ID IF2G_DROME Reviewed; 475 AA.
AC Q24208; Q9VFA7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 3;
DE EC=3.6.5.3 {ECO:0000250|UniProtKB:P32481};
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit gamma;
DE Short=eIF2-gamma;
GN Name=eIF2gamma {ECO:0000312|FlyBase:FBgn0263740};
GN Synonyms=eIF-2gamma, eIF2g;
GN ORFNames=CG6476 {ECO:0000312|FlyBase:FBgn0263740};
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] (ISOFORM B), AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=7915232; DOI=10.1002/j.1460-2075.1994.tb06693.x;
RA Tschiersch B., Hofmann A., Krauss V., Dorn R., Korge G., Reuter G.;
RT "The protein encoded by the Drosophila position-effect variegation
RT suppressor gene Su(var)3-9 combines domains of antagonistic regulators of
RT homeotic gene complexes.";
RL EMBO J. 13:3822-3831(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Karsnas;
RX PubMed=11063691; DOI=10.1093/genetics/156.3.1157;
RA Krauss V., Reuter G.;
RT "Two genes become one: the genes encoding heterochromatin protein Su(var)3-
RT 9 and translation initiation factor subunit eIF-2gamma are joined to a
RT dicistronic unit in holometabolic insects.";
RL Genetics 156:1157-1167(2000).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORM B).
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).
CC -!- FUNCTION: As a subunit of eukaryotic initiation factor 2 eIF2, involved
CC in the early steps of protein synthesis. In the presence of GTP, eIF-2
CC forms a ternary complex with initiator tRNA Met-tRNAi and then recruits
CC the 40S ribosomal complex and initiation factors eIF-1, eIF-1A and eIF-
CC 3 to form the 43S pre-initiation complex (43S PIC), a step that
CC determines the rate of protein translation. The 43S PIC binds to mRNA
CC and scans downstream to the initiation codon, where it forms a 48S
CC initiation complex by codon-anticodon base pairing. This leads to the
CC displacement of eIF-1 to allow GTPase-activating protein (GAP) eIF-5-
CC mediated hydrolysis of eIF2-bound GTP. Hydrolysis of GTP and release of
CC Pi, which makes GTP hydrolysis irreversible, causes the release of the
CC eIF-2-GDP binary complex from the 40S subunit, an event that is
CC essential for the subsequent joining of the 60S ribosomal subunit to
CC form an elongation-competent 80S ribosome. In order for eIF-2 to
CC recycle and catalyze another round of initiation, the GDP bound to eIF-
CC 2 must be exchanged with GTP by way of a reaction catalyzed by GDP-GTP
CC exchange factor (GEF) eIF-2B. {ECO:0000250|UniProtKB:P32481}.
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; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P32481};
CC -!- SUBUNIT: Eukaryotic translation initiation factor 2 eIF2 is a
CC heterotrimeric complex composed of an alpha, a beta and a gamma
CC subunit. The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC ribosome. {ECO:0000250|UniProtKB:P32481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q09130}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=eIF-2gamma;
CC IsoId=Q24208-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q24208-2; Sequence=VSP_001432;
CC -!- DEVELOPMENTAL STAGE: Isoform B expressed maternally and zygotically.
CC Isoform B expressed throughout development, in larvae, in pupae and in
CC adult flies. {ECO:0000269|PubMed:7915232}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EIF2G subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; X80069; CAA56375.1; -; mRNA.
DR EMBL; AJ290956; CAB93767.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55153.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13641.1; -; Genomic_DNA.
DR EMBL; AY061102; AAL28650.1; -; mRNA.
DR PIR; S47005; S46941.
DR RefSeq; NP_001262587.1; NM_001275658.1. [Q24208-1]
DR RefSeq; NP_731993.1; NM_169629.2. [Q24208-1]
DR RefSeq; NP_731994.1; NM_169630.2. [Q24208-2]
DR AlphaFoldDB; Q24208; -.
DR SMR; Q24208; -.
DR BioGRID; 66907; 10.
DR STRING; 7227.FBpp0307983; -.
DR PaxDb; 7227-FBpp0302537; -.
DR DNASU; 41843; -.
DR EnsemblMetazoa; FBtr0310386; FBpp0302537; FBgn0263740. [Q24208-1]
DR EnsemblMetazoa; FBtr0310387; FBpp0302538; FBgn0263740. [Q24208-2]
DR EnsemblMetazoa; FBtr0337054; FBpp0307983; FBgn0263740. [Q24208-1]
DR GeneID; 41843; -.
DR KEGG; dme:Dmel_CG43665; -.
DR AGR; FB:FBgn0263740; -.
DR CTD; 41843; -.
DR FlyBase; FBgn0263740; eIF2gamma.
DR VEuPathDB; VectorBase:FBgn0263740; -.
DR eggNOG; KOG0466; Eukaryota.
DR GeneTree; ENSGT00940000172475; -.
DR InParanoid; Q24208; -.
DR OMA; NIGMVGH; -.
DR OrthoDB; 1512042at2759; -.
DR PhylomeDB; Q24208; -.
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; 41843; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 41843; -.
DR PRO; PR:Q24208; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0263740; Expressed in egg chamber and 47 other cell types or tissues.
DR ExpressionAtlas; Q24208; baseline and differential.
DR Genevisible; Q24208; DM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; ISS:FlyBase.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:UniProtKB.
DR GO; GO:0043614; C:multi-eIF complex; ISS:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:1990856; F:methionyl-initiator methionine tRNA binding; ISS:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:FlyBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; ISS:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; ISS:FlyBase.
DR CDD; cd01888; eIF2_gamma; 1.
DR CDD; cd03688; eIF2_gamma_II; 1.
DR CDD; cd15490; eIF2_gamma_III; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015256; eIF2g_C.
DR InterPro; IPR044127; eIF2g_dom_2.
DR InterPro; IPR044128; eIF2g_GTP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR PANTHER; PTHR42854; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3 FAMILY MEMBER; 1.
DR PANTHER; PTHR42854:SF3; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 3-RELATED; 1.
DR Pfam; PF09173; eIF2_C; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; GTP-binding; Hydrolase; Initiation factor;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..475
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 3"
FT /id="PRO_0000137444"
FT DOMAIN 38..247
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 47..54
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 75..79
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 133..136
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 189..192
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 224..226
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 456..468
FT /note="Interacts with CDC123"
FT /evidence="ECO:0000250|UniProtKB:P41091"
FT BINDING 50..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 189..192
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT BINDING 224..226
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32481"
FT VAR_SEQ 1..22
FT /note="MATAEAQIGVNRNLQKQDLSNL -> MHLRGDVLLGGVAA (in isoform
FT C)"
FT /evidence="ECO:0000305"
FT /id="VSP_001432"
SQ SEQUENCE 475 AA; 51485 MW; 8370B07089DD5422 CRC64;
MATAEAQIGV NRNLQKQDLS NLDVSKLTPL SPEVISRQAT INIGTIGHVA HGKSTVVKAI
SGVQTVRFKN ELERNITIKL GYANAKIYKC DNPKCPRPAS FVSDASSKDD SLPCTRLNCS
GNFRLVRHVS FVDCPGHDIL MATMLNGAAV MDAALLLIAG NESCPQPQTS EHLAAIEIMK
LKQILILQNK IDLIKESQAK EQYEEITKFV QGTVAEGAPI IPISAQLKYN IDVLCEYIVN
KIPVPPRDFN APPRLIVIRS FDVNKPGCEV ADLKGGVAGG SILSGVLKVG QEIEVRPGVV
TKDSDGNITC RPIFSRIVSL FAEQNELQYA VPGGLIGVGT KIDPTLCRAD RLVGQVLGAV
GQLPDIYQEL EISYYLLRRL LGVRTDGDKK GARVEKLQKN EILLVNIGSL STGGRISATK
GDLAKIVLTT PVCTEKGEKI ALSRRVENHW RLIGWGQIFG GKTITPVLDS QVAKK
//
