INO4_YEAST
ID INO4_YEAST Reviewed; 151 AA.
AC P13902; D6W1V9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Protein INO4;
GN Name=INO4; OrderedLocusNames=YOL108C; ORFNames=HRF151;
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=2155238; DOI=10.1016/s0021-9258(19)39624-3;
RA Hoshizaki D.K., Hill J.E., Henry S.A.;
RT "The Saccharomyces cerevisiae INO4 gene encodes a small, highly basic
RT protein required for derepression of phospholipid biosynthetic enzymes.";
RL J. Biol. Chem. 265:4736-4745(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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: Transcriptional activator of phospholipid synthetic genes
CC (such as INO1, CHO1/PSS, CHO2/PEM1, OPI3/PEM2, etc.).
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. {ECO:0000250}.
CC -!- INTERACTION:
CC P13902; P26798: INO2; NbExp=2; IntAct=EBI-9270, EBI-9262;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; J05267; AAA34707.1; -; Genomic_DNA.
DR EMBL; Z48149; CAA88153.1; -; Genomic_DNA.
DR EMBL; Z74850; CAA99127.1; -; Genomic_DNA.
DR EMBL; AY693163; AAT93182.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10675.1; -; Genomic_DNA.
DR PIR; A35735; A35735.
DR RefSeq; NP_014533.1; NM_001183362.1.
DR AlphaFoldDB; P13902; -.
DR SMR; P13902; -.
DR BioGRID; 34293; 752.
DR ComplexPortal; CPX-1277; INO2-INO4 transcription activation complex.
DR DIP; DIP-86N; -.
DR IntAct; P13902; 22.
DR MINT; P13902; -.
DR STRING; 4932.YOL108C; -.
DR iPTMnet; P13902; -.
DR MaxQB; P13902; -.
DR PaxDb; P13902; -.
DR PRIDE; P13902; -.
DR TopDownProteomics; P13902; -.
DR EnsemblFungi; YOL108C_mRNA; YOL108C; YOL108C.
DR GeneID; 854042; -.
DR KEGG; sce:YOL108C; -.
DR SGD; S000005468; INO4.
DR VEuPathDB; FungiDB:YOL108C; -.
DR eggNOG; KOG3582; Eukaryota.
DR HOGENOM; CLU_145552_0_0_1; -.
DR InParanoid; P13902; -.
DR OMA; EDEVRMN; -.
DR BioCyc; YEAST:G3O-33505-MON; -.
DR PRO; PR:P13902; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P13902; 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 Gene3D; 4.10.280.10; -; 1.
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..151
FT /note="Protein INO4"
FT /id="PRO_0000127254"
FT DOMAIN 45..97
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 112..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 17378 MW; 1663EC64429E16C1 CRC64;
MTNDIKEIQT IQPGLSEIKE IKGELANVKK RKRRSKKINK LTDGQIRINH VSSEKKRREL
ERAIFDELVA VVPDLQPQES RSELIIYLKS LSYLSWLYER NEKLRKQIIA KHEAKTGSSS
SSDPVQEQNG NIRDLVPKEL IWELGDGQSG Q
