IF2B_DROME
ID IF2B_DROME Reviewed; 312 AA.
AC P41375; Q8SYX9; Q9VTZ3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE Short=eIF-2-beta;
GN Name=eIF2beta {ECO:0000312|FlyBase:FBgn0004926};
GN Synonyms=eIF-2beta {ECO:0000303|PubMed:8194763};
GN ORFNames=CG4153 {ECO:0000312|FlyBase:FBgn0004926};
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].
RC STRAIN=Oregon-R; TISSUE=Embryo, and Pupae;
RX PubMed=8194763; DOI=10.1016/0378-1119(94)90273-9;
RA Ye X., Cavener D.R.;
RT "Isolation and characterization of the Drosophila melanogaster gene
RT encoding translation-initiation factor eIF-2 beta.";
RL Gene 142:271-274(1994).
RN [2]
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND THR-145, AND
RP 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: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA. This
CC preinitiation complex mediates ribosomal recognition of a start codon
CC during the scanning process of the leader region.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; L19197; AAA28504.1; -; mRNA.
DR EMBL; AE014296; AAF49902.1; -; Genomic_DNA.
DR EMBL; AY071253; AAL48875.1; -; mRNA.
DR RefSeq; NP_524043.1; NM_079319.4.
DR AlphaFoldDB; P41375; -.
DR SMR; P41375; -.
DR BioGRID; 64782; 10.
DR DIP; DIP-21095N; -.
DR IntAct; P41375; 1.
DR STRING; 7227.FBpp0075700; -.
DR iPTMnet; P41375; -.
DR SwissPalm; P41375; -.
DR PaxDb; P41375; -.
DR PRIDE; P41375; -.
DR EnsemblMetazoa; FBtr0075968; FBpp0075700; FBgn0004926.
DR GeneID; 39433; -.
DR KEGG; dme:Dmel_CG4153; -.
DR CTD; 39433; -.
DR FlyBase; FBgn0004926; eIF2beta.
DR VEuPathDB; VectorBase:FBgn0004926; -.
DR eggNOG; KOG2768; Eukaryota.
DR GeneTree; ENSGT00390000001804; -.
DR HOGENOM; CLU_026663_0_1_1; -.
DR InParanoid; P41375; -.
DR OMA; CMREGNK; -.
DR OrthoDB; 1178655at2759; -.
DR PhylomeDB; P41375; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-381042; PERK regulates gene expression.
DR Reactome; R-DME-382556; ABC-family proteins mediated transport.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DME-72731; Recycling of eIF2:GDP.
DR BioGRID-ORCS; 39433; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39433; -.
DR PRO; PR:P41375; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004926; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P41375; baseline and differential.
DR Genevisible; P41375; DM.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; ISS:FlyBase.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:FlyBase.
DR GO; GO:0043614; C:multi-eIF complex; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:FlyBase.
DR GO; GO:0031369; F:translation initiation factor binding; IBA:GO_Central.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP: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; ISS:FlyBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:FlyBase.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
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 PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
PE 1: Evidence at protein level;
KW Initiation factor; Metal-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..312
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 2"
FT /id="PRO_0000137409"
FT ZN_FING 260..284
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 26..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 60
FT /note="S -> G (in Ref. 4; AAL48875)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="K -> E (in Ref. 4; AAL48875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 35218 MW; 163B98C43A35A764 CRC64;
MDAEDGFDPT LLKKKKKKKT TFDLDAALGL EDDTKKEDPQ DEASAEGGAA AEEDNLDLES
FGKKKKKKKK PFNMDEIEAA IPSFGGDDVA ASEEPEEEEI NLDMDFSMAK KKKKSKKKEL
DELFADQADD DKSEDKENDE DNSSTWFGSD RDYTYDELLK RVFEIILDKN PDMAAGRKPK
FVMRPPQVLR VGTKKTSFAN FMDIAKTLHR LPKHLLDFLL AELGTSGSMD GNQQLIIKGR
FQPKQIENVL RRYIKEYVTC HTCRSPETIL QKDTRLFFLQ CESCGSRCSV ASIKSGFQAV
TGKRAAIRAK TT
