ELP2_DANRE
ID ELP2_DANRE Reviewed; 821 AA.
AC Q05AM5; Q1LUN8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Elongator complex protein 2;
DE Short=ELP2;
GN Name=elp2; ORFNames=si:dkey-190l1.1, zgc:153559;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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). The elongator complex catalyzes the
CC formation of carboxymethyluridine in the wobble base at position 34 in
CC tRNAs. {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- SUBUNIT: Component of the elongator complex.
CC {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6IA86}. Nucleus
CC {ECO:0000250|UniProtKB:Q6IA86}.
CC -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is
CC required for elongator complex assembly.
CC {ECO:0000250|UniProtKB:P42935}.
CC -!- SIMILARITY: Belongs to the WD repeat ELP2 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:Q6IA86}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK05339.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX927389; CAK05339.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC124388; AAI24389.1; -; mRNA.
DR AlphaFoldDB; Q05AM5; -.
DR SMR; Q05AM5; -.
DR STRING; 7955.ENSDARP00000104754; -.
DR PaxDb; Q05AM5; -.
DR PeptideAtlas; Q05AM5; -.
DR ZFIN; ZDB-GENE-060503-525; elp2.
DR eggNOG; KOG1063; Eukaryota.
DR InParanoid; Q05AM5; -.
DR PhylomeDB; Q05AM5; -.
DR TreeFam; TF105985; -.
DR UniPathway; UPA00988; -.
DR PRO; PR:Q05AM5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033588; C:elongator holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 2.130.10.10; -; 6.
DR InterPro; IPR037289; Elp2.
DR InterPro; IPR011048; Haem_d1_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44111; PTHR44111; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 11.
DR SUPFAM; SSF50978; SSF50978; 2.
DR SUPFAM; SSF51004; SSF51004; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..821
FT /note="Elongator complex protein 2"
FT /id="PRO_0000284000"
FT REPEAT 14..53
FT /note="WD 1"
FT REPEAT 54..98
FT /note="WD 2"
FT REPEAT 103..145
FT /note="WD 3"
FT REPEAT 151..193
FT /note="WD 4"
FT REPEAT 198..239
FT /note="WD 5"
FT REPEAT 271..319
FT /note="WD 6"
FT REPEAT 329..368
FT /note="WD 7"
FT REPEAT 374..413
FT /note="WD 8"
FT REPEAT 424..462
FT /note="WD 9"
FT REPEAT 602..641
FT /note="WD 10"
FT REPEAT 656..695
FT /note="WD 11"
FT REPEAT 715..754
FT /note="WD 12"
FT REPEAT 769..821
FT /note="WD 13"
FT CONFLICT 689
FT /note="V -> G (in Ref. 1; CAK05339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 821 AA; 90083 MW; D2DCBF260C16C2ED CRC64;
MAAPVMDTCH VSCCANRAPN VVSWGRGGLI AFGTCNSVAI YNPEEIRVVD LLNKHTGRVN
AVQWVHEPDC SPENQLISGG SDNNVIVWEK LDGKFRACAV CSGHSGPVCA VDAVSLSSSH
LLVASASSDS TVKLWTYSSD AAECLQTVAF GSGFMMDVSL ALLPGSRVPV LACGGDDSRV
HLYVQLSGQF QRVLTLTGHE DWVRGVEWAN KDGELWLASC SQDCLIRVWR LFAKTAAEPD
LQTDGIIKMK ENIFQVSGEE FAVTLETVLA GHENWVYGIH WQPPSVKGDS VEQSLKLLSA
SMDKTMILWG PEEDSGMWVE MVRVGEVGGN TLGFYGCQMS PDGSMILAHA FHGALHLWHH
DSNQEWRPSV VISGHFNAVQ DMSWDPEGEF IITVGSDQTT RLFTPWTRKG SSQITWHEIS
RPQIHGYDMQ CLTMVGRFQF VSGADEKVLR VFKAPRNFVE NFAHISGTSL EKLLGCNDIA
DLPEGASTPA LGLSNKAVFQ GDLASPSPQQ DGGDFNSLSD QYKESYFQPL KLAEPPTEDD
LLQNTLWPEV QKLYGHGFEM FCLASDCART VVASACKASK AEHASILLWS TASWKQLQSL
SCHSLTITQM AFSPNGQLLL AVSRDRTWSL WRRGNPDLDT EAMFSLYANT SKDTSVHTRI
IWSCDWSADN KYFVTSSRDK KVIIWGHAVS GVAVGEGEDA RVTSCSSVLD VGDSATAVSI
CPFLCSDHSY LLAVGLENGQ ILLYKWKPLE DLSSESDWSR CKDTDACQGH TMVVKRLRWR
PRLGRGGHGG QDSKEEQAWV QLASAGADHV VKIFDINLSA L