IF5_DROME
ID IF5_DROME Reviewed; 464 AA.
AC Q9VXK6; A4V4K0; Q0KHS2;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=eIF5; ORFNames=CG9177;
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-9; SER-412; SER-413 AND
RP SER-415, AND IDENTIFICATION BY 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: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]) (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48553.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65378.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65379.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65380.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65381.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65382.1; -; Genomic_DNA.
DR EMBL; AY060843; AAL28391.1; -; mRNA.
DR RefSeq; NP_573098.1; NM_132870.4.
DR RefSeq; NP_727922.1; NM_167477.2.
DR RefSeq; NP_996477.1; NM_206754.2.
DR RefSeq; NP_996478.1; NM_206755.2.
DR RefSeq; NP_996479.1; NM_206756.2.
DR RefSeq; NP_996480.1; NM_206757.2.
DR RefSeq; NP_996481.1; NM_206758.2.
DR AlphaFoldDB; Q9VXK6; -.
DR SMR; Q9VXK6; -.
DR BioGRID; 58910; 7.
DR DIP; DIP-21354N; -.
DR IntAct; Q9VXK6; 1.
DR STRING; 7227.FBpp0073947; -.
DR iPTMnet; Q9VXK6; -.
DR PaxDb; Q9VXK6; -.
DR PRIDE; Q9VXK6; -.
DR EnsemblMetazoa; FBtr0074144; FBpp0073947; FBgn0030719.
DR EnsemblMetazoa; FBtr0074145; FBpp0073948; FBgn0030719.
DR EnsemblMetazoa; FBtr0074146; FBpp0089136; FBgn0030719.
DR EnsemblMetazoa; FBtr0074147; FBpp0089137; FBgn0030719.
DR EnsemblMetazoa; FBtr0074148; FBpp0089138; FBgn0030719.
DR EnsemblMetazoa; FBtr0074149; FBpp0089139; FBgn0030719.
DR EnsemblMetazoa; FBtr0074150; FBpp0089140; FBgn0030719.
DR GeneID; 32566; -.
DR KEGG; dme:Dmel_CG9177; -.
DR UCSC; CG9177-RA; d. melanogaster.
DR CTD; 1983; -.
DR FlyBase; FBgn0030719; eIF5.
DR VEuPathDB; VectorBase:FBgn0030719; -.
DR eggNOG; KOG2767; Eukaryota.
DR GeneTree; ENSGT00390000016478; -.
DR HOGENOM; CLU_026663_1_0_1; -.
DR InParanoid; Q9VXK6; -.
DR OMA; YRYKMEK; -.
DR PhylomeDB; Q9VXK6; -.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR BioGRID-ORCS; 32566; 0 hits in 1 CRISPR screen.
DR ChiTaRS; eIF5; fly.
DR GenomeRNAi; 32566; -.
DR PRO; PR:Q9VXK6; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030719; Expressed in ovary and 27 other tissues.
DR Genevisible; Q9VXK6; DM.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:FlyBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..464
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000212520"
FT DOMAIN 254..415
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 145..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 464 AA; 51700 MW; B236088EA54FD880 CRC64;
MATVNVNRSV TDIFYRYKMP RLQAKVEGKG NGIKTVLVNM AEVARAIGRP ATYPTKYFGC
ELGAQTLFDH KNERFVVNGS HDVNKLQDLL DGFIRKFVLC PECDNPETNL TVSAKNQTIS
QSCKACGFHG LLKVNHKVNT FIVKNPPSLN PAAQGSSLTE GKRSRKQKQK NDNADGSMTN
NSLANNSGGE SDGGNGTNQA SQTEAEISAA IPEKTAKDDD DEGWSVDVSK EAIRARLQDL
TDGAKGMTIS DDYDKTEKER IDIFYELVKD KRDKKQLDDV QTHKELVIEA ERLDIINKAP
LVLAELLFTE NIIKDVQKNR PLLLRFTLNN PKAQRYLIGG VEQTVELHKG ILMSKVAGIF
KLFYDLDILD EAVILEWAQK VSKRHVSKNI AAEIHEKAMP FVLWLKNAEE ESSESEEEED
DESEEDNYVS SAGQRGGQRV VQRGIPRAVA GDEDDEDDVN IDDI
