OPI1_YEAST
ID OPI1_YEAST Reviewed; 404 AA.
AC P21957; D3DKP9;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Transcriptional repressor OPI1;
DE AltName: Full=Negative regulator of phospholipid biosynthesis;
DE AltName: Full=Overproducer of inositol protein 1;
GN Name=OPI1; OrderedLocusNames=YHL020C;
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=1985968; DOI=10.1016/s0021-9258(17)35253-5;
RA White M.J., Hirsch J.P., Henry S.A.;
RT "The OPI1 gene of Saccharomyces cerevisiae, a negative regulator of
RT phospholipid biosynthesis, encodes a protein containing polyglutamine
RT tracts and a leucine zipper.";
RL J. Biol. Chem. 266:863-872(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 DOMAIN FFAT MOTIF, INTERACTION WITH SCS2, AND SUBCELLULAR LOCATION.
RX PubMed=12727870; DOI=10.1093/emboj/cdg201;
RA Loewen C.J.R., Roy A., Levine T.P.;
RT "A conserved ER targeting motif in three families of lipid binding proteins
RT and in Opi1p binds VAP.";
RL EMBO J. 22:2025-2035(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP INTERACTION WITH SCS2.
RX PubMed=15455074; DOI=10.1371/journal.pbio.0020342;
RA Brickner J.H., Walter P.;
RT "Gene recruitment of the activated INO1 locus to the nuclear membrane.";
RL PLoS Biol. 2:1843-1852(2004).
RN [9]
RP FUNCTION, PHOSPHATIDIC ACID-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=15192221; DOI=10.1126/science.1096083;
RA Loewen C.J.R., Gaspar M.L., Jesch S.A., Delon C., Ktistakis N.T.,
RA Henry S.A., Levine T.P.;
RT "Phospholipid metabolism regulated by a transcription factor sensing
RT phosphatidic acid.";
RL Science 304:1644-1647(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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).
CC -!- FUNCTION: Negative regulator of the transcriptional complex INO2-INO4
CC in response to phospholipid precursor availability. When precursors
CC become limiting, OPI1 is retained at the endoplasmic reticulum (ER) and
CC INO2-INO4 activates INO1 and other genes required for phospholipid
CC biosynthesis, whereas abundant precursor availability results in
CC targeting of OPI1 to the nucleus to repress transcription of these
CC genes. Binds directly to phosphatidic acid, which is required for ER
CC targeting and may act as sensing mechanism for precursor availability,
CC as phosphatidic acid becomes rapidly depleted upon phospholipid
CC biosynthesis. {ECO:0000269|PubMed:15192221}.
CC -!- SUBUNIT: Interacts with SCS2. {ECO:0000269|PubMed:12727870,
CC ECO:0000269|PubMed:15455074}.
CC -!- INTERACTION:
CC P21957; P40075: SCS2; NbExp=3; IntAct=EBI-12555, EBI-16735;
CC P21957; P22579: SIN3; NbExp=6; IntAct=EBI-12555, EBI-17160;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:12727870, ECO:0000269|PubMed:15192221}. Nucleus
CC {ECO:0000269|PubMed:15192221}. Note=Maintained at the endoplasmic
CC reticulum by SCS2 (PubMed:12727870). In response to elevated inositol
CC levels, translocates to the nucleus (PubMed:15192221).
CC -!- DOMAIN: The FFAT motif is required for interaction with SCS2 and proper
CC localization of the protein. {ECO:0000269|PubMed:12727870}.
CC -!- MISCELLANEOUS: Present with 1281 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57383; AAA34828.1; -; Genomic_DNA.
DR EMBL; U11582; AAB65073.1; -; Genomic_DNA.
DR EMBL; AY558103; AAS56429.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06665.1; -; Genomic_DNA.
DR PIR; S13741; S13741.
DR RefSeq; NP_011843.1; NM_001179100.1.
DR AlphaFoldDB; P21957; -.
DR SMR; P21957; -.
DR BioGRID; 36403; 477.
DR DIP; DIP-5505N; -.
DR ELM; P21957; -.
DR IntAct; P21957; 8.
DR STRING; 4932.YHL020C; -.
DR iPTMnet; P21957; -.
DR MaxQB; P21957; -.
DR PaxDb; P21957; -.
DR PRIDE; P21957; -.
DR EnsemblFungi; YHL020C_mRNA; YHL020C; YHL020C.
DR GeneID; 856366; -.
DR KEGG; sce:YHL020C; -.
DR SGD; S000001012; OPI1.
DR VEuPathDB; FungiDB:YHL020C; -.
DR eggNOG; ENOG502RG16; Eukaryota.
DR HOGENOM; CLU_039546_0_0_1; -.
DR InParanoid; P21957; -.
DR OMA; HYANCEE; -.
DR BioCyc; YEAST:G3O-31040-MON; -.
DR PRO; PR:P21957; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P21957; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IPI:SGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR013927; TF_Opi1.
DR PANTHER; PTHR38406; PTHR38406; 2.
DR Pfam; PF08618; Opi1; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Nucleus; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..404
FT /note="Transcriptional repressor OPI1"
FT /id="PRO_0000058061"
FT REGION 25..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..138
FT /note="Basic motif"
FT REGION 139..160
FT /note="Leucine-zipper"
FT REGION 170..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 200..206
FT /note="FFAT"
FT COMPBIAS 378..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 404 AA; 46065 MW; 59E55D7BE7122EDA CRC64;
MSENQRLGLS EEEVEAAEVL GVLKQSCRQK SQPSEDVSQA DKMPASESST TPLNILDRVS
NKIISNVVTF YDEINTNKRP LKSIGRLLDD DDDEHDDYDY NDDEFFTNKR QKLSRAIAKG
KDNLKEYKLN MSIESKKRLV TCLHLLKLAN KQLSDKISCL QDLVEKEQVH PLHKQDGNAR
TTTGAGEDET SSDEDDDDEE FFDASEQVNA SEQSIVVKME VVGTVKKVYS LISKFTANSL
PEPARSQVRE SLLNLPTNWF DSVHSTSLPH HASFHYANCE EQKVEQQQQQ QQQQQQQQLL
QQQLLQQQQQ KRNKDGDDSA SPSSSVTANG KVLILAKESL EMVRNVMGVV DSTLGKAEEW
VKQKQEVKEM IRERFLQQQQ QYRQQQQKDG NYVKPSQDNV DSKD
