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Database: UniProt
Entry: P20459
LinkDB: P20459
Original site: P20459 
ID   IF2A_YEAST              Reviewed;         304 AA.
AC   P20459; D6VWI2; E9P8T6;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   07-APR-2021, entry version 195.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit alpha;
DE            Short=eIF-2-alpha;
GN   Name=SUI2 {ECO:0000303|PubMed:2649894, ECO:0000312|SGD:S000003767};
GN   Synonyms=TIF211; OrderedLocusNames=YJR007W; ORFNames=J1429;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2649894; DOI=10.1073/pnas.86.8.2784;
RA   Cigan A.M., Pabich E.K., Feng L., Donahue T.F.;
RT   "Yeast translation initiation suppressor sui2 encodes the alpha subunit of
RT   eukaryotic initiation factor 2 and shares sequence identity with the human
RT   alpha subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:2784-2788(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [5]
RP   FUNCTION, PHOSPHORYLATION AT SER-52 BY GCN2, AND MUTAGENESIS OF SER-52.
RX   PubMed=1739968; DOI=10.1016/0092-8674(92)90193-g;
RA   Dever T.E., Feng L., Wek R.C., Cigan A.M., Donahue T.F., Hinnebusch A.G.;
RT   "Phosphorylation of initiation factor 2 alpha by protein kinase GCN2
RT   mediates gene-specific translational control of GCN4 in yeast.";
RL   Cell 68:585-596(1992).
RN   [6]
RP   PHOSPHORYLATION AT SER-52 BY GCN2.
RX   PubMed=8336737; DOI=10.1128/mcb.13.8.5099;
RA   Rolfes R.J., Hinnebusch A.G.;
RT   "Translation of the yeast transcriptional activator GCN4 is stimulated by
RT   purine limitation: implications for activation of the protein kinase
RT   GCN2.";
RL   Mol. Cell. Biol. 13:5099-5111(1993).
RN   [7]
RP   PHOSPHORYLATION AT SER-52 DURING CARBON STARVATION, AND MUTAGENESIS OF
RP   SER-52.
RX   PubMed=10733573; DOI=10.1128/mcb.20.8.2706-2717.2000;
RA   Yang R., Wek S.A., Wek R.C.;
RT   "Glucose limitation induces GCN4 translation by activation of Gcn2 protein
RT   kinase.";
RL   Mol. Cell. Biol. 20:2706-2717(2000).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292 AND SER-294, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 2-176.
RX   PubMed=14607111; DOI=10.1016/j.jmb.2003.09.045;
RA   Dhaliwal S., Hoffman D.W.;
RT   "The crystal structure of the N-terminal region of the alpha subunit of
RT   translation initiation factor 2 (eIF2alpha) from Saccharomyces cerevisiae
RT   provides a view of the loop containing serine 51, the target of the
RT   eIF2alpha-specific kinases.";
RL   J. Mol. Biol. 334:187-195(2003).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 4-176.
RX   PubMed=16179258; DOI=10.1016/j.cell.2005.06.044;
RA   Dar A.C., Dever T.E., Sicheri F.;
RT   "Higher-order substrate recognition of eIF2alpha by the RNA-dependent
RT   protein kinase PKR.";
RL   Cell 122:887-900(2005).
CC   -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC       forming a ternary complex with GTP and initiator tRNA. This complex
CC       binds to a 40S ribosomal subunit, followed by mRNA binding to form a
CC       43S pre-initiation complex. Junction of the 60S ribosomal subunit to
CC       form the 80S initiation complex is preceded by hydrolysis of the GTP
CC       bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for
CC       eIF-2 to recycle and catalyze another round of initiation, the GDP
CC       bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by
CC       eIF-2B. {ECO:0000305}.
CC   -!- SUBUNIT: Eukaryotic translation initiation factor 2 (eIF-2) is a
CC       heterotrimer composed of an alpha, a beta and a gamma subunit. The
CC       factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a
CC       multifactor complex (MFC) that may bind to the 40S ribosome.
CC       {ECO:0000305}.
CC   -!- INTERACTION:
CC       P20459; P32481: GCD11; NbExp=11; IntAct=EBI-8915, EBI-8924;
CC       P20459; P38431: TIF5; NbExp=4; IntAct=EBI-8915, EBI-9038;
CC   -!- PTM: Phosphorylated; phosphorylation on Ser-52 by the GCN2 protein
CC       kinase occurs in response to low amino acid, carbon, or purine
CC       availability. {ECO:0000269|PubMed:10733573, ECO:0000269|PubMed:1739968,
CC       ECO:0000269|PubMed:8336737}.
CC   -!- MISCELLANEOUS: Present with 17100 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}.
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DR   EMBL; M25552; AAA70332.1; -; Genomic_DNA.
DR   EMBL; X87611; CAA60929.1; -; Genomic_DNA.
DR   EMBL; Z49507; CAA89529.1; -; Genomic_DNA.
DR   EMBL; AY557876; AAS56202.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08798.1; -; Genomic_DNA.
DR   PIR; A32108; A32108.
DR   RefSeq; NP_012540.3; NM_001181664.3.
DR   PDB; 1Q46; X-ray; 2.86 A; A=2-176.
DR   PDB; 2A19; X-ray; 2.50 A; A=4-176.
DR   PDB; 2A1A; X-ray; 2.80 A; A=4-176.
DR   PDB; 3J81; EM; 4.00 A; j=1-300.
DR   PDB; 3JAP; EM; 4.90 A; j=1-304.
DR   PDB; 3JAQ; EM; 6.00 A; j=1-304.
DR   PDB; 6FYX; EM; 3.05 A; j=1-304.
DR   PDB; 6FYY; EM; 3.05 A; j=1-304.
DR   PDB; 6GSM; EM; 5.15 A; j=3-265.
DR   PDB; 6GSN; EM; 5.75 A; j=3-265.
DR   PDB; 6I3M; EM; 3.93 A; K/L=1-304.
DR   PDB; 6I7T; EM; 4.61 A; K/L=1-304.
DR   PDB; 6JLY; X-ray; 3.50 A; L/M=1-304.
DR   PDB; 6JLZ; X-ray; 3.35 A; L/M=1-304.
DR   PDB; 6QG0; EM; 4.20 A; K/L=1-304.
DR   PDB; 6QG1; EM; 4.20 A; K/L=1-304.
DR   PDB; 6QG2; EM; 4.60 A; K/L=1-304.
DR   PDB; 6QG3; EM; 9.40 A; K/L=1-304.
DR   PDB; 6QG5; EM; 10.10 A; K/L=1-304.
DR   PDB; 6QG6; EM; 4.65 A; K/L=1-304.
DR   PDBsum; 1Q46; -.
DR   PDBsum; 2A19; -.
DR   PDBsum; 2A1A; -.
DR   PDBsum; 3J81; -.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   PDBsum; 6FYX; -.
DR   PDBsum; 6FYY; -.
DR   PDBsum; 6GSM; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6I3M; -.
DR   PDBsum; 6I7T; -.
DR   PDBsum; 6JLY; -.
DR   PDBsum; 6JLZ; -.
DR   PDBsum; 6QG0; -.
DR   PDBsum; 6QG1; -.
DR   PDBsum; 6QG2; -.
DR   PDBsum; 6QG3; -.
DR   PDBsum; 6QG5; -.
DR   PDBsum; 6QG6; -.
DR   SMR; P20459; -.
DR   BioGRID; 33763; 296.
DR   ComplexPortal; CPX-427; Eukaryotic translation initiation factor 2 complex.
DR   DIP; DIP-2327N; -.
DR   IntAct; P20459; 35.
DR   MINT; P20459; -.
DR   STRING; 4932.YJR007W; -.
DR   iPTMnet; P20459; -.
DR   MaxQB; P20459; -.
DR   PaxDb; P20459; -.
DR   PRIDE; P20459; -.
DR   EnsemblFungi; YJR007W_mRNA; YJR007W; YJR007W.
DR   GeneID; 853463; -.
DR   KEGG; sce:YJR007W; -.
DR   SGD; S000003767; SUI2.
DR   VEuPathDB; FungiDB:YJR007W; -.
DR   eggNOG; KOG2916; Eukaryota.
DR   GeneTree; ENSGT00390000007015; -.
DR   HOGENOM; CLU_033458_0_1_1; -.
DR   InParanoid; P20459; -.
DR   OMA; DVNEHQR; -.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-381042; PERK regulates gene expression.
DR   Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR   Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-SCE-72731; Recycling of eIF2:GDP.
DR   EvolutionaryTrace; P20459; -.
DR   PRO; PR:P20459; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P20459; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR   GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IMP:SGD.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IBA:GO_Central.
DR   GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR   GO; GO:0001731; P:formation of translation preinitiation complex; IDA:SGD.
DR   CDD; cd04452; S1_IF2_alpha; 1.
DR   Gene3D; 1.10.150.190; -; 1.
DR   Gene3D; 3.30.70.1130; -; 1.
DR   IDEAL; IID50184; -.
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   1: Evidence at protein level;
KW   3D-structure; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..304
FT                   /note="Eukaryotic translation initiation factor 2 subunit
FT                   alpha"
FT                   /id="PRO_0000137389"
FT   DOMAIN          17..88
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT   MOD_RES         52
FT                   /note="Phosphoserine; by GCN2"
FT                   /evidence="ECO:0000269|PubMed:10733573,
FT                   ECO:0000269|PubMed:1739968, ECO:0000269|PubMed:8336737"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         294
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         52
FT                   /note="S->A: Inhibits derepression of GCN4 expression in
FT                   amino acid, purine, and glucose-starved cells."
FT                   /evidence="ECO:0000269|PubMed:10733573,
FT                   ECO:0000269|PubMed:1739968"
FT   MUTAGEN         52
FT                   /note="S->D: Weakly impairs derepression of GCN4 expression
FT                   in amino acid-starved cells."
FT                   /evidence="ECO:0000269|PubMed:1739968"
FT   CONFLICT        258
FT                   /note="Y -> H (in Ref. 4; AAS56202)"
FT                   /evidence="ECO:0000305"
FT   STRAND          8..13
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   STRAND          19..28
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   STRAND          31..36
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   TURN            37..41
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   STRAND          43..47
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   HELIX           48..50
FT                   /evidence="ECO:0007744|PDB:1Q46"
FT   STRAND          56..58
FT                   /evidence="ECO:0007744|PDB:6JLZ"
FT   HELIX           59..61
FT                   /evidence="ECO:0007744|PDB:1Q46"
FT   STRAND          67..77
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   TURN            78..81
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   STRAND          82..87
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   HELIX           92..118
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   HELIX           123..129
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   HELIX           131..138
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   HELIX           141..150
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   HELIX           152..155
FT                   /evidence="ECO:0007744|PDB:2A19"
FT   HELIX           163..173
FT                   /evidence="ECO:0007744|PDB:2A19"
SQ   SEQUENCE   304 AA;  34718 MW;  AF4F1C80303A4E98 CRC64;
     MSTSHCRFYE NKYPEIDDIV MVNVQQIAEM GAYVKLLEYD NIEGMILLSE LSRRRIRSIQ
     KLIRVGKNDV AVVLRVDKEK GYIDLSKRRV SSEDIIKCEE KYQKSKTVHS ILRYCAEKFQ
     IPLEELYKTI AWPLSRKFGH AYEAFKLSII DETVWEGIEP PSKDVLDELK NYISKRLTPQ
     AVKIRADVEV SCFSYEGIDA IKDALKSAED MSTEQMQVKV KLVAAPLYVL TTQALDKQKG
     IEQLESAIEK ITEVITKYGG VCNITMPPKA VTATEDAELQ ALLESKELDN RSDSEDDEDE
     SDDE
//
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