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   02-SEP-2026, entry version 219.
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; DOI=10.1038/387s103;
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   AlphaFoldDB; P29547; -.
DR   SMR; P29547; -.
DR   BioGRID; 36132; 199.
DR   ComplexPortal; CPX-2854; Elongation Factor eEF1 complex, variant CAM1.
DR   DIP; DIP-6813N; -.
DR   FunCoup; P29547; 1159.
DR   IntAct; P29547; 20.
DR   MINT; P29547; -.
DR   STRING; 4932.YPL048W; -.
DR   CarbonylDB; P29547; -.
DR   iPTMnet; 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   HOGENOM; CLU_011226_3_0_1; -.
DR   InParanoid; P29547; -.
DR   OMA; TQYFSWT; -.
DR   OrthoDB; 249703at2759; -.
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   CD-CODE; E03F929F; Stress granule.
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:InterPro.
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:ComplexPortal.
DR   CDD; cd03181; GST_C_EF1Bgamma_like; 1.
DR   CDD; cd03044; GST_N_EF1Bgamma; 1.
DR   FunFam; 1.20.1050.10:FF:000006; Elongation factor 1 gamma; 1.
DR   FunFam; 3.40.30.10:FF:000142; Elongation factor 1 gamma; 1.
DR   FunFam; 3.30.70.1010:FF:000001; Elongation factor 1-gamma 1; 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.
DR   PDBsum; 1NHY; -.
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..102
FT                   /evidence="ECO:0007829|PDB:1NHY"
FT   HELIX           103..107
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
//