IF4F2_YEAST
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 03-AUG-2022, entry version 184.
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;
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=2; 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; 140.
DR ComplexPortal; CPX-431; Eukaryotic translation initiation factor 4F complex, variant TIF4632.
DR DIP; DIP-330N; -.
DR ELM; P39936; -.
DR IntAct; P39936; 34.
DR MINT; P39936; -.
DR STRING; 4932.YGL049C; -.
DR iPTMnet; P39936; -.
DR MaxQB; P39936; -.
DR PaxDb; P39936; -.
DR PRIDE; P39936; -.
DR EnsemblFungi; YGL049C_mRNA; YGL049C; YGL049C.
DR GeneID; 852833; -.
DR KEGG; sce:YGL049C; -.
DR SGD; S000003017; TIF4632.
DR VEuPathDB; FungiDB:YGL049C; -.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000154675; -.
DR HOGENOM; CLU_006715_1_0_1; -.
DR InParanoid; P39936; -.
DR OMA; VEMELWE; -.
DR BioCyc; YEAST:G3O-30559-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-166208; mTORC1-mediated signalling.
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 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; IC: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:1901195; P:positive regulation of formation of translation preinitiation complex; ISS:SGD.
DR GO; GO:1902280; P:regulation of RNA helicase activity; ISS:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IC:ComplexPortal.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR Gene3D; 1.20.970.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022745; eIF4G1_eIF4E-bd.
DR InterPro; IPR036211; eIF4G_eIF4E-bd_sf.
DR InterPro; IPR045208; IF4G.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR PANTHER; PTHR23253; PTHR23253; 1.
DR Pfam; PF12152; eIF_4G1; 1.
DR Pfam; PF02854; MIF4G; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF101489; SSF101489; 1.
DR SUPFAM; SSF48371; SSF48371; 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..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..885
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
