ID EF1G1_YEAST Reviewed; 415 AA.
AC P29547; D6W3W6; Q9URC6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 27-MAR-2024, entry version 209.
DE RecName: Full=Elongation factor 1-gamma 1;
DE Short=EF-1-gamma 1;
DE AltName: Full=Calcium and membrane-binding protein 1;
DE AltName: Full=Calcium phospholipid-binding protein;
DE Short=CPBP;
DE AltName: Full=Eukaryotic elongation factor 1Bgamma 1;
DE Short=eEF1Bgamma 1;
DE AltName: Full=Translation elongation factor 1B gamma 1;
GN Name=CAM1; Synonyms=TEF3; OrderedLocusNames=YPL048W;
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=8247005; DOI=10.1128/mcb.13.12.7901-7912.1993;
RA Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr.;
RT "DRS1 to DRS7, novel genes required for ribosome assembly and function in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:7901-7912(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8465602; DOI=10.1002/yea.320090206;
RA Kambouris N.G., Burke D.J., Creutz C.E.;
RT "Cloning and genetic characterization of a calcium- and phospholipid-
RT binding protein from Saccharomyces cerevisiae that is homologous to
RT translation elongation factor-1 gamma.";
RL Yeast 9:151-163(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 357-373.
RX PubMed=1882548; DOI=10.1002/yea.320070305;
RA Creutz C.E., Snyder S.L., Kambouris N.G.;
RT "Calcium-dependent secretory vesicle-binding and lipid-binding proteins of
RT Saccharomyces cerevisiae.";
RL Yeast 7:229-244(1991).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 FUNCTION IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12824466; DOI=10.1073/pnas.1432898100;
RA Hanbauer I., Boja E.S., Moskovitz J.;
RT "A homologue of elongation factor 1 gamma regulates methionine sulfoxide
RT reductase A gene expression in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8199-8204(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, 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 [10]
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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-219, INTERACTION WITH EFB1, AND
RP PUTATIVE STRUCTURE OF THE EEF1 COMPLEX.
RX PubMed=12972429; DOI=10.1074/jbc.m306630200;
RA Jeppesen M.G., Ortiz P.A., Shepard W., Kinzy T.G., Nyborg J.,
RA Andersen G.R.;
RT "The crystal structure of the glutathione S-transferase-like domain of
RT elongation factor 1Bgamma from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:47190-47198(2003).
CC -!- FUNCTION: Subunit of the eukaryotic elongation factor 1 complex (eEF1).
CC Probably plays a role in anchoring the complex to other cellular
CC components. May be involved in transcriptional regulation of MXR1.
CC {ECO:0000269|PubMed:12824466}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC -!- SUBUNIT: The eukaryotic elongation factor 1 complex (eEF1) is probably
CC a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1
CC or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably
CC dimerized via the eF1Bgamma subunits. The eEF1B subcomplex with the GEF
CC activity is formed of eEF1Balpha and eEF1Bgamma. CAM1 interacts with
CC EFB1. Component of a complex bound to MXR1 promoter region.
CC {ECO:0000269|PubMed:12972429}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: Ths GST-like domain mediates the interaction to eEFB1 and may
CC be responsible for dimerization of the eEF1 complex.
CC -!- MISCELLANEOUS: Present with 60865 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 isoforms for eEF1Bgamma in yeast.
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DR EMBL; L01879; AAA16892.1; -; Unassigned_DNA.
DR EMBL; X67917; CAA48116.1; -; Genomic_DNA.
DR EMBL; U44030; AAB68173.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11382.1; -; Genomic_DNA.
DR PIR; S29345; S29345.
DR RefSeq; NP_015277.1; NM_001183862.1.
DR PDB; 1NHY; X-ray; 3.00 A; A=1-219.
DR PDBsum; 1NHY; -.
DR AlphaFoldDB; P29547; -.
DR SMR; P29547; -.
DR BioGRID; 36132; 190.
DR ComplexPortal; CPX-2854; Elongation Factor eEF1 complex, variant CAM1.
DR DIP; DIP-6813N; -.
DR IntAct; P29547; 12.
DR MINT; P29547; -.
DR STRING; 4932.YPL048W; -.
DR CarbonylDB; P29547; -.
DR iPTMnet; P29547; -.
DR MaxQB; P29547; -.
DR PaxDb; 4932-YPL048W; -.
DR PeptideAtlas; P29547; -.
DR EnsemblFungi; YPL048W_mRNA; YPL048W; YPL048W.
DR GeneID; 856059; -.
DR KEGG; sce:YPL048W; -.
DR AGR; SGD:S000005969; -.
DR SGD; S000005969; CAM1.
DR VEuPathDB; FungiDB:YPL048W; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR GeneTree; ENSGT00940000176354; -.
DR HOGENOM; CLU_011226_3_0_1; -.
DR InParanoid; P29547; -.
DR OMA; TQYFSWT; -.
DR OrthoDB; 159792at2759; -.
DR BioCyc; YEAST:G3O-33961-MONOMER; -.
DR Reactome; R-SCE-156842; Eukaryotic Translation Elongation.
DR UniPathway; UPA00345; -.
DR BioGRID-ORCS; 856059; 0 hits in 10 CRISPR screens.
DR EvolutionaryTrace; P29547; -.
DR PRO; PR:P29547; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P29547; Protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; NAS:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005840; C:ribosome; IDA:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IDA:SGD.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006449; P:regulation of translational termination; IGI:SGD.
DR GO; GO:0006414; P:translational elongation; IDA:SGD.
DR CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR CDD; cd03044; GST_N_EF1Bgamma; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 3.30.70.1010; Translation elongation factor EF1B, gamma chain, conserved domain; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR PANTHER; PTHR43986:SF1; ELONGATION FACTOR 1-GAMMA; 1.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF89942; eEF1-gamma domain; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Elongation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..415
FT /note="Elongation factor 1-gamma 1"
FT /id="PRO_0000208831"
FT DOMAIN 2..78
FT /note="GST N-terminal"
FT DOMAIN 89..215
FT /note="GST C-terminal"
FT DOMAIN 254..415
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 212..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 191
FT /note="W -> C (in Ref. 1; AAA16892)"
FT /evidence="ECO:0000305"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 12..24
FT /evidence="ECO:0007829|PDB:1NHY"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:1NHY"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:1NHY"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:1NHY"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 126..147
FT /evidence="ECO:0007829|PDB:1NHY"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:1NHY"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1NHY"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:1NHY"
SQ SEQUENCE 415 AA; 47088 MW; 17BCE60FFB7B2890 CRC64;
MSQGTLYANF RIRTWVPRGL VKALKLDVKV VTPDAAAEQF ARDFPLKKVP AFVGPKGYKL
TEAMAINYYL VKLSQDDKMK TQLLGADDDL NAQAQIIRWQ SLANSDLCIQ IANTIVPLKG
GAPYNKKSVD SAMDAVDKIV DIFENRLKNY TYLATENISL ADLVAASIFT RYFESLFGTE
WRAQHPAIVR WFNTVRASPF LKDEYKDFKF ADKPLSPPQK KKEKKAPAAA PAASKKKEEA
KPAATETETS SKKPKHPLEL LGKSTFVLDD WKRKYSNEDT RPVALPWFWE HYNPEEYSLW
KVTYKYNDEL TLTFMSNNLV GGFFNRLSAS TKYMFGCLVV YGENNNNGIV GAVMVRGQDY
VPAFDVAPDW ESYDYAKLDP TNDDDKEFIN NMWAWDKPVS VNGEPKEIVD GKVLK
//
