IGO1_YEAST
ID IGO1_YEAST Reviewed; 168 AA.
AC P53897; D6W126;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=mRNA stability protein IGO1;
DE AltName: Full=Initiation of G zero protein 1;
GN Name=IGO1; OrderedLocusNames=YNL157W; ORFNames=N1743;
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 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, 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 [8]
RP INTERACTION WITH RIM15; DHH1; PBP1; PBP4 AND LSM12, PHOSPHORYLATION AT
RP SER-64, AND FUNCTION.
RX PubMed=20471941; DOI=10.1016/j.molcel.2010.02.039;
RA Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S.,
RA Devgan G., Snyder M., Broach J.R., De Virgilio C.;
RT "Initiation of the TORC1-regulated G0 program requires Igo1/2, which
RT license specific mRNAs to evade degradation via the 5'-3' mRNA decay
RT pathway.";
RL Mol. Cell 38:345-355(2010).
CC -!- FUNCTION: Required for TORC1 to properly control gene expression and
CC chronological life span. Plays an essential role in initiation of the
CC G0 program by preventing the degradation of specific nutrient-regulated
CC mRNAs via the 5'-3' mRNA decay pathway. {ECO:0000269|PubMed:20471941}.
CC -!- SUBUNIT: Interacts with RIM15, DHH1, PBP1, PBP4 AND LSM12.
CC {ECO:0000269|PubMed:20471941}.
CC -!- PTM: Phosphorylated at Ser-64 by RIM15. {ECO:0000269|PubMed:20471941}.
CC -!- SIMILARITY: Belongs to the endosulfine family. {ECO:0000305}.
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DR EMBL; X92517; CAA63282.1; -; Genomic_DNA.
DR EMBL; Z71433; CAA96044.1; -; Genomic_DNA.
DR EMBL; AY558004; AAS56330.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10392.1; -; Genomic_DNA.
DR PIR; S60970; S60970.
DR RefSeq; NP_014242.1; NM_001182995.1.
DR AlphaFoldDB; P53897; -.
DR BioGRID; 35672; 70.
DR DIP; DIP-2011N; -.
DR IntAct; P53897; 12.
DR MINT; P53897; -.
DR STRING; 4932.YNL157W; -.
DR iPTMnet; P53897; -.
DR MaxQB; P53897; -.
DR PaxDb; P53897; -.
DR PRIDE; P53897; -.
DR EnsemblFungi; YNL157W_mRNA; YNL157W; YNL157W.
DR GeneID; 855565; -.
DR KEGG; sce:YNL157W; -.
DR SGD; S000005101; IGO1.
DR VEuPathDB; FungiDB:YNL157W; -.
DR eggNOG; KOG4076; Eukaryota.
DR GeneTree; ENSGT00940000174856; -.
DR HOGENOM; CLU_135184_0_0_1; -.
DR InParanoid; P53897; -.
DR BioCyc; YEAST:G3O-33173-MON; -.
DR PRO; PR:P53897; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53897; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:SGD.
DR GO; GO:0048255; P:mRNA stabilization; IGI:SGD.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IGI:SGD.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IBA:GO_Central.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:1903452; P:positive regulation of G1 to G0 transition; IGI:SGD.
DR GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; IGI:SGD.
DR GO; GO:1905184; P:positive regulation of protein serine/threonine phosphatase activity; IGI:SGD.
DR InterPro; IPR006760; Endosulphine.
DR PANTHER; PTHR10358; PTHR10358; 1.
DR Pfam; PF04667; Endosulfine; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..168
FT /note="mRNA stability protein IGO1"
FT /id="PRO_0000203416"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20471941,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 168 AA; 18051 MW; 9534A95F1BD2CFFB CRC64;
MSNENLSPNS SNPDLTKLNN GESGTIDTSK FSPNEMKLYK MYGKLPSKKD IFKHTMQKRK
YFDSGDYALQ KAGIQNNDPI NYGKNNLPLT NPSKLREDII KRRISTCPST ASTAGVVDNA
TLIQKEGSIS SGPPSSNNGT IGGGSTSSTP VGNHSSSSSS LYTESPIR
