IF5_YEAST
ID IF5_YEAST Reviewed; 405 AA.
AC P38431; D6W450;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=TIF5; OrderedLocusNames=YPR041W; ORFNames=YP3085.05;
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], AND PROTEIN SEQUENCE OF 19-30; 326-340
RP AND 363-377.
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=8486705; DOI=10.1016/s0021-9258(18)82230-x;
RA Chakravarti D., Maitra U.;
RT "Eukaryotic translation initiation factor 5 from Saccharomyces cerevisiae.
RT Cloning, characterization, and expression of the gene encoding the 45,346-
RT Da protein.";
RL J. Biol. Chem. 268:10524-10533(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 46191 / IL125-2B;
RX PubMed=9730282;
RX DOI=10.1002/(sici)1097-0061(199808)14:11<1027::aid-yea295>3.0.co;2-s;
RA Waskiewicz-Staniorowska B., Skala J., Jasinski M., Grenson M., Goffeau A.,
RA Ulaszewski S.;
RT "Functional analysis of three adjacent open reading frames from the right
RT arm of yeast chromosome XVI.";
RL Yeast 14:1027-1039(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
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 INTERACTION WITH NIP1.
RX PubMed=9671501; DOI=10.1128/mcb.18.8.4935;
RA Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R.,
RA Qin J., Hinnebusch A.G.;
RT "Identification of a translation initiation factor 3 (eIF3) core complex,
RT conserved in yeast and mammals, that interacts with eIF5.";
RL Mol. Cell. Biol. 18:4935-4946(1998).
RN [6]
RP INTERACTION WITH SUI3 AND NIP1, AND MUTAGENESIS OF 342-LYS--PHE-364 AND
RP 388-PHE--ASP-398.
RX PubMed=10075937; DOI=10.1093/emboj/18.6.1673;
RA Asano K., Krishnamoorthy T., Phan L., Pavitt G.D., Hinnebusch A.G.;
RT "Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon, GTPase-
RT activating and GDP-GTP exchange factors in translation initiation, mediate
RT binding to their common substrate eIF2.";
RL EMBO J. 18:1673-1688(1999).
RN [7]
RP FUNCTION, AND ASSOCIATION WITH THE 40S RIBOSOME.
RX PubMed=12651896; DOI=10.1101/gad.1065403;
RA Valasek L., Mathew A.A., Shin B.-S., Nielsen K.H., Szamecz B.,
RA Hinnebusch A.G.;
RT "The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical
RT connections with the 40S ribosome in vivo.";
RL Genes Dev. 17:786-799(2003).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-191 AND SER-397, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; THR-317 AND SER-397, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-172; THR-191 AND
RP SER-397, AND 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: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]). eIF-5 is essential for cell viability.
CC {ECO:0000269|PubMed:12651896}.
CC -!- SUBUNIT: Monomer. Interacts with NIP1 and SUI3. The factors eIF-1, eIF-
CC 2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor complex
CC (MFC) that may bind to the 40S ribosome. TIF32, NIP1 and TIF5/eIF-5
CC comprise a minimal 40S-ribosome-binding unit.
CC {ECO:0000269|PubMed:10075937, ECO:0000269|PubMed:9671501}.
CC -!- INTERACTION:
CC P38431; P32481: GCD11; NbExp=3; IntAct=EBI-9038, EBI-8924;
CC P38431; P32497: NIP1; NbExp=5; IntAct=EBI-9038, EBI-8965;
CC P38431; P20459: SUI2; NbExp=4; IntAct=EBI-9038, EBI-8915;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=P38431-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P38431-2; Sequence=VSP_018724;
CC -!- MISCELLANEOUS: Present with 48300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: [Isoform Short]: Produced by alternative initiation at
CC Met-18 of isoform Long. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; L10840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z71255; CAA94989.1; -; Genomic_DNA.
DR EMBL; Z68111; CAA92145.1; -; Genomic_DNA.
DR EMBL; Z73616; CAA97991.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11466.1; -; Genomic_DNA.
DR PIR; A46699; A46699.
DR RefSeq; NP_015366.1; NM_001184138.1. [P38431-1]
DR PDB; 2FUL; X-ray; 1.50 A; A/B/C/D/E/F=241-405.
DR PDB; 6FYX; EM; 3.05 A; m=1-405.
DR PDB; 6FYY; EM; 3.05 A; m=1-405.
DR PDB; 6ZU9; EM; 6.20 A; m=1-405.
DR PDBsum; 2FUL; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; P38431; -.
DR SMR; P38431; -.
DR BioGRID; 36218; 110.
DR DIP; DIP-2303N; -.
DR IntAct; P38431; 40.
DR MINT; P38431; -.
DR STRING; 4932.YPR041W; -.
DR iPTMnet; P38431; -.
DR MaxQB; P38431; -.
DR PaxDb; P38431; -.
DR PeptideAtlas; P38431; -.
DR PRIDE; P38431; -.
DR EnsemblFungi; YPR041W_mRNA; YPR041W; YPR041W. [P38431-1]
DR GeneID; 856154; -.
DR KEGG; sce:YPR041W; -.
DR SGD; S000006245; TIF5.
DR VEuPathDB; FungiDB:YPR041W; -.
DR eggNOG; KOG2767; Eukaryota.
DR GeneTree; ENSGT00390000016478; -.
DR HOGENOM; CLU_026663_1_0_1; -.
DR InParanoid; P38431; -.
DR OMA; YRYKMEK; -.
DR BioCyc; YEAST:G3O-34197-MON; -.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR EvolutionaryTrace; P38431; -.
DR PRO; PR:P38431; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P38431; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; 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:0001732; P:formation of cytoplasmic translation initiation complex; IDA:SGD.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0042256; P:mature ribosome assembly; IMP:SGD.
DR GO; GO:0045947; P:negative regulation of translational initiation; IMP:SGD.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Direct protein sequencing;
KW GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..405
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000007791"
FT DOMAIN 241..402
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 143..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 191
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_018724"
FT MUTAGEN 343..364
FT /note="LPKILVQLYNNDIISEEEIMRF->APKAAVQAANNDAASAAEAARA: In
FT TIF5-12A; Abolishes binding to SUI3 and NIP1."
FT MUTAGEN 388..398
FT /note="FITWLETAESD->AATAAETAAAA: In TIF5-7A; Abolishes
FT binding to SUI3 and NIP1."
FT /evidence="ECO:0000269|PubMed:10075937"
FT HELIX 244..259
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 318..333
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 337..342
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:2FUL"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:2FUL"
FT HELIX 386..394
FT /evidence="ECO:0007829|PDB:2FUL"
SQ SEQUENCE 405 AA; 45261 MW; 1A1DA563B4ED1B1F CRC64;
MSINICRDNH DPFYRYKMPP IQAKVEGRGN GIKTAVLNVA DISHALNRPA PYIVKYFGFE
LGAQTSISVD KDRYLVNGVH EPAKLQDVLD GFINKFVLCG SCKNPETEII ITKDNDLVRD
CKACGKRTPM DLRHKLSSFI LKNPPDSVSG SKKKKKAATA SANVRGGGLS ISDIAQGKSQ
NAPSDGTGSS TPQHHDEDED ELSRQIKAAA STLEDIEVKD DEWAVDMSEE AIRARAKELE
VNSELTQLDE YGEWILEQAG EDKENLPSDV ELYKKAAELD VLNDPKIGCV LAQCLFDEDI
VNEIAEHNAF FTKILVTPEY EKNFMGGIER FLGLEHKDLI PLLPKILVQL YNNDIISEEE
IMRFGTKSSK KFVPKEVSKK VRRAAKPFIT WLETAESDDD EEDDE
