ID   INO2_YEAST              Reviewed;         304 AA.
AC   P26798; D6VSA9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Protein INO2;
GN   Name=INO2; Synonyms=DIE1, SCS1; OrderedLocusNames=YDR123C;
GN   ORFNames=YD9727.18C;
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=1620625; DOI=10.1093/nar/20.12.3253;
RA   Nikoloff D.M., McGraw P., Henry S.A.;
RT   "The INO2 gene of Saccharomyces cerevisiae encodes a helix-loop-helix
RT   protein that is required for activation of phospholipid synthesis.";
RL   Nucleic Acids Res. 20:3253-3253(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8188619; DOI=10.1093/oxfordjournals.jbchem.a124287;
RA   Hosaka K., Nikawa J., Kodaki T., Yamashita S.;
RT   "Cloning and characterization of the SCS1 gene required for the expression
RT   of genes in yeast phospholipid synthesis.";
RL   J. Biochem. 115:131-136(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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   CHARACTERIZATION.
RX   PubMed=8125958; DOI=10.1016/s0021-9258(17)37299-x;
RA   Nikoloff D.M., Henry S.A.;
RT   "Functional characterization of the INO2 gene of Saccharomyces cerevisiae.
RT   A positive regulator of phospholipid biosynthesis.";
RL   J. Biol. Chem. 269:7402-7411(1994).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=7565092; DOI=10.1111/j.1365-2958.1995.tb02302.x;
RA   Nikawa J., Hosaka K.;
RT   "Isolation and characterization of genes that promote the expression of
RT   inositol transporter gene ITR1 in Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 16:301-308(1995).
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).
CC   -!- FUNCTION: Positive regulatory factor required for depression of the
CC       coregulated phospholipid biosynthetic enzymes. Also involved in the
CC       expression of ITR1.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P26798; P13902: INO4; NbExp=2; IntAct=EBI-9262, EBI-9270;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X66066; CAA46866.1; -; Genomic_DNA.
DR   EMBL; D90460; BAA14424.1; -; Genomic_DNA.
DR   EMBL; Z48758; CAA88676.1; -; Genomic_DNA.
DR   EMBL; AY557685; AAS56011.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11969.1; -; Genomic_DNA.
DR   PIR; S21570; S21570.
DR   RefSeq; NP_010408.1; NM_001180431.1.
DR   AlphaFoldDB; P26798; -.
DR   SMR; P26798; -.
DR   BioGRID; 32179; 509.
DR   ComplexPortal; CPX-1277; INO2-INO4 transcription activation complex.
DR   DIP; DIP-680N; -.
DR   IntAct; P26798; 3.
DR   MINT; P26798; -.
DR   STRING; 4932.YDR123C; -.
DR   PaxDb; P26798; -.
DR   PRIDE; P26798; -.
DR   EnsemblFungi; YDR123C_mRNA; YDR123C; YDR123C.
DR   GeneID; 851701; -.
DR   KEGG; sce:YDR123C; -.
DR   SGD; S000002530; INO2.
DR   VEuPathDB; FungiDB:YDR123C; -.
DR   eggNOG; ENOG502S8Z5; Eukaryota.
DR   HOGENOM; CLU_052055_0_0_1; -.
DR   InParanoid; P26798; -.
DR   OMA; YEMINNE; -.
DR   BioCyc; YEAST:G3O-29723-MON; -.
DR   PRO; PR:P26798; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P26798; protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IDA:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Lipid biosynthesis; Lipid metabolism; Nucleus;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..304
FT                   /note="Protein INO2"
FT                   /id="PRO_0000127253"
FT   DOMAIN          236..290
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
SQ   SEQUENCE   304 AA;  34234 MW;  ADF0F0D745A12CE8 CRC64;
     MQQATGNELL GILDLDNDID FETAYQMLSS NFDDQMSAHI HENTFSATSP PLLTHELGII
     PNVATVQPSH VETIPADNQT HHAPLHTHAH YLNHNPHQPS MGFDQALGLK LSPSSSGLLS
     TNESNAIEQF LDNLISQDMM SSNASMNSES HLHIRSPKKQ HRYTELNQRY PETHPHSNTG
     ELPTNTADVP TEFTTREGPH QPIGNDHYNP PPFSVPEIRI PDSDIPANIE DDPVKVRKWK
     HVQMEKIRRI NTKEAFERLI KSVRTPPKEN GKRIPKHILL TCVMNDIKSI RSANEALQHI
     LDDS