ID   EI2BB_YEAST             Reviewed;         381 AA.
AC   P32502; D6VYT7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   04-NOV-2026, entry version 192.
DE   RecName: Full=Translation initiation factor eIF2B subunit beta;
DE   AltName: Full=GCD complex subunit GCD7;
DE   AltName: Full=Guanine nucleotide exchange factor subunit GCD7;
DE   AltName: Full=eIF2B GDP-GTP exchange factor subunit beta;
GN   Name=GCD7; Synonyms=TIF222; OrderedLocusNames=YLR291C;
GN   ORFNames=L8003.17;
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=8441423; DOI=10.1128/mcb.13.3.1920-1932.1993;
RA   Bushman J.L., Asuru A.I., Matts R.L., Hinnebusch A.G.;
RT   "Evidence that GCD6 and GCD7, translational regulators of GCN4, are
RT   subunits of the guanine nucleotide exchange factor for eIF-2 in
RT   Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 13:1920-1932(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871; DOI=10.1038/387s087;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   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   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   [7]
RP   INTERACTION WITH GCD11.
RX   PubMed=35031321; DOI=10.1016/j.jbc.2022.101583;
RA   Vanselow S., Neumann-Arnold L., Wojciech-Moock F., Seufert W.;
RT   "Stepwise assembly of the eukaryotic translation initiation factor 2
RT   complex.";
RL   J. Biol. Chem. 298:101583-101583(2022).
CC   -!- FUNCTION: Acts as a component of the translation initiation factor 2B
CC       (eIF2B) complex, which catalyzes the exchange of GDP for GTP on the
CC       eukaryotic initiation factor 2 (eIF2) complex gamma subunit. Its
CC       guanine nucleotide exchange factor activity is repressed when bound to
CC       eIF2 complex phosphorylated on the alpha subunit, thereby limiting the
CC       amount of methionyl-initiator methionine tRNA available to the ribosome
CC       and consequently global translation is repressed (By similarity). It
CC       activates the synthesis of GCN4 in yeast under amino acid starvation
CC       conditions by suppressing the inhibitory effects of multiple AUG codons
CC       present in the leader of GCN4 mRNA. It may promote either repression or
CC       activation of GCN4 expression depending on amino acid availability.
CC       GCD6 and GCD7 repress GCN4 expression at the translational level by
CC       ensuring that ribosomes which have translated UORF1 will reinitiate at
CC       UORF2, -3, or -4 and thus fail to reach the GCN4 start site.
CC       {ECO:0000250|UniProtKB:Q9UT76, ECO:0000269|PubMed:8506384,
CC       ECO:0000269|PubMed:9472020}.
CC   -!- SUBUNIT: Component of the translation initiation factor 2B (eIF2B)
CC       complex which is a heterodecamer of two sets of five different
CC       subunits: alpha, beta, gamma, delta and epsilon. Subunits alpha, beta
CC       and delta comprise a regulatory subcomplex and subunits epsilon and
CC       gamma comprise a catalytic subcomplex (PubMed:35031321, PubMed:8506384,
CC       PubMed:9472020). Within the complex, the hexameric regulatory complex
CC       resides at the center, with the two heterodimeric catalytic
CC       subcomplexes bound on opposite sides (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UT76, ECO:0000269|PubMed:35031321,
CC       ECO:0000269|PubMed:8506384, ECO:0000269|PubMed:9472020}.
CC   -!- INTERACTION:
CC       P32502; P12754: GCD2; NbExp=11; IntAct=EBI-6260, EBI-6265;
CC       P32502; P14741: GCN3; NbExp=11; IntAct=EBI-6260, EBI-6253;
CC       P32502; Q02866: MUK1; NbExp=3; IntAct=EBI-6260, EBI-32646;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9UT76}.
CC   -!- MISCELLANEOUS: Present with 6650 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; L07116; AAA34634.1; -; Genomic_DNA.
DR   EMBL; U17243; AAB67337.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09603.1; -; Genomic_DNA.
DR   PIR; B48156; B48156.
DR   RefSeq; NP_013394.1; NM_001182179.1.
DR   PDB; 6I3M; EM; 3.93 A; E/F=1-381.
DR   PDB; 6I7T; EM; 4.61 A; E/F=1-381.
DR   PDB; 6QG0; EM; 4.20 A; C/D=1-381.
DR   PDB; 6QG1; EM; 4.20 A; C/D=1-381.
DR   PDB; 6QG2; EM; 4.60 A; C/D=1-381.
DR   PDB; 6QG3; EM; 9.40 A; C/D=1-381.
DR   PDB; 6QG5; EM; 10.10 A; C/D=1-381.
DR   PDB; 6QG6; EM; 4.65 A; C/D=1-381.
DR   SMR; P32502; -.
DR   BioGRID; 31557; 429.
DR   ComplexPortal; CPX-429; Eukaryotic translation initiation factor 2B complex.
DR   DIP; DIP-1185N; -.
DR   IntAct; P32502; 161.
DR   STRING; 4932.YLR291C; -.
DR   iPTMnet; P32502; -.
DR   PaxDb; 4932-YLR291C; -.
DR   PeptideAtlas; P32502; -.
DR   EnsemblFungi; YLR291C_mRNA; YLR291C; YLR291C.
DR   GeneID; 850998; -.
DR   KEGG; sce:YLR291C; -.
DR   VEuPathDB; FungiDB:YLR291C; -.
DR   AGR; SGD:S000004282; -.
DR   SGD; S000004282; GCD7.
DR   eggNOG; KOG1465; Eukaryota.
DR   HOGENOM; CLU_016218_4_3_1; -.
DR   InParanoid; P32502; -.
DR   OMA; AAEYHSV; -.
DR   OrthoDB; 269919at2759; -.
DR   BioCyc; YEAST:G3O-32386-MONOMER; -.
DR   Reactome; R-SCE-72731; Recycling of eIF2:GDP.
DR   PRO; PR:P32502; -.
DR   FunFam; 1.20.120.420:FF:000009; Gcd7p; 1.
DR   FunFam; 3.40.50.10470:FF:000009; Translation initiation factor eIF2B subunit; 1.
DR   Gene3D; 1.20.120.420; translation initiation factor eif-2b, domain 1; 1.
DR   Gene3D; 3.40.50.10470; Translation initiation factor eif-2b, domain 2; 1.
DR   InterPro; IPR051855; eIF2B_beta_subunit.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR027363; M1Pi_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   PANTHER; PTHR45859; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR   PANTHER; PTHR45859:SF1; TRANSLATION INITIATION FACTOR EIF-2B SUBUNIT BETA; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
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:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0030234; F:enzyme regulator activity; IMP:SGD.
DR   GO; GO:0003743; F:translation initiation factor activity; IGI:SGD.
DR   GO; GO:0002183; P:cytoplasmic translational initiation; ISS:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; IDA:SGD.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P32502; protein.
DR   BioGRID-ORCS; 850998; 0 hits in 10 CRISPR screens.
DR   AlphaFoldDB; P32502; -.
DR   EMDB; EMD-4404; -.
DR   EMDB; EMD-4428; -.
DR   EMDB; EMD-4543; -.
DR   EMDB; EMD-4544; -.
DR   EMDB; EMD-4545; -.
DR   EMDB; EMD-4546; -.
DR   EMDB; EMD-4547; -.
DR   EMDB; EMD-4548; -.
DR   FunCoup; P32502; 1260.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Initiation factor; Protein biosynthesis;
KW   Reference proteome; Translation regulation.
FT   CHAIN           1..381
FT                   /note="Translation initiation factor eIF2B subunit beta"
FT                   /id="PRO_0000156066"
FT   REGION          125..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   381 AA;  42570 MW;  A5409FAF1594854C CRC64;
     MSSQAFTSVH PNAATSDVNV TIDTFVAKLK RRQVQGSYAI ALETLQLLMR FISAARWNHV
     NDLIEQIRDL GNSLEKAHPT AFSCGNVIRR ILAVLRDEVE EDTMSTTVTS TSVAEPLISS
     MFNLLQKPEQ PHQNRKNSSG SSSMKTKTDY RQVAIQGIKD LIDEIKNIDE GIQQIAIDLI
     HDHEILLTPT PDSKTVLKFL ITARERSNRT FTVLVTEGFP NNTKNAHEFA KKLAQHNIET
     LVVPDSAVFA LMSRVGKVII GTKAVFVNGG TISSNSGVSS VCECAREFRT PVFAVAGLYK
     LSPLYPFDVE KFVEFGGSQR ILPRMDPRKR LDTVNQITDY VPPENIDIYI TNVGGFNPSF
     IYRIAWDNYK QIDVHLDKNK A
//