EI2BB_YEAST
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 03-AUG-2022, entry version 174.
DE RecName: Full=Translation initiation factor eIF-2B subunit beta;
DE AltName: Full=GCD complex subunit GCD7;
DE AltName: Full=Guanine nucleotide exchange factor subunit GCD7;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit beta;
GN Name=GCD7; Synonyms=TIF222; OrderedLocusNames=YLR291C; 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;
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).
CC -!- FUNCTION: Acts as a regulatory component of the translation initiation
CC factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of
CC eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is
CC regulated by phosphorylated eIF-2. It activates the synthesis of GCN4
CC in yeast under amino acid starvation conditions by suppressing the
CC inhibitory effects of multiple AUG codons present in the leader of GCN4
CC mRNA. It may promote either repression or activation of GCN4 expression
CC depending on amino acid availability. GCD6 and GCD7 repress GCN4
CC expression at the translational level by ensuring that ribosomes which
CC have translated UORF1 will reinitiate at UORF2, -3, or -4 and thus fail
CC to reach the GCN4 start site. {ECO:0000269|PubMed:8506384,
CC 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 P32502; P12754: GCD2; NbExp=10; IntAct=EBI-6260, EBI-6265;
CC P32502; P14741: GCN3; NbExp=10; IntAct=EBI-6260, EBI-6253;
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 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; P32502; -.
DR SMR; P32502; -.
DR BioGRID; 31557; 418.
DR ComplexPortal; CPX-429; Eukaryotic translation initiation factor 2B complex.
DR DIP; DIP-1185N; -.
DR IntAct; P32502; 156.
DR MINT; P32502; -.
DR STRING; 4932.YLR291C; -.
DR iPTMnet; P32502; -.
DR MaxQB; P32502; -.
DR PaxDb; P32502; -.
DR PRIDE; P32502; -.
DR EnsemblFungi; YLR291C_mRNA; YLR291C; YLR291C.
DR GeneID; 850998; -.
DR KEGG; sce:YLR291C; -.
DR SGD; S000004282; GCD7.
DR VEuPathDB; FungiDB:YLR291C; -.
DR eggNOG; KOG1465; Eukaryota.
DR GeneTree; ENSGT00550000074908; -.
DR HOGENOM; CLU_016218_4_3_1; -.
DR InParanoid; P32502; -.
DR OMA; TSHTSYA; -.
DR BioCyc; YEAST:G3O-32386-MON; -.
DR Reactome; R-SCE-72731; Recycling of eIF2:GDP.
DR ChiTaRS; GCD7; yeast.
DR PRO; PR:P32502; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32502; 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: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: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; 1.20.120.420; -; 1.
DR Gene3D; 3.40.50.10470; -; 1.
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 Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis; Reference proteome;
KW Translation regulation.
FT CHAIN 1..381
FT /note="Translation initiation factor eIF-2B subunit beta"
FT /id="PRO_0000156066"
FT REGION 125..148
FT /note="Disordered"
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
