EIF2A_YEAST
ID EIF2A_YEAST Reviewed; 642 AA.
AC P53235; D6VUI9; Q45U32;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Eukaryotic translation initiation factor 2A;
DE Short=eIF-2A;
GN OrderedLocusNames=YGR054W;
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], AND VARIANTS ALA-145; LYS-165 AND
RP SER-569.
RC STRAIN=SK1;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 FUNCTION.
RX PubMed=12133843; DOI=10.1074/jbc.m207109200;
RA Zoll W.L., Horton L.E., Komar A.A., Hensold J.O., Merrick W.C.;
RT "Characterization of mammalian eIF2A and identification of the yeast
RT homolog.";
RL J. Biol. Chem. 277:37079-37087(2002).
RN [5]
RP FUNCTION.
RX PubMed=15718232; DOI=10.1074/jbc.m413728200;
RA Komar A.A., Gross S.R., Barth-Baus D., Strachan R., Hensold J.O.,
RA Goss Kinzy T., Merrick W.C.;
RT "Novel characteristics of the biological properties of the yeast
RT Saccharomyces cerevisiae eukaryotic initiation factor 2A.";
RL J. Biol. Chem. 280:15601-15611(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564; SER-567 AND SER-572, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Functions in the early steps of protein synthesis of a small
CC number of specific mRNAs. Acts by directing the binding of methionyl-
CC tRNAi to 40S ribosomal subunits. In contrast to the eIF-2 complex, it
CC binds methionyl-tRNAi to 40S subunits in a codon-dependent manner,
CC whereas the eIF-2 complex binds methionyl-tRNAi to 40S subunits in a
CC GTP-dependent manner. Specifically associates with both 40S subunits
CC and 80S ribosomes. {ECO:0000269|PubMed:12133843,
CC ECO:0000269|PubMed:15718232}.
CC -!- PTM: Ubiquitinated, probably leading to its degradation. May explain
CC why it has a short half-life of 17 minutes.
CC {ECO:0000269|PubMed:15718232}.
CC -!- SIMILARITY: Belongs to the WD repeat EIF2A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ115391; AAZ22467.1; -; Genomic_DNA.
DR EMBL; Z72839; CAA97054.1; -; Genomic_DNA.
DR EMBL; Z72840; CAA97056.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08150.1; -; Genomic_DNA.
DR PIR; S64348; S64348.
DR RefSeq; NP_011568.3; NM_001181183.4.
DR AlphaFoldDB; P53235; -.
DR SMR; P53235; -.
DR BioGRID; 33299; 150.
DR DIP; DIP-5518N; -.
DR IntAct; P53235; 21.
DR MINT; P53235; -.
DR STRING; 4932.YGR054W; -.
DR iPTMnet; P53235; -.
DR MaxQB; P53235; -.
DR PaxDb; P53235; -.
DR PRIDE; P53235; -.
DR EnsemblFungi; YGR054W_mRNA; YGR054W; YGR054W.
DR GeneID; 852945; -.
DR KEGG; sce:YGR054W; -.
DR SGD; S000003286; YGR054W.
DR VEuPathDB; FungiDB:YGR054W; -.
DR eggNOG; KOG2315; Eukaryota.
DR GeneTree; ENSGT00730000111053; -.
DR HOGENOM; CLU_013809_0_1_1; -.
DR InParanoid; P53235; -.
DR OMA; LITWQRP; -.
DR BioCyc; YEAST:G3O-30771-MON; -.
DR PRO; PR:P53235; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53235; protein.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:SGD.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR011387; TIF2A.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13227; PTHR13227; 1.
DR Pfam; PF08662; eIF2A; 1.
DR PIRSF; PIRSF017222; eIF2A; 1.
PE 1: Evidence at protein level;
KW Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Repeat; Translation regulation; Ubl conjugation;
KW WD repeat.
FT CHAIN 1..642
FT /note="Eukaryotic translation initiation factor 2A"
FT /id="PRO_0000202800"
FT REPEAT 69..115
FT /note="WD 1"
FT REPEAT 186..224
FT /note="WD 2"
FT REPEAT 289..331
FT /note="WD 3"
FT REPEAT 374..419
FT /note="WD 4"
FT REGION 485..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 145
FT /note="G -> A (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 165
FT /note="N -> K (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
FT VARIANT 569
FT /note="P -> S (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:16273108"
SQ SEQUENCE 642 AA; 71305 MW; F3C2E78504D83418 CRC64;
MSSQFFLKTS QDIELFQSYP TFEQSNTNSK DFPVISSVLS PCGRFLALST KENVKVFTGP
CLDNVLLTMK LSDVYDLHFS PAGNYLSTWE RASIQDPNHK NVKVWYLNKP FKKDCVSEDI
VPAYEYQAKS QSGWFLQFSK LDNYGLRLFK HDLKIVKLSS ANADNFDFQS PFAVLSDDET
SQHFTTYLIS PAEHPTICTF TPEKGGKPAQ LIIWALSEGK ITKKIASKTF FKADSCQLKW
NPLGNAILCL AITDFDSSNK SYYGENTLYL LSFQGVNGTL GGNSVRVSLT TGPVHDFTWS
PTSRQFGVIA GYMPATISFF DLRGNVVHSL PQQAKNTMLF SPSGHYILIA GFGNLQGSVE
ILDRLDKFKC VSKFDATNTS VCKWSPGGEF IMTATTSPRL RVDNGVKIWH VSGSLVFVKE
FKELLKVDWR SPCNYKTLEN KDEAFFENHI INNWEPLPDS TTSSLDPKIS NKSELQIHSS
VQEYISQHPS REASSNGNGS KAKAGGAYKP PHARRTGGGR IVPGVPPGAA KKTIPGLVPG
MSANKDANTK NRRRRANKKS SETSPDSTPA PSAPASTNAP TNNKETSPEE KKIRSLLKKL
RAIETLKERQ AVGDKLEDTQ VLKIQTEEKV LKDLEKLGWK DE
