IF2A_DROME
ID IF2A_DROME Reviewed; 341 AA.
AC P41374; Q9V3G2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Eukaryotic translation initiation factor 2 subunit 1;
DE AltName: Full=Eukaryotic translation initiation factor 2 subunit alpha;
DE Short=eIF-2-alpha;
GN Name=eIF2alpha {ECO:0000312|FlyBase:FBgn0261609};
GN Synonyms=eIF2-alpha {ECO:0000312|FlyBase:FBgn0261609},
GN eIF2a {ECO:0000312|FlyBase:FBgn0261609};
GN ORFNames=CG9946 {ECO:0000312|FlyBase:FBgn0261609};
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;
RX PubMed=8144032; DOI=10.1016/0378-1119(94)90550-9;
RA Qu S., Cavener D.R.;
RT "Isolation and characterization of the Drosophila melanogaster eIF-2 alpha
RT gene encoding the alpha subunit of translation initiation factor eIF-2.";
RL Gene 140:239-242(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=Head;
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: 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 -!- PTM: Phosphorylation of eIF-2-alpha impairs the recycling of eIF-2
CC between successive rounds of initiation and thus leads to inhibition of
CC translation.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
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DR EMBL; L19196; AAA53627.1; -; mRNA.
DR EMBL; AE014298; AAF48615.1; -; Genomic_DNA.
DR EMBL; AF145633; AAD38608.1; -; mRNA.
DR RefSeq; NP_001285329.1; NM_001298400.1.
DR RefSeq; NP_573130.1; NM_132902.4.
DR AlphaFoldDB; P41374; -.
DR SMR; P41374; -.
DR BioGRID; 58956; 18.
DR DIP; DIP-23926N; -.
DR IntAct; P41374; 3.
DR STRING; 7227.FBpp0074075; -.
DR iPTMnet; P41374; -.
DR PaxDb; P41374; -.
DR PRIDE; P41374; -.
DR ABCD; P41374; 2 sequenced antibodies.
DR DNASU; 32617; -.
DR EnsemblMetazoa; FBtr0074300; FBpp0074075; FBgn0261609.
DR EnsemblMetazoa; FBtr0343016; FBpp0309768; FBgn0261609.
DR GeneID; 32617; -.
DR KEGG; dme:Dmel_CG9946; -.
DR CTD; 32617; -.
DR FlyBase; FBgn0261609; eIF2alpha.
DR VEuPathDB; VectorBase:FBgn0261609; -.
DR eggNOG; KOG2916; Eukaryota.
DR HOGENOM; CLU_033458_0_0_1; -.
DR InParanoid; P41374; -.
DR OMA; DVNEHQR; -.
DR OrthoDB; 1093186at2759; -.
DR PhylomeDB; P41374; -.
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 SignaLink; P41374; -.
DR BioGRID-ORCS; 32617; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 32617; -.
DR PRO; PR:P41374; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0261609; Expressed in secondary oocyte and 23 other tissues.
DR ExpressionAtlas; P41374; baseline and differential.
DR Genevisible; P41374; DM.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IBA:GO_Central.
DR GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; ISS:FlyBase.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:FlyBase.
DR GO; GO:0043614; C:multi-eIF complex; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IGI:FlyBase.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 1.10.150.190; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.1130; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; PTHR10602; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; SSF110993; 1.
DR SUPFAM; SSF116742; SSF116742; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
PE 2: Evidence at transcript level;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..341
FT /note="Eukaryotic translation initiation factor 2 subunit
FT 1"
FT /id="PRO_0000137387"
FT DOMAIN 16..87
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 293..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 38646 MW; D06D1B6FBC628DF6 CRC64;
MALTSRFYNE RYPEIEDVVM VNVLSIAEMG AYVHLLEYNN IEGMILLSEL SRRRIRSINK
LIRVGKTEPV VVIRVDKEKG YIDLSKRRVS PEDVEKCTER FAKAKAINSL LRHVADILGF
EGNEKLEDLY QKTAWHFEKK YNNKTVAYDI FKQSVTDPTV FDECNLEPET KEVLLSNIKR
KLVSPTVKIR ADIECSCYGY EGIDAVKASL TKGLELSTEE LPIRINLIAP PLYVMTTSTT
KKTDGLKALE VAIEHIRAKT SEYDGEFKVI MAPKLVTAID EADLARRLER AEAENAQVAG
DDDEEDGADQ EGMQFDPEKE FNHKGSGAGR ANEEDEEEEE D
