET QFHGSEGKQA AKQKESDSTF
IRDEQELNQD VSISWRGDGE FFVVSYVAAQ LGRTFKVYDS EGKLNHTAEK SANLKDSVVW
RPTGNWIAVP QQFPNKSTIA LFEKNGLRHR ELVLPFDLQE EPVVQLRWSE DSDILAIRTC
AKEEQRVYLY TIGNYHWYLK QVLIFEQADP LALLHWDTRC GAEHTLHVLK ESGKHLVYRW
AFAVDRNNSI VGVIDGKRLL LTDFDEAIVP PPMSKIVLKF ETYINAFISH GTSLWVYTCD
RKIYLNEHIH TLGKELQKPI MLMPDAELSG LHLANLTHFS PHYLLATHSS AGSTRLLLLS
YKDNDNKPGE WFYRVHSSVR INGLVNAVAV APYAMNEFYV QTVNNGHTYE VSLKADKTLK
VERSYVQLHE PADQIDWVIV KGCIWDGYTG ALVTLRNQHL LHIDGYRIGE DVTSFCVVTN
YLVYTQLNAM HFVQLDDRRQ VASRNIERGA KIVTAVARKA RVVLQLPRGN LEAICPRVLV
LELVGDLLER GKYQKAIEMS RKQRINLNII FDHDVKRFVS SVGAFLNDIN EPQWLCLFLS
ELQNEDFTKG MYSSNYDASK QTYPSDYRVD QKVEYVCRLL EQQMNRFVSR FRLPLITAYV
KLGCLEMALQ VIWKEQQEDA SLADQLLQHL LYLVDVNDLY NVALGTYDFG LVLFVAQKSQ
KDPKEFLPYL NDLKALPIDY RKFRIDDHLK RYTSALSHLA ACGEQHYEEA LEYIRKHGLY
TDGLAFYREH IEFQKNIYVA YADHLRAIAK LDNASLMYER GGQLQQALLS AKHTLDWQRV
LVLAKKLSEP LDQVAQSLVG PLQQQGRHME AYELVKEHCQ DRKRQFDVLL EGHLYSRAIY
EAGLEDDDVS EKIAPALLAY GVQLESSLQA DLQLFLDYKQ RLLDIRRNQA KSGEGYIDTD
VNLKEVDLLS DTTSLHSSQY SGTSRRTGKT FRSSKNRRKH ERKLFSLKPG NPFEDIALID
ALHNHVTKIA QQQQPVRDTC KALLQLANAA DADPLAAALQ REFKTLLQAV DAALDEIWTP
ELRGNGLMAD HLTGPNVDYL ALQKEQRYAL LSPLKRFKPQ LIMMDWQHEI LQ
