EF1G2_YEAST
ID EF1G2_YEAST Reviewed; 412 AA.
AC P36008; D6VXK6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Elongation factor 1-gamma 2;
DE Short=EF-1-gamma 2;
DE AltName: Full=Eukaryotic elongation factor 1Bgamma 2;
DE Short=eEF1Bgamma 2;
DE AltName: Full=Translation elongation factor 1B gamma 2;
GN Name=TEF4; Synonyms=EFC1; OrderedLocusNames=YKL081W;
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=8041634; DOI=10.1093/nar/22.13.2703;
RA Kinzy T.G., Ripmaster T.L., Woolford J.L. Jr.;
RT "Multiple genes encode the translation elongation factor EF-1 gamma in
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 22:2703-2707(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-412.
RX PubMed=1730668; DOI=10.1016/s0021-9258(18)48351-2;
RA Beltran C., Kopecky J., Pan Y.-C.E., Nelson H., Nelson N.;
RT "Cloning and mutational analysis of the gene encoding subunit C of yeast
RT vacuolar H(+)-ATPase.";
RL J. Biol. Chem. 267:774-779(1992).
RN [5]
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 [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 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).
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 (By similarity). {ECO:0000250}.
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. TEF4 interacts with
CC EFB1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P36008; P43573: BUD27; NbExp=3; IntAct=EBI-6329, EBI-22787;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 102130 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; L01880; AAA21473.1; -; Genomic_DNA.
DR EMBL; Z28081; CAA81919.1; -; Genomic_DNA.
DR EMBL; Z28080; CAA81918.1; -; Genomic_DNA.
DR EMBL; M77143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006944; DAA09076.1; -; Genomic_DNA.
DR PIR; S37906; S37906.
DR RefSeq; NP_012842.1; NM_001179647.1.
DR AlphaFoldDB; P36008; -.
DR SMR; P36008; -.
DR BioGRID; 34051; 366.
DR ComplexPortal; CPX-425; Elongation Factor eEF1 complex, variant TEF4.
DR DIP; DIP-6386N; -.
DR IntAct; P36008; 60.
DR MINT; P36008; -.
DR STRING; 4932.YKL081W; -.
DR CarbonylDB; P36008; -.
DR iPTMnet; P36008; -.
DR MaxQB; P36008; -.
DR PaxDb; P36008; -.
DR PRIDE; P36008; -.
DR EnsemblFungi; YKL081W_mRNA; YKL081W; YKL081W.
DR GeneID; 853781; -.
DR KEGG; sce:YKL081W; -.
DR SGD; S000001564; TEF4.
DR VEuPathDB; FungiDB:YKL081W; -.
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR GeneTree; ENSGT00940000176354; -.
DR HOGENOM; CLU_011226_3_0_1; -.
DR InParanoid; P36008; -.
DR OMA; VQWATEN; -.
DR BioCyc; YEAST:G3O-31876-MON; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:P36008; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36008; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005840; C:ribosome; IDA:ComplexPortal.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0003746; F:translation elongation factor activity; TAS:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0006414; P:translational elongation; IDA:SGD.
DR Gene3D; 3.30.70.1010; -; 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; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF89942; SSF89942; 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 Acetylation; Cytoplasm; Elongation factor; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..412
FT /note="Elongation factor 1-gamma 2"
FT /id="PRO_0000208832"
FT DOMAIN 2..77
FT /note="GST N-terminal"
FT DOMAIN 86..217
FT /note="GST C-terminal"
FT DOMAIN 251..412
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 216..253
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 CONFLICT 8
FT /note="I -> L (in Ref. 1; AAA21473)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="Missing (in Ref. 1; AAA21473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 46520 MW; 42F1B5B25EF66189 CRC64;
MSQGTLYINR SPRNYASEAL ISYFKLDVKI VDLEQSSEFA SLFPLKQAPA FLGPKGLKLT
EALAIQFYLA NQVADEKERA RLLGSDVIEK SQILRWASLA NSDVMSNIAR PFLSFKGLIP
YNKKDVDACF VKIDNLAAVF DARLRDYTFV ATENISLGDL HAAGSWAFGL ATILGPEWRA
KHPHLMRWFN TVAASPIVKT PFAEVKLAEK ALTYTPPKKQ KAEKPKAEKS KAEKKKDEAK
PADDAAPAKK PKHPLEALGK STFVLDDWKR KYSNDDTRPV ALPWFWEHYN PEEYSIWKVG
YKYNDELTLT FMSNNLVGGF FNRLSASTKY MFGCLVVYGE NNNNGIVGAV MVRGQDFAPA
FDVAPDWESY EYTKLDPTKE EDKEFVNNMW AWDKPVVVNG EDKEIVDGKV LK
