ID   IF4F2_YEAST             Reviewed;         914 AA.
AC   P39936; D6VU91;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 204.
DE   RecName: Full=Eukaryotic initiation factor 4F subunit p130;
DE            Short=eIF-4F p130;
DE            Short=eIF4F p130;
DE   AltName: Full=Translation initiation factor 4(4)-F(6) subunit gamma(3) protein 2 {ECO:0000303|PubMed:8336723};
DE   AltName: Full=eIF4G2;
DE   AltName: Full=mRNA cap-binding protein complex subunit p130;
GN   Name=TIF4632 {ECO:0000303|PubMed:8336723}; OrderedLocusNames=YGL049C;
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=8336723; DOI=10.1128/mcb.13.8.4860-4874.1993;
RA   Goyer C., Altmann M., Lee H.S., Blanc A., Deshmukh M., Woolford J.L. Jr.,
RA   Trachsel H., Sonenberg N.;
RT   "TIF4631 and TIF4632: two yeast genes encoding the high-molecular-weight
RT   subunits of the cap-binding protein complex (eukaryotic initiation factor
RT   4F) contain an RNA recognition motif-like sequence and carry out an
RT   essential function.";
RL   Mol. Cell. Biol. 13:4860-4874(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9234674;
RX   DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA   Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT   "The characterization of two new clusters of duplicated genes suggests a
RT   'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL   Yeast 13:861-869(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869; DOI=10.1038/387s081;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   INTERACTION WITH PAB1.
RX   PubMed=9003792; DOI=10.1002/j.1460-2075.1996.tb01108.x;
RA   Tarun S.Z. Jr., Sachs A.B.;
RT   "Association of the yeast poly(A) tail binding protein with translation
RT   initiation factor eIF-4G.";
RL   EMBO J. 15:7168-7177(1996).
RN   [6]
RP   FUNCTION, INTERACTION WITH PAB1, AND MUTAGENESIS OF 233-ARG--LYS-236.
RX   PubMed=9256432; DOI=10.1073/pnas.94.17.9046;
RA   Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B.;
RT   "Translation initiation factor eIF4G mediates in vitro poly(A) tail-
RT   dependent translation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997).
RN   [7]
RP   INTERACTION WITH PAB1.
RX   PubMed=9418852; DOI=10.1128/mcb.18.1.51;
RA   Kessler S.H., Sachs A.B.;
RT   "RNA recognition motif 2 of yeast Pab1p is required for its functional
RT   interaction with eukaryotic translation initiation factor 4G.";
RL   Mol. Cell. Biol. 18:51-57(1998).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH PAB1.
RX   PubMed=10357826; DOI=10.1093/emboj/18.11.3153;
RA   Otero L.J., Ashe M.P., Sachs A.B.;
RT   "The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-
RT   dependent and cap-dependent translation by distinct mechanisms.";
RL   EMBO J. 18:3153-3163(1999).
RN   [9]
RP   INTERACTION WITH PAT1.
RX   PubMed=11741542; DOI=10.1016/s1097-2765(01)00395-1;
RA   Tharun S., Parker R.;
RT   "Targeting an mRNA for decapping: displacement of translation factors and
RT   association of the Lsm1p-7p complex on deadenylated yeast mRNAs.";
RL   Mol. Cell 8:1075-1083(2001).
RN   [10]
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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-301 AND SER-913, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; THR-196 AND SER-913, AND
RP   IDENTIFICATION BY 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: Component of the eIF4F complex, which interacts with the mRNA
CC       cap structure and serves as an initial point of assembly for the
CC       translation apparatus. Stimulates translation by interaction with
CC       polyadenylate-binding protein PAB1, bringing the 5'- and 3'-ends of the
CC       mRNA in proximity. The formation of this circular mRNP structure
CC       appears to be critical for the synergistic effects of the cap and the
CC       poly(A) tail in facilitating translation initiation, recycling of
CC       ribosomes, and mRNA stability. TIF4632 is probably essential when
CC       TIF4631 is missing. {ECO:0000269|PubMed:10357826,
CC       ECO:0000269|PubMed:9256432}.
CC   -!- SUBUNIT: Component of the eIF4F complex, which composition varies with
CC       external and internal environmental conditions. It is composed of at
CC       least eIF4A (TIF1/TIF2), eIF4E (TIF45) and eIF4G (TIF4631 or TIF4632)
CC       (By similarity). Interacts with PAT1 in a RNA-dependent manner.
CC       {ECO:0000250, ECO:0000269|PubMed:10357826, ECO:0000269|PubMed:11741542,
CC       ECO:0000269|PubMed:9003792, ECO:0000269|PubMed:9256432,
CC       ECO:0000269|PubMed:9418852}.
CC   -!- INTERACTION:
CC       P39936; P04147: PAB1; NbExp=5; IntAct=EBI-9006, EBI-12823;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3390 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4G family.
CC       {ECO:0000305}.
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DR   EMBL; L16924; AAA18474.1; -; Unassigned_DNA.
DR   EMBL; Z72571; CAA96751.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08052.1; -; Genomic_DNA.
DR   PIR; B48086; B48086.
DR   RefSeq; NP_011466.1; NM_001180914.1.
DR   AlphaFoldDB; P39936; -.
DR   SMR; P39936; -.
DR   BioGRID; 33199; 189.
DR   ComplexPortal; CPX-431; Eukaryotic translation initiation factor 4F complex, variant TIF4632.
DR   DIP; DIP-330N; -.
DR   ELM; P39936; -.
DR   FunCoup; P39936; 511.
DR   IntAct; P39936; 75.
DR   STRING; 4932.YGL049C; -.
DR   GlyCosmos; P39936; 2 sites, 1 glycan.
DR   GlyGen; P39936; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; P39936; -.
DR   PaxDb; 4932-YGL049C; -.
DR   PeptideAtlas; P39936; -.
DR   EnsemblFungi; YGL049C_mRNA; YGL049C; YGL049C.
DR   GeneID; 852833; -.
DR   KEGG; sce:YGL049C; -.
DR   AGR; SGD:S000003017; -.
DR   SGD; S000003017; TIF4632.
DR   VEuPathDB; FungiDB:YGL049C; -.
DR   eggNOG; KOG0401; Eukaryota.
DR   HOGENOM; CLU_006715_1_0_1; -.
DR   InParanoid; P39936; -.
DR   OMA; AAFKKFW; -.
DR   OrthoDB; 514777at2759; -.
DR   BioCyc; YEAST:G3O-30559-MONOMER; -.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-166208; mTORC1-mediated signalling.
DR   Reactome; R-SCE-429947; Deadenylation of mRNA.
DR   Reactome; R-SCE-72649; Translation initiation complex formation.
DR   Reactome; R-SCE-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR   Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR   Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 852833; 2 hits in 10 CRISPR screens.
DR   CD-CODE; 26E28FFB; Synthetic Condensate 000009.
DR   CD-CODE; A777E0F8; P-body.
DR   CD-CODE; BD836276; Synthetic Condensate 000030.
DR   CD-CODE; CABCA76D; Synthetic Condensate 000018.
DR   CD-CODE; CEC93CD4; Synthetic Condensate 000048.
DR   CD-CODE; E03F929F; Stress granule.
DR   PRO; PR:P39936; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P39936; protein.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IMP:SGD.
DR   GO; GO:0000932; C:P-body; IDA:SGD.
DR   GO; GO:0005840; C:ribosome; NAS:ComplexPortal.
DR   GO; GO:0001671; F:ATPase activator activity; ISS:SGD.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR   GO; GO:0031369; F:translation initiation factor binding; IDA:SGD.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR   GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; ISS:SGD.
DR   GO; GO:0006446; P:regulation of translational initiation; NAS:ComplexPortal.
DR   GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR   GO; GO:0006413; P:translational initiation; IDA:SGD.
DR   FunFam; 1.25.40.180:FF:000020; Eukaryotic translation initiation factor subunit; 1.
DR   FunFam; 1.20.970.30:FF:000002; Translation initiation factor eIF4G; 1.
DR   Gene3D; 1.25.40.180; -; 1.
DR   Gene3D; 1.20.970.30; eIF4G, eIF4E-binding domain; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR022745; eIF4G1_eIF4E-bd.
DR   InterPro; IPR036211; eIF4G_eIF4E-bd_sf.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   PANTHER; PTHR23253; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA; 1.
DR   PANTHER; PTHR23253:SF9; EUKARYOTIC TRANSLATION INITIATION FACTOR 4 GAMMA 2; 1.
DR   Pfam; PF12152; eIF_4G1; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF101489; Eukaryotic initiation factor 4f subunit eIF4g, eIF4e-binding domain; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   Reference proteome; RNA-binding; Translation regulation.
FT   CHAIN           1..914
FT                   /note="Eukaryotic initiation factor 4F subunit p130"
FT                   /id="PRO_0000213332"
FT   DOMAIN          567..810
FT                   /note="MIF4G"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..315
FT                   /note="Interaction with PAB1"
FT   REGION          240..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..12
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..155
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..263
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..325
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        841..867
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..886
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         196
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         301
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MUTAGEN         233..236
FT                   /note="RLRK->AVAA: In TIF4632-233; abolishes interaction
FT                   with PAB1 and inhibits poly(A)-dependent translation."
FT                   /evidence="ECO:0000269|PubMed:9256432"
SQ   SEQUENCE   914 AA;  103899 MW;  BF5E9805CD47908E CRC64;
     MTDQRGPPPP HPQQANGYKK FPPHDNQYSG ANNSQPNNHY NENLYSAREP HNNKQYQSKN
     GKYGTNKYNN RNNSQGNAQY YNNRFNNGYR LNNNDYNPAM LPGMQWPANY YAPQMYYIPQ
     QMVPVASPPY THQPLNTNPE PPSTPKTTKI EITTKTGERL NLKKFHEEKK ASKGEEKNDG
     VEQKSKSGTP FEKEATPVLP ANEAVKDTLT ETSNEKSTSE AENTKRLFLE QVRLRKAAME
     RKKNGLISET EKKQETSNHD NTDTTKPNSV IESEPIKEAP KPTGEANEVV IDGKSGASVK
     TPQHVTGSVT KSVTFNEPEN ESSSQDVDEL VKDDDTTEIS DTTGGKTVNK SDDETINSVI
     TTEENTVKET EPSTSDIEMP TVSQLLETLG KAQPISDIYE FAYPENVERP DIKYKKPSVK
     YTYGPTFLLQ FKDKLKFRPD PAWVEAVSSK IVIPPHIARN KPKDSGRFGG DFRSPSMRGM
     DHTSSSRVSS KRRSKRMGDD RRSNRGYTSR KDREKAAEKA EEQAPKEEIA PLVPSANRWI
     PKSRVKKTEK KLAPDGKTEL FDKEEVERKM KSLLNKLTLE MFDSISSEIL DIANQSKWED
     DGETLKIVIE QIFHKACDEP HWSSMYAQLC GKVVKDLDPN IKDKENEGKN GPKLVLHYLV
     ARCHEEFEKG WADKLPAGED GNPLEPEMMS DEYYIAAAAK RRGLGLVRFI GYLYCLNLLT
     GKMMFECFRR LMKDLNNDPS EETLESVIEL LNTVGEQFEH DKFVTPQATL EGSVLLDNLF
     MLLQHIIDGG TISNRIKFKL IDVKELREIK HWNSAKKDAG PKTIQQIHQE EEQLRQKKNS
     QRSNSRFNNH NQSNSNRYSS NRRNMQNTQR DSFASTKTGS FRNNQRNARK VEEVSQAPRA
     NMFDALMNND GDSD
//