IF5A_DROME
ID IF5A_DROME Reviewed; 159 AA.
AC Q9GU68; A0A1B2AK02; Q2MGM4; Q9NDH0; Q9W1C0;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Eukaryotic translation initiation factor 5A;
DE Short=eIF-5A;
GN Name=eEF5 {ECO:0000312|FlyBase:FBgn0285952};
GN ORFNames=CG3186 {ECO:0000312|FlyBase:FBgn0285952};
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 [MRNA].
RA Posey K.L., Roman G., He J., Cerda R., Davis R.L., Hardin S.H.;
RT "Drosophila melanogaster eukaryotic initiation factor 5A.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Irion U., Leptin M.;
RT "Drosophila homolog of eIF-5a.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6] {ECO:0000312|EMBL:ANY27489.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19546244; DOI=10.1083/jcb.200904161;
RA Patel P.H., Costa-Mattioli M., Schulze K.L., Bellen H.J.;
RT "The Drosophila deoxyhypusine hydroxylase homologue nero and its target
RT eIF5A are required for cell growth and the regulation of autophagy.";
RL J. Cell Biol. 185:1181-1194(2009).
CC -!- FUNCTION: mRNA-binding protein involved in translation elongation. Has
CC an important function at the level of mRNA turnover, probably acting
CC downstream of decapping. Critical for the efficient synthesis of
CC peptide bonds between consecutive proline residues. Can resolve
CC ribosomal stalling caused by consecutive prolines during translation
CC (By similarity). Involved in actin dynamics and cell cycle progression,
CC mRNA decay and probably in a pathway involved in stress response and
CC maintenance of cell wall integrity. Functions as a regulator of
CC apoptosis. {ECO:0000250|UniProtKB:P63241, ECO:0000269|PubMed:19546244}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Lys-51 undergoes hypusination, a unique post-translational
CC modification that consists in the addition of a butylamino group from
CC spermidine to lysine side chain, leading to the formation of the
CC unusual amino acid hypusine. eIF-5As are the only known proteins to
CC undergo this modification, which is essential for their function.
CC {ECO:0000250|UniProtKB:P63241, ECO:0000269|PubMed:19546244}.
CC -!- DISRUPTION PHENOTYPE: Severe larval growth defect.
CC {ECO:0000269|PubMed:19546244}.
CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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DR EMBL; AF159443; AAF80375.1; -; mRNA.
DR EMBL; AF187730; AAG17032.1; -; mRNA.
DR EMBL; AE013599; AAF47151.1; -; Genomic_DNA.
DR EMBL; AY071396; AAL49018.1; -; mRNA.
DR EMBL; KX531679; ANY27489.1; -; mRNA.
DR RefSeq; NP_611878.1; NM_138034.3.
DR RefSeq; NP_726411.1; NM_166654.2.
DR AlphaFoldDB; Q9GU68; -.
DR SMR; Q9GU68; -.
DR BioGRID; 63427; 51.
DR DIP; DIP-17842N; -.
DR IntAct; Q9GU68; 5.
DR STRING; 7227.FBpp0072081; -.
DR PaxDb; Q9GU68; -.
DR PRIDE; Q9GU68; -.
DR ABCD; Q9GU68; 1 sequenced antibody.
DR DNASU; 37846; -.
DR EnsemblMetazoa; FBtr0072172; FBpp0072081; FBgn0285952.
DR EnsemblMetazoa; FBtr0072173; FBpp0072082; FBgn0285952.
DR GeneID; 37846; -.
DR KEGG; dme:Dmel_CG3186; -.
DR UCSC; CG3186-RA; d. melanogaster.
DR CTD; 37846; -.
DR FlyBase; FBgn0285952; eEF5.
DR VEuPathDB; VectorBase:FBgn0285952; -.
DR eggNOG; KOG3271; Eukaryota.
DR GeneTree; ENSGT00390000003738; -.
DR HOGENOM; CLU_102600_0_0_1; -.
DR InParanoid; Q9GU68; -.
DR OMA; VFRNEYQ; -.
DR OrthoDB; 1370513at2759; -.
DR PhylomeDB; Q9GU68; -.
DR Reactome; R-DME-204626; Hypusine synthesis from eIF5A-lysine.
DR SignaLink; Q9GU68; -.
DR BioGRID-ORCS; 37846; 1 hit in 3 CRISPR screens.
DR ChiTaRS; eIF-5A; fly.
DR GenomeRNAi; 37846; -.
DR PRO; PR:Q9GU68; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0285952; Expressed in thoracico-abdominal ganglion (Drosophila) and 25 other tissues.
DR Genevisible; Q9GU68; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IMP:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0045901; P:positive regulation of translational elongation; IMP:UniProtKB.
DR GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR GO; GO:0019953; P:sexual reproduction; IEP:FlyBase.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR001884; IF5A-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR InterPro; IPR020189; Transl_elong_IF5A_C.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR11673; PTHR11673; 1.
DR Pfam; PF01287; eIF-5a; 1.
DR PIRSF; PIRSF003025; eIF5A; 1.
DR SMART; SM01376; eIF-5a; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00037; eIF_5A; 1.
DR PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Elongation factor; Hypusine; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..159
FT /note="Eukaryotic translation initiation factor 5A"
FT /id="PRO_0000142460"
FT MOD_RES 51
FT /note="Hypusine"
FT /evidence="ECO:0000250|UniProtKB:P63241"
FT CONFLICT 7
FT /note="Q -> H (in Ref. 1; AAF80375 and 2; AAG17032)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="E -> D (in Ref. 2; AAG17032)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 17591 MW; 3F348B25D5AEA040 CRC64;
MAELDDQFET TDSGASTTYP MQCSALRKNG FVMLKSRPCK IVEMSTSKTG KHGHAKVHMV
GIDIFSNKKY EDICPSTHNM DVPNVKREDL QLIAISDDSF LTLMTESGDL REDLKVPEGE
LGEQLRLDFD SGKDLLCTVL KACGEECVIA IKTNTALDK
