IF4F1_YEAST
ID IF4F1_YEAST Reviewed; 952 AA.
AC P39935; D6VUU6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Eukaryotic initiation factor 4F subunit p150;
DE Short=eIF-4F p150 {ECO:0000303|PubMed:8336723};
DE Short=eIF4F p150;
DE AltName: Full=Translation initiation factor 4(4)-F(6) subunit gamma(3) protein 1 {ECO:0000303|PubMed:8336723};
DE AltName: Full=eIF4G1;
DE AltName: Full=mRNA cap-binding protein complex subunit p150;
GN Name=TIF4631 {ECO:0000303|PubMed:8336723}; OrderedLocusNames=YGR162W;
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=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION, INTERACTION WITH PAB1, AND MUTAGENESIS OF 214-LYS--LYS-217.
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, AND ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP
RP STRUCTURE.
RX PubMed=9702200; DOI=10.1016/s1097-2765(00)80122-7;
RA Wells S.E., Hillner P.E., Vale R.D., Sachs A.B.;
RT "Circularization of mRNA by eukaryotic translation initiation factors.";
RL Mol. Cell 2:135-140(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 PAB1.
RX PubMed=10944120; DOI=10.1093/emboj/19.16.4372;
RA Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G.;
RT "The eukaryotic mRNA decapping protein Dcp1 interacts physically and
RT functionally with the eIF4F translation initiation complex.";
RL EMBO J. 19:4372-4382(2000).
RN [10]
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 [11]
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181 AND SER-948, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND THR-888, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908 AND SER-948, AND
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND IDENTIFICATION BY
RP 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).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=23222640; DOI=10.1038/nsmb.2468;
RA Mitchell S.F., Jain S., She M., Parker R.;
RT "Global analysis of yeast mRNPs.";
RL Nat. Struct. Mol. Biol. 20:127-133(2013).
RN [18]
RP PHOSPHORYLATION AT SER-163; SER-195; SER-503; SER-892; SER-896; SER-908 AND
RP SER-948.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
RN [19] {ECO:0007744|PDB:1RF8}
RP STRUCTURE BY NMR OF 389-488.
RX PubMed=14675538; DOI=10.1016/s0092-8674(03)00975-9;
RA Gross J.D., Moerke N.J., von der Haar T., Lugovskoy A.A., Sachs A.B.,
RA McCarthy J.E.G., Wagner G.;
RT "Ribosome loading onto the mRNA cap is driven by conformational coupling
RT between eIF4G and eIF4E.";
RL Cell 115:739-750(2003).
RN [20] {ECO:0007744|PDB:2VSO, ECO:0007744|PDB:2VSX}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 572-854.
RX PubMed=18606994; DOI=10.1073/pnas.0800418105;
RA Schuetz P., Bumann M., Oberholzer A.E., Bieniossek C., Trachsel H.,
RA Altmann M., Baumann U.;
RT "Crystal structure of the yeast eIF4A-eIF4G complex: an RNA-helicase
RT controlled by protein-protein interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9564-9569(2008).
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. TIF4631 is probably essential when
CC TIF4632 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:10944120,
CC ECO:0000269|PubMed:11741542, ECO:0000269|PubMed:9256432,
CC ECO:0000269|PubMed:9702200}.
CC -!- INTERACTION:
CC P39935; P07260: CDC33; NbExp=14; IntAct=EBI-9002, EBI-150;
CC P39935; P04147: PAB1; NbExp=16; IntAct=EBI-9002, EBI-12823;
CC P39935; P10081: TIF2; NbExp=10; IntAct=EBI-9002, EBI-9017;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:23222640}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:23222640}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:23222640}.
CC -!- MISCELLANEOUS: Present with 9760 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; L16923; AAA02757.1; -; Genomic_DNA.
DR EMBL; Z72947; CAA97184.1; -; Genomic_DNA.
DR EMBL; AY692973; AAT92992.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08257.1; -; Genomic_DNA.
DR PIR; S64473; S64473.
DR RefSeq; NP_011678.3; NM_001181291.3.
DR PDB; 1RF8; NMR; -; B=391-488.
DR PDB; 2VSO; X-ray; 2.60 A; E/F=572-854.
DR PDB; 2VSX; X-ray; 2.80 A; E/F=572-854.
DR PDB; 6Z29; NMR; -; A=35-49.
DR PDBsum; 1RF8; -.
DR PDBsum; 2VSO; -.
DR PDBsum; 2VSX; -.
DR PDBsum; 6Z29; -.
DR AlphaFoldDB; P39935; -.
DR SMR; P39935; -.
DR BioGRID; 33414; 405.
DR ComplexPortal; CPX-430; Eukaryotic translation initiation factor 4F complex, variant TIF4631.
DR DIP; DIP-985N; -.
DR ELM; P39935; -.
DR IntAct; P39935; 74.
DR MINT; P39935; -.
DR STRING; 4932.YGR162W; -.
DR iPTMnet; P39935; -.
DR MaxQB; P39935; -.
DR PaxDb; P39935; -.
DR PRIDE; P39935; -.
DR EnsemblFungi; YGR162W_mRNA; YGR162W; YGR162W.
DR GeneID; 853071; -.
DR KEGG; sce:YGR162W; -.
DR SGD; S000003394; TIF4631.
DR VEuPathDB; FungiDB:YGR162W; -.
DR eggNOG; KOG0401; Eukaryota.
DR GeneTree; ENSGT00940000154675; -.
DR HOGENOM; CLU_006715_1_0_1; -.
DR InParanoid; P39935; -.
DR OMA; ANISVWE; -.
DR BioCyc; YEAST:G3O-30861-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 EvolutionaryTrace; P39935; -.
DR PRO; PR:P39935; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P39935; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
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:0005739; C:mitochondrion; HDA: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; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0010942; P:positive regulation of cell death; IGI:ParkinsonsUK-UCL.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IGI:ParkinsonsUK-UCL.
DR GO; GO:1901195; P:positive regulation of formation of translation preinitiation complex; IDA:SGD.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IGI:ParkinsonsUK-UCL.
DR GO; GO:1902280; P:regulation of RNA helicase activity; IDA:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IC:ComplexPortal.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR GO; GO:0006413; P:translational initiation; IMP:SGD.
DR DisProt; DP00082; -.
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 3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..952
FT /note="Eukaryotic initiation factor 4F subunit p150"
FT /id="PRO_0000213331"
FT DOMAIN 607..850
FT /note="MIF4G"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..299
FT /note="Interaction with PAB1"
FT REGION 481..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 888
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 214..217
FT /note="KLRK->AAAA: In TIF4631-213; abolishes interaction
FT with PAB1 and inhibits poly(A)-dependent translation."
FT /evidence="ECO:0000269|PubMed:9256432"
FT CONFLICT 7
FT /note="H -> Q (in Ref. 1; AAA02757)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="T -> N (in Ref. 1; AAA02757)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="Q -> K (in Ref. 1; AAA02757)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="R -> K (in Ref. 1; AAA02757)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="D -> E (in Ref. 1; AAA02757)"
FT /evidence="ECO:0000305"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6Z29"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:1RF8"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:1RF8"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:1RF8"
FT HELIX 454..464
FT /evidence="ECO:0007829|PDB:1RF8"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:1RF8"
FT HELIX 603..615
FT /evidence="ECO:0007829|PDB:2VSO"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:2VSX"
FT HELIX 622..634
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 643..658
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 663..676
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 692..709
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 733..755
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 761..776
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 781..798
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 812..827
FT /evidence="ECO:0007829|PDB:2VSO"
FT HELIX 834..848
FT /evidence="ECO:0007829|PDB:2VSO"
SQ SEQUENCE 952 AA; 107101 MW; 391256802F86118E CRC64;
MTDETAHPTQ SASKQESAAL KQTGDDQQES QQQRGYTNYN NGSNYTQKKP YNSNRPHQQR
GGKFGPNRYN NRGNYNGGGS FRGGHMGANS SNVPWTGYYN NYPVYYQPQQ MAAAGSAPAN
PIPVEEKSPV PTKIEITTKS GEHLDLKEQH KAKLQSQERS TVSPQPESKL KETSDSTSTS
TPTPTPSTND SKASSEENIS EAEKTRRNFI EQVKLRKAAL EKKRKEQLEG SSGNNNIPMK
TTPENVEEKG SDKPEVTEKT KPAEEKSAEP EVKQETPAEE GEQGEKGQIK EESTPKVLTF
AERLKLKKQQ KEREEKTEGK ENKEVPVQEE TKSAIESAPV PPSEQVKEET EVAETEQSNI
DESATTPAIP TKSDEAEAEV EAEAGDAGTK IGLEAEIETT TDETDDGTNT VSHILNVLKD
ATPIEDVFSF NYPEGIEGPD IKYKKEHVKY TYGPTFLLQF KDKLNVKADA EWVQSTASKI
VIPPGMGRGN RSRDSGRFGN NSSRGHDFRN TSVRNMDDRA NSRTSSKRRS KRMNDDRRSN
RSYTSRRDRE RGSYRNEEKR EDDKPKEEVA PLVPSANRWV PKFKSKKTEK KLAPDGKTEL
LDKDEVERKM KSLLNKLTLE MFDAISSEIL AIANISVWET NGETLKAVIE QIFLKACDEP
HWSSMYAQLC GKVVKELNPD ITDETNEGKT GPKLVLHYLV ARCHAEFDKG WTDKLPTNED
GTPLEPEMMS EEYYAAASAK RRGLGLVRFI GFLYRLNLLT GKMMFECFRR LMKDLTDSPS
EETLESVVEL LNTVGEQFET DSFRTGQATL EGSQLLDSLF GILDNIIQTA KISSRIKFKL
IDIKELRHDK NWNSDKKDNG PKTIQQIHEE EERQRQLKNN SRSNSRRTNN SSNRHSFRRD
APPASKDSFI TTRTYSQRNS QRAPPPKEEP AAPTSTATNM FSALMGESDD EE
