EI2BA_YEAST
ID EI2BA_YEAST Reviewed; 305 AA.
AC P14741; D6VX91;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Translation initiation factor eIF-2B subunit alpha;
DE AltName: Full=GCD complex subunit GCN3;
DE AltName: Full=Guanine nucleotide exchange factor subunit GCN3 {ECO:0000303|PubMed:8506384};
DE AltName: Full=Translational activator GCN3 {ECO:0000303|PubMed:3062370};
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit alpha;
GN Name=GCN3 {ECO:0000312|SGD:S000001734};
GN Synonyms=AAS2 {ECO:0000312|SGD:S000001734}, TIF221;
GN OrderedLocusNames=YKR026C;
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=3062370; DOI=10.1128/mcb.8.11.4808-4820.1988;
RA Hannig E.M., Hinnebusch A.G.;
RT "Molecular analysis of GCN3, a translational activator of GCN4: evidence
RT for posttranslational control of GCN3 regulatory function.";
RL Mol. Cell. Biol. 8:4808-4820(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 IDENTIFICATION IN THE EIF2-B COMPLEX, AND FUNCTION OF THE EIF2-B COMPLEX.
RX PubMed=8506384; DOI=10.1073/pnas.90.11.5350;
RA Cigan A.M., Bushman J.L., Boal T.R., Hinnebusch A.G.;
RT "A protein complex of translational regulators of GCN4 mRNA is the guanine
RT nucleotide-exchange factor for translation initiation factor 2 in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5350-5354(1993).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN A EIF2-B SUBCOMPLEX.
RX PubMed=9472020; DOI=10.1101/gad.12.4.514;
RA Pavitt G.D., Ramaiah K.V., Kimball S.R., Hinnebusch A.G.;
RT "eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and
RT regulate guanine-nucleotide exchange.";
RL Genes Dev. 12:514-526(1998).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-291, AND IDENTIFICATION BY
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a non-essential regulatory component of the
CC translation initiation factor 2B (eIF2-B or GCD complex), which
CC catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound
CC GDP for GTP and is regulated by phosphorylated eIF-2 (PubMed:8506384,
CC PubMed:9472020). It activates the translation of GCN4 in response to
CC low amino acid, carbon, or purine availability, by suppressing the
CC inhibitory effects of multiple uORFs present in the leader of GCN4 mRNA
CC (PubMed:10733573). It may promote either repression or activation of
CC GCN4 expression depending on amino acid availability (PubMed:8506384).
CC Modulation of GCN3 regulatory function in response to amino acid
CC availability occurs post-translationally (PubMed:8506384,
CC PubMed:9472020). {ECO:0000269|PubMed:10733573,
CC ECO:0000269|PubMed:8506384, ECO:0000269|PubMed:9472020}.
CC -!- SUBUNIT: Translation initiation factor 2B (eIF2-B) is composed of five
CC different subunits; alpha (GCN3), beta (GCD7), gamma (GCD1), delta
CC (GCD2) and epsilon (GCD6). A regulatory subcomplex comprising GCN3,
CC GCD7 and GCD2 interacts preferentially with phosphorylated eIF-2 and
CC has no exchange activity in vitro. {ECO:0000269|PubMed:8506384,
CC ECO:0000269|PubMed:9472020}.
CC -!- INTERACTION:
CC P14741; P12754: GCD2; NbExp=7; IntAct=EBI-6253, EBI-6265;
CC P14741; P32502: GCD7; NbExp=10; IntAct=EBI-6253, EBI-6260;
CC -!- DISRUPTION PHENOTYPE: Inhibits GCN4 derepression in glucose, amino
CC acid, or purine-starved cells. {ECO:0000269|PubMed:10733573}.
CC -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
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DR EMBL; M23356; AAA34637.1; -; Genomic_DNA.
DR EMBL; Z28251; CAA82098.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09181.1; -; Genomic_DNA.
DR PIR; A31562; A31562.
DR RefSeq; NP_012951.1; NM_001179816.1.
DR PDB; 6I3M; EM; 3.93 A; A/B=1-305.
DR PDB; 6I7T; EM; 4.61 A; A/B=1-305.
DR PDB; 6QG0; EM; 4.20 A; A/B=1-305.
DR PDB; 6QG1; EM; 4.20 A; A/B=1-305.
DR PDB; 6QG2; EM; 4.60 A; A/B=1-305.
DR PDB; 6QG3; EM; 9.40 A; A/B=1-305.
DR PDB; 6QG5; EM; 10.10 A; A/B=1-305.
DR PDB; 6QG6; EM; 4.65 A; A/B=1-305.
DR PDBsum; 6I3M; -.
DR PDBsum; 6I7T; -.
DR PDBsum; 6QG0; -.
DR PDBsum; 6QG1; -.
DR PDBsum; 6QG2; -.
DR PDBsum; 6QG3; -.
DR PDBsum; 6QG5; -.
DR PDBsum; 6QG6; -.
DR AlphaFoldDB; P14741; -.
DR SMR; P14741; -.
DR BioGRID; 34158; 180.
DR ComplexPortal; CPX-429; Eukaryotic translation initiation factor 2B complex.
DR DIP; DIP-1328N; -.
DR IntAct; P14741; 82.
DR MINT; P14741; -.
DR STRING; 4932.YKR026C; -.
DR iPTMnet; P14741; -.
DR MaxQB; P14741; -.
DR PaxDb; P14741; -.
DR PRIDE; P14741; -.
DR EnsemblFungi; YKR026C_mRNA; YKR026C; YKR026C.
DR GeneID; 853896; -.
DR KEGG; sce:YKR026C; -.
DR SGD; S000001734; GCN3.
DR VEuPathDB; FungiDB:YKR026C; -.
DR eggNOG; KOG1466; Eukaryota.
DR GeneTree; ENSGT00550000074853; -.
DR HOGENOM; CLU_016218_0_2_1; -.
DR InParanoid; P14741; -.
DR OMA; LYPLGQY; -.
DR BioCyc; YEAST:G3O-32002-MON; -.
DR Reactome; R-SCE-72731; Recycling of eIF2:GDP.
DR PRO; PR:P14741; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P14741; protein.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:SGD.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:SGD.
DR GO; GO:0030234; F:enzyme regulator activity; IMP:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:1903833; P:positive regulation of cellular response to amino acid starvation; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:ComplexPortal.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:SGD.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR Gene3D; 1.20.120.1070; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
DR InterPro; IPR042528; elF-2B_alpha_N.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repressor;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..305
FT /note="Translation initiation factor eIF-2B subunit alpha"
FT /id="PRO_0000156060"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 305 AA; 34025 MW; 8E9A928D6D56E12B CRC64;
MSEFNITETY LRFLEEDTEM TMPIAAIEAL VTLLRIKTPE TAAEMINTIK SSTEELIKSI
PNSVSLRAGC DIFMRFVLRN LHLYGDWENC KQHLIENGQL FVSRAKKSRN KIAEIGVDFI
ADDDIILVHG YSRAVFSLLN HAANKFIRFR CVVTESRPSK QGNQLYTLLE QKGIPVTLIV
DSAVGAVIDK VDKVFVGAEG VAESGGIINL VGTYSVGVLA HNARKPFYVV TESHKFVRMF
PLSSDDLPMA GPPLDFTRRT DDLEDALRGP TIDYTAQEYI TALITDLGVL TPSAVSEELI
KMWYD
