EI2BG_YEAST
ID EI2BG_YEAST Reviewed; 578 AA.
AC P09032; D6W2W1; Q08721;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Translation initiation factor eIF-2B subunit gamma;
DE AltName: Full=GCD complex subunit GCD1;
DE AltName: Full=Guanine nucleotide exchange factor subunit GCD1;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit gamma;
GN Name=GCD1; Synonyms=TIF223, TRA3; OrderedLocusNames=YOR260W;
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=3050897; DOI=10.1093/nar/16.19.9253;
RA Hill D.E., Struhl K.;
RT "Molecular characterization of GCD1, a yeast gene required for general
RT control of amino acid biosynthesis and cell-cycle initiation.";
RL Nucleic Acids Res. 16:9253-9265(1988).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Cigan A.M., Pavitt G.;
RL Submitted (NOV-1994) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153759;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<483::aid-yea105>3.0.co;2-u;
RA Poirey R., Jauniaux J.-C.;
RT "Sequencing analysis of a 36.8 kb fragment of yeast chromosome XV reveals
RT 26 open reading frames including SEC63, CDC31, SUG2, GCD1, RBL2, PNT1, PAC1
RT and VPH1.";
RL Yeast 13:483-487(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
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 [6]
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 [7]
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 [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-296 AND SER-300, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306, AND IDENTIFICATION BY
RP 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: Acts as essential 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. GCD1 stabilizes the interaction
CC between eIF-2 and GCD6 and stimulates the catalytic activity in vitro.
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 catalytic subcomplex comprising GCD1 and
CC GCD6 interacts with both, phosphorylated and non-phosphorylated eIF-2
CC and has exchange activity in vitro. {ECO:0000269|PubMed:8506384,
CC ECO:0000269|PubMed:9472020}.
CC -!- INTERACTION:
CC P09032; P32501: GCD6; NbExp=8; IntAct=EBI-6275, EBI-6270;
CC -!- MISCELLANEOUS: Present with 9530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30693.1; Type=Frameshift; Evidence={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; X07846; CAA30693.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z75168; CAA99482.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11027.1; -; Genomic_DNA.
DR PIR; S67157; BVBYD1.
DR RefSeq; NP_014903.1; NM_001183679.1.
DR PDB; 6I3M; EM; 3.93 A; I/J=1-578.
DR PDB; 6I7T; EM; 4.61 A; I/J=1-578.
DR PDB; 6QG0; EM; 4.20 A; E/F=1-578.
DR PDB; 6QG1; EM; 4.20 A; E/F=1-578.
DR PDB; 6QG2; EM; 4.60 A; E/F=1-578.
DR PDB; 6QG3; EM; 9.40 A; E/F=1-578.
DR PDB; 6QG5; EM; 10.10 A; E/F=1-578.
DR PDB; 6QG6; EM; 4.65 A; E/F=1-578.
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; P09032; -.
DR SMR; P09032; -.
DR BioGRID; 34650; 399.
DR ComplexPortal; CPX-429; Eukaryotic translation initiation factor 2B complex.
DR DIP; DIP-1327N; -.
DR IntAct; P09032; 18.
DR MINT; P09032; -.
DR STRING; 4932.YOR260W; -.
DR iPTMnet; P09032; -.
DR MaxQB; P09032; -.
DR PaxDb; P09032; -.
DR PRIDE; P09032; -.
DR EnsemblFungi; YOR260W_mRNA; YOR260W; YOR260W.
DR GeneID; 854434; -.
DR KEGG; sce:YOR260W; -.
DR SGD; S000005786; GCD1.
DR VEuPathDB; FungiDB:YOR260W; -.
DR eggNOG; KOG1462; Eukaryota.
DR GeneTree; ENSGT00510000047486; -.
DR HOGENOM; CLU_016743_3_0_1; -.
DR InParanoid; P09032; -.
DR OMA; QAFIFCG; -.
DR BioCyc; YEAST:G3O-33751-MON; -.
DR Reactome; R-SCE-72731; Recycling of eIF2:GDP.
DR PRO; PR:P09032; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P09032; 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:0003743; F:translation initiation factor activity; IMP:SGD.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:1903574; P:negative 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 Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Translation regulation.
FT CHAIN 1..578
FT /note="Translation initiation factor eIF-2B subunit gamma"
FT /id="PRO_0000156083"
FT REGION 298..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 217..240
FT /note="QKQQQFFTVYSENEDSERQPILLD -> AKNNSNFSLFIQKTKTQRGSQYFW
FT N (in Ref. 1; CAA30693)"
FT /evidence="ECO:0000305"
FT CONFLICT 491..492
FT /note="IG -> SV (in Ref. 1; CAA30693)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 65700 MW; EC25BAE00F4D1E94 CRC64;
MSIQAFVFCG KGSNLAPFTQ PDFPFQTQNK DSTAATSGDK LNELVNSALD STVINEFMQH
STRLPKALLP IGNRPMIEYV LDWCDQADFK EISVVAPVDE IELIESGLTS FLSLRKQQFE
LIYKALSNSN HSHHLQDPKK INFIPSKANS TGESLQKELL PRINGDFVIL PCDFVTDIPP
QVLVDQFRNR DDNNLAMTIY YKNSLDSSID KKQQQKQKQQ QFFTVYSENE DSERQPILLD
VYSQRDVTKT KYLQIRSHLL WNYPNLTVST KLLNSFIYFC SFELCQLLKL GPQSMSRQAS
FKDPFTGNQQ QQNPPTTDDD EDRNHDDDDD YKPSATSIQP TYFKKKNDLI LDPINCNKSL
SKVFRDLSRR SWQHSKPREP IGIFILPNET LFIRANNLNA YMDANRFVLK IKSQTMFTKN
IQIQSAAIGA DAIVDPKCQI SAHSNVKMSV LGTQANIGSR CRVAGSLLFP GVHLGDEVIL
ENCIIGPMAK IGSKCKLSNC YIEGHYVVEP KNNFKGETLA NVYLDEDEED ELIYDDSVIA
GESEIAEETD SDDRSDEDSD DSEYTDEYEY EDDGLFER
