GenomeNet

Database: UniProt
Entry: Q1LYG5_DANRE
LinkDB: Q1LYG5_DANRE
Original site: Q1LYG5_DANRE 
ID   Q1LYG5_DANRE            Unreviewed;       854 AA.
AC   Q1LYG5; A0A8M1NA43;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   SubName: Full=Eukaryotic translation elongation factor 2a, tandem duplicate 1 {ECO:0000313|Ensembl:ENSDARP00000118068, ECO:0000313|RefSeq:NP_001038626.2};
GN   Name=eef2a.1 {ECO:0000313|Ensembl:ENSDARP00000118068,
GN   ECO:0000313|RefSeq:NP_001038626.2,
GN   ECO:0000313|ZFIN:ZDB-GENE-050522-500};
GN   Synonyms=si:dkey-110c1.3 {ECO:0000313|RefSeq:NP_001038626.2},
GN   zgc:113191 {ECO:0000313|RefSeq:NP_001038626.2};
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 {ECO:0000313|Ensembl:ENSDARP00000118068};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000118068, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118068};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   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] {ECO:0000313|Ensembl:ENSDARP00000118068}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000118068};
RG   Ensembl;
RL   Submitted (AUG-2013) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:NP_001038626.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001038626.2};
RX   PubMed=25260251;
RA   Hatef A., Shajan S., Unniappan S.;
RT   "Nutrient status modulates the expression of nesfatin-1 encoding
RT   nucleobindin 2A and 2B mRNAs in zebrafish gut, liver and brain.";
RL   Gen. Comp. Endocrinol. 215:51-60(2015).
RN   [4] {ECO:0000313|RefSeq:NP_001038626.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001038626.2};
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [5] {ECO:0000313|RefSeq:NP_001038626.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001038626.2};
RX   PubMed=26226634;
RA   Hatef A., Yufa R., Unniappan S.;
RT   "Ghrelin O-Acyl Transferase in Zebrafish Is an Evolutionarily Conserved
RT   Peptide Upregulated During Calorie Restriction.";
RL   Zebrafish 12:327-338(2015).
RN   [6] {ECO:0000313|RefSeq:NP_001038626.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001038626.2};
RX   PubMed=28252024;
RA   Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA   Choudhary J.S., Emes R.D., Grant S.G.;
RT   "Evolution of complexity in the zebrafish synapse proteome.";
RL   Nat. Commun. 8:14613-14613(2017).
RN   [7] {ECO:0000313|RefSeq:NP_001038626.2}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001038626.2};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; BX005203; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001038626.2; NM_001045161.2.
DR   STRING; 7955.ENSDARP00000118068; -.
DR   PaxDb; 7955-ENSDARP00000118068; -.
DR   Ensembl; ENSDART00000143641; ENSDARP00000118068; ENSDARG00000042094.
DR   Ensembl; ENSDART00000143641.3; ENSDARP00000118068.1; ENSDARG00000042094.8.
DR   GeneID; 792182; -.
DR   KEGG; dre:792182; -.
DR   AGR; ZFIN:ZDB-GENE-050522-500; -.
DR   CTD; 792182; -.
DR   ZFIN; ZDB-GENE-050522-500; eef2a.1.
DR   eggNOG; KOG0469; Eukaryota.
DR   HOGENOM; CLU_002794_11_2_1; -.
DR   OrthoDB; 166721at2759; -.
DR   PhylomeDB; Q1LYG5; -.
DR   TreeFam; TF300575; -.
DR   Reactome; R-DRE-156902; Peptide chain elongation.
DR   Reactome; R-DRE-5358493; Synthesis of diphthamide-EEF2.
DR   Reactome; R-DRE-6798695; Neutrophil degranulation.
DR   Reactome; R-DRE-8876725; Protein methylation.
DR   Proteomes; UP000000437; Alternate scaffold 22.
DR   Proteomes; UP000000437; Chromosome 22.
DR   Bgee; ENSDARG00000042094; Expressed in gastrula and 26 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR   GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR   CDD; cd01681; aeEF2_snRNP_like_IV; 1.
DR   CDD; cd04096; eEF2_snRNP_like_C; 1.
DR   CDD; cd01885; EF2; 1.
DR   CDD; cd16261; EF2_snRNP_III; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR041095; EFG_II.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR42908:SF29; EUKARYOTIC TRANSLATION ELONGATION FACTOR 2B-RELATED; 1.
DR   PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF14492; EFG_III; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   1: Evidence at protein level;
KW   Elongation factor {ECO:0000313|RefSeq:NP_001038626.2};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q1LYG5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   DOMAIN          17..360
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   854 AA;  94978 MW;  E98DDD2D4F59B149 CRC64;
     MENFNVDQIR ATMDKKSNIR NMSVIGAFDH GKSTLTDWLV SEAGIVSSAR AGETRFMDTR
     RDEQERCITI KSTAISIFYE LAEKDLAFIK ECKDGSGFLL NLIDSPGHVD FSSEVTAALR
     ITDGALLVVD CVSGVCLQTE TVLRQAIGER IKPVLMINKM DRALLELQLV PEELYQIFQR
     IVEKVNVTIS TYAEDEKGPM GNVMIDPVIG NLAFGSGLHG WAFTLKQFAE LYVKKFAGKA
     QLGPEEYIKK VEDMIKRLWG DSYFDSTTGK FSESATSPDG KKLPRTFVHL VLDPIFKVFD
     AIMNFKKEET VKLIEKMGIK LDVEDKEKEG KILLKAVMRC WLPAGEALLQ MITIHLPSPV
     TAQIYRCELL YEGPGDDEAA MGIKNCDPKA PLMMYISKMI PTSDKGCFYA FGRVFSGCVS
     TGLNVRIMGP NFTPGKKDDL YLKPIQRTVL MMGRYVEPIE DVPCGNIVGL LGVDQFLVKT
     GTITTFTKAY NMRVMKFSVS PVVRVSVEVM DPADLPKLVE GLKHLAKSDP MLQCIIEDTG
     EHIIAGAGEL HLEICLKDLE EDHACIPLKK SDPFASYRET VSDGSKQLCL AKTPNKHSRL
     FMKACPLADG LAEDIDKGRV TASQEMNARA QYLAENYKWE VTEARKIWCF GPEGTGPNIL
     VDLTKRVQYL NEIKDSVIAG FQWATREGVL CAENMRGIRF DIHDATLTST AIHRGPGQII
     VATRRVLYGC QLTAEPRLSE PIYLVEMQCP ESVIGNVYGE LVRRRGVVFS ESQVMGTPVY
     LLKAYLPVSE SFGFTADLCA NTSGQAFSQC VFDHWQILPG DPMDPTSKVA HIMADIRKSK
     GLDEAIPALH CYLD
//
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