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Database: UniProt
Entry: P32911
LinkDB: P32911
Original site: P32911 
ID   SUI1_YEAST              Reviewed;         108 AA.
AC   P32911; D6W0U9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   07-APR-2021, entry version 157.
DE   RecName: Full=Eukaryotic translation initiation factor eIF-1;
DE   AltName: Full=Protein translation factor SUI1;
GN   Name=SUI1; Synonyms=RFR1; OrderedLocusNames=YNL244C; ORFNames=N0905;
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=ATCC 204508 / S288c;
RX   PubMed=1729602; DOI=10.1128/mcb.12.1.248;
RA   Yoon H., Donahue T.F.;
RT   "The sui1 suppressor locus in Saccharomyces cerevisiae encodes a
RT   translation factor that functions during tRNA(iMet) recognition of the
RT   start codon.";
RL   Mol. Cell. Biol. 12:248-260(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9234673;
RX   DOI=10.1002/(sici)1097-0061(199707)13:9<849::aid-yea106>3.0.co;2-n;
RA   Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.;
RT   "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the
RT   left arm of chromosome XIV from Saccharomyces cerevisiae.";
RL   Yeast 13:849-860(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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: Additional factor that functions in concert with eIF-2 and
CC       the initiator tRNA in directing the ribosome to the proper start site
CC       of translation.
CC   -!- SUBUNIT: The factors eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-
CC       tRNAi form a multifactor complex (MFC) that may bind to the 40S
CC       ribosome. Interacts with NIP1. {ECO:0000269|PubMed:9671501}.
CC   -!- SIMILARITY: Belongs to the SUI1 family. {ECO:0000305}.
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DR   EMBL; M77514; AAA35131.1; -; Genomic_DNA.
DR   EMBL; X96722; CAA65499.1; -; Genomic_DNA.
DR   EMBL; Z71520; CAA96150.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10315.1; -; Genomic_DNA.
DR   PIR; S31245; S31245.
DR   RefSeq; NP_014155.1; NM_001183082.1.
DR   PDB; 2OGH; NMR; -; A=1-108.
DR   PDB; 2RVH; NMR; -; A=1-108.
DR   PDB; 3J80; EM; 3.75 A; j=1-108.
DR   PDB; 3J81; EM; 4.00 A; m=1-108.
DR   PDB; 3JAM; EM; 3.46 A; j=1-108.
DR   PDB; 3JAP; EM; 4.90 A; m=1-108.
DR   PDB; 3JAQ; EM; 6.00 A; m=1-108.
DR   PDB; 6GSM; EM; 5.15 A; m=13-108.
DR   PDB; 6GSN; EM; 5.75 A; m=19-108.
DR   PDB; 6ZCE; EM; 5.30 A; m=1-108.
DR   PDBsum; 2OGH; -.
DR   PDBsum; 2RVH; -.
DR   PDBsum; 3J80; -.
DR   PDBsum; 3J81; -.
DR   PDBsum; 3JAM; -.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   PDBsum; 6GSM; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6ZCE; -.
DR   SMR; P32911; -.
DR   BioGRID; 35595; 67.
DR   DIP; DIP-1471N; -.
DR   IntAct; P32911; 65.
DR   MINT; P32911; -.
DR   STRING; 4932.YNL244C; -.
DR   iPTMnet; P32911; -.
DR   MaxQB; P32911; -.
DR   PaxDb; P32911; -.
DR   PRIDE; P32911; -.
DR   EnsemblFungi; YNL244C_mRNA; YNL244C; YNL244C.
DR   GeneID; 855477; -.
DR   KEGG; sce:YNL244C; -.
DR   SGD; S000005188; SUI1.
DR   VEuPathDB; FungiDB:YNL244C; -.
DR   eggNOG; KOG1770; Eukaryota.
DR   GeneTree; ENSGT00940000176611; -.
DR   HOGENOM; CLU_082805_3_2_1; -.
DR   InParanoid; P32911; -.
DR   OMA; ICHIRIQ; -.
DR   EvolutionaryTrace; P32911; -.
DR   PRO; PR:P32911; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P32911; protein.
DR   GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IDA:SGD.
DR   GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR   GO; GO:0043024; F:ribosomal small subunit binding; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
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:0001731; P:formation of translation preinitiation complex; IDA:SGD.
DR   GO; GO:1990145; P:maintenance of translational fidelity; IMP:SGD.
DR   GO; GO:0006450; P:regulation of translational fidelity; IMP:SGD.
DR   CDD; cd11566; eIF1_SUI1; 1.
DR   InterPro; IPR001950; SUI1.
DR   InterPro; IPR036877; SUI1_dom_sf.
DR   InterPro; IPR005874; SUI1_euk.
DR   Pfam; PF01253; SUI1; 1.
DR   PIRSF; PIRSF004499; SUI1_euk; 1.
DR   SUPFAM; SSF55159; SSF55159; 1.
DR   TIGRFAMs; TIGR01160; SUI1_MOF2; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Protein biosynthesis; Reference proteome;
KW   Translation regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..108
FT                   /note="Eukaryotic translation initiation factor eIF-1"
FT                   /id="PRO_0000130566"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   STRAND          26..32
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          34..36
FT                   /evidence="ECO:0007744|PDB:2OGH"
FT   STRAND          38..44
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          47..49
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   HELIX           51..62
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          67..69
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   TURN            72..74
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          77..83
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   HELIX           86..94
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          100..105
FT                   /evidence="ECO:0007744|PDB:3JAM"
SQ   SEQUENCE   108 AA;  12312 MW;  03ECB94F3EF3A417 CRC64;
     MSIENLKSFD PFADTGDDET ATSNYIHIRI QQRNGRKTLT TVQGVPEEYD LKRILKVLKK
     DFACNGNIVK DPEMGEIIQL QGDQRAKVCE FMISQLGLQK KNIKIHGF
//
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