IF1A_YEAST
ID IF1A_YEAST Reviewed; 153 AA.
AC P38912; D6W086;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Eukaryotic translation initiation factor 1A;
DE Short=eIF-1A;
DE AltName: Full=Eukaryotic translation initiation factor 4C;
DE Short=eIF-4C;
GN Name=TIF11; OrderedLocusNames=YMR260C; ORFNames=YM8156.02C;
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].
RC STRAIN=X2180 / W303-1A;
RX PubMed=7559407; DOI=10.1074/jbc.270.39.22788;
RA Wei C.-L., Kainuma M., Hershey J.W.B.;
RT "Characterization of yeast translation initiation factor 1A and cloning of
RT its essential gene.";
RL J. Biol. Chem. 270:22788-22794(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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].
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Seems to be required for maximal rate of protein
CC biosynthesis. Enhances ribosome dissociation into subunits and
CC stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC subunits.
CC -!- MISCELLANEOUS: Present with 35100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR EMBL; U11585; AAA82039.1; -; Genomic_DNA.
DR EMBL; Z49260; CAA89243.1; -; Genomic_DNA.
DR EMBL; AY557964; AAS56290.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10160.1; -; Genomic_DNA.
DR PIR; S47943; S47943.
DR RefSeq; NP_013987.1; NM_001182767.1.
DR PDB; 3J80; EM; 3.75 A; i=1-153.
DR PDB; 3J81; EM; 4.00 A; i=1-153.
DR PDB; 3JAM; EM; 3.46 A; i=1-153.
DR PDB; 3JAP; EM; 4.90 A; i=1-153.
DR PDB; 3JAQ; EM; 6.00 A; i=1-153.
DR PDB; 3WBK; X-ray; 3.30 A; C=27-153.
DR PDB; 6FYX; EM; 3.05 A; i=1-153.
DR PDB; 6FYY; EM; 3.05 A; i=1-153.
DR PDB; 6GSM; EM; 5.15 A; i=21-115.
DR PDB; 6GSN; EM; 5.75 A; i=5-115.
DR PDB; 6ZCE; EM; 5.30 A; i=1-153.
DR PDB; 6ZU9; EM; 6.20 A; A=1-153.
DR PDBsum; 3J80; -.
DR PDBsum; 3J81; -.
DR PDBsum; 3JAM; -.
DR PDBsum; 3JAP; -.
DR PDBsum; 3JAQ; -.
DR PDBsum; 3WBK; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6GSM; -.
DR PDBsum; 6GSN; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; P38912; -.
DR SMR; P38912; -.
DR BioGRID; 35438; 207.
DR DIP; DIP-4401N; -.
DR IntAct; P38912; 3.
DR MINT; P38912; -.
DR STRING; 4932.YMR260C; -.
DR iPTMnet; P38912; -.
DR MaxQB; P38912; -.
DR PaxDb; P38912; -.
DR PRIDE; P38912; -.
DR EnsemblFungi; YMR260C_mRNA; YMR260C; YMR260C.
DR GeneID; 855302; -.
DR KEGG; sce:YMR260C; -.
DR SGD; S000004873; TIF11.
DR VEuPathDB; FungiDB:YMR260C; -.
DR eggNOG; KOG3403; Eukaryota.
DR GeneTree; ENSGT00390000008256; -.
DR HOGENOM; CLU_109098_0_1_1; -.
DR InParanoid; P38912; -.
DR OMA; IWINNGD; -.
DR BioCyc; YEAST:G3O-32935-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:P38912; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38912; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:SGD.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IDA:SGD.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:SGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0043024; F:ribosomal small subunit 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:0001732; P:formation of cytoplasmic translation initiation complex; IMP:SGD.
DR GO; GO:0001677; P:formation of translation initiation ternary complex; IMP:SGD.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IDA:SGD.
DR GO; GO:0002188; P:translation reinitiation; IMP:SGD.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd05793; S1_IF1A; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00216; aIF_1A; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR001253; TIF_eIF-1A.
DR InterPro; IPR018104; TIF_eIF-1A_CS.
DR PANTHER; PTHR21668; PTHR21668; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00523; eIF-1A; 1.
DR PROSITE; PS01262; IF1A; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..153
FT /note="Eukaryotic translation initiation factor 1A"
FT /id="PRO_0000145113"
FT DOMAIN 22..96
FT /note="S1-like"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:3JAM"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:3JAM"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:3JAM"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:3JAM"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3JAM"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:3JAM"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:3JAM"
SQ SEQUENCE 153 AA; 17435 MW; AEF000104BBA3041 CRC64;
MGKKNTKGGK KGRRGKNDSD GPKRELIYKE EGQEYAQITK MLGNGRVEAS CFDGNKRMAH
IRGKLRKKVW MGQGDIILVS LRDFQDDQCD VVHKYNLDEA RTLKNQGELP ENAKINETDN
FGFESDEDVN FEFGNADEDD EEGEDEELDI DDI
