ID PACC_YEAST Reviewed; 625 AA. AC P33400; D3DKU1; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 02-SEP-2026, entry version 208. DE RecName: Full=pH-response transcription factor pacC/RIM101; DE AltName: Full=Regulator of IME2 protein 1; DE AltName: Full=pH-response regulator protein RIM101; GN Name=RIM101; Synonyms=RIM1; OrderedLocusNames=YHL027W; 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], AND MUTAGENESIS OF CYS-153; CYS-189; RP CYS-217 AND SER-255. RC STRAIN=SK1; RX PubMed=8367297; DOI=10.1093/nar/21.16.3789; RA Su S.S.Y., Mitchell A.P.; RT "Molecular characterization of the yeast meiotic regulatory gene RIM1."; RL Nucleic Acids Res. 21:3789-3797(1993). 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 PROTEOLYTIC PROCESSING. RX PubMed=9017390; DOI=10.1093/genetics/145.1.63; RA Li W., Mitchell A.P.; RT "Proteolytic activation of Rim1p, a positive regulator of yeast sporulation RT and invasive growth."; RL Genetics 145:63-73(1997). RN [6] RP FUNCTION. RX PubMed=11050096; DOI=10.1074/jbc.m008381200; RA Lamb T.M., Xu W., Diamond A., Mitchell A.P.; RT "Alkaline response genes of Saccharomyces cerevisiae and their relationship RT to the RIM101 pathway."; RL J. Biol. Chem. 276:1850-1856(2001). RN [7] RP INTERACTION WITH RIM20. RX PubMed=11698381; DOI=10.1128/jb.183.23.6917-6923.2001; RA Xu W., Mitchell A.P.; RT "Yeast PalA/AIP1/Alix homolog Rim20p associates with a PEST-like region and RT is required for its proteolytic cleavage."; RL J. Bacteriol. 183:6917-6923(2001). RN [8] RP FUNCTION IN TRANSCRIPTIONAL REPRESSION, AND DNA-BINDING. RX PubMed=12509465; DOI=10.1128/mcb.23.2.677-686.2003; RA Lamb T.M., Mitchell A.P.; RT "The transcription factor Rim101p governs ion tolerance and cell RT differentiation by direct repression of the regulatory genes NRG1 and SMP1 RT in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 23:677-686(2003). RN [9] 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 [10] 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 [11] RP IDENTIFICATION BY 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: Transcription factor that mediates regulation of both CC acid- and alkaline-expressed genes in response to ambient pH. At CC alkaline ambient pH, activates transcription of alkaline-expressed CC genes (including RIM101 itself), mainly by repressing transcriptional CC repressors of those genes, and represses transcription of acid- CC expressed genes. Required for meiosis, sporulation and invasive growth. CC {ECO:0000269|PubMed:11050096, ECO:0000269|PubMed:12509465}. CC -!- SUBUNIT: Binds to DNA. Interacts with RIM20, which probably binds to CC the two YPX[LI] motifs and is required for proteolytic processing. CC {ECO:0000269|PubMed:11698381}. CC -!- INTERACTION: CC P33400; P43603: LSB3; NbExp=2; IntAct=EBI-14422, EBI-22980; CC P33400; Q12033: RIM20; NbExp=3; IntAct=EBI-14422, EBI-38947; CC P33400; P32793: YSC84; NbExp=2; IntAct=EBI-14422, EBI-24460; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000269|PubMed:14562095}. CC -!- PTM: Activated by C-terminal proteolytic cleavage. At neutral to CC alkaline ambient pH, the signaling protease (probably RIM13) cleaves CC RIM101, removing a C-terminal 8 kDa peptide to yield the active form. CC {ECO:0000269|PubMed:9017390}. CC -!- MISCELLANEOUS: Present with 1822 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the pacC/RIM101 family. {ECO:0000305}. 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; X72960; CAA51462.1; -; Genomic_DNA. DR EMBL; U11583; AAB65039.1; -; Genomic_DNA. DR EMBL; AY693138; AAT93157.1; -; Genomic_DNA. DR EMBL; BK006934; DAA06658.1; -; Genomic_DNA. DR PIR; S48941; S48941. DR RefSeq; NP_011836.1; NM_001179107.1. DR AlphaFoldDB; P33400; -. DR BioGRID; 36395; 484. DR DIP; DIP-1564N; -. DR FunCoup; P33400; 1870. DR IntAct; P33400; 12. DR MINT; P33400; -. DR STRING; 4932.YHL027W; -. DR GlyGen; P33400; 4 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P33400; -. DR PaxDb; 4932-YHL027W; -. DR PeptideAtlas; P33400; -. DR EnsemblFungi; YHL027W_mRNA; YHL027W; YHL027W. DR GeneID; 856358; -. DR KEGG; sce:YHL027W; -. DR AGR; SGD:S000001019; -. DR SGD; S000001019; RIM101. DR VEuPathDB; FungiDB:YHL027W; -. DR eggNOG; KOG1721; Eukaryota. DR HOGENOM; CLU_029652_0_0_1; -. DR InParanoid; P33400; -. DR OMA; DRIWGYM; -. DR OrthoDB; 6155966at2759; -. DR BioCyc; YEAST:G3O-31047-MONOMER; -. DR BioGRID-ORCS; 856358; 1 hit in 13 CRISPR screens. DR PRO; PR:P33400; -. DR Proteomes; UP000002311; Chromosome VIII. DR RNAct; P33400; protein. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0030437; P:ascospore formation; IMP:SGD. DR GO; GO:0071469; P:cellular response to alkaline pH; IMP:SGD. DR GO; GO:0071454; P:cellular response to anoxia; IMP:SGD. DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:SGD. DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD. DR GO; GO:0010973; P:positive regulation of division septum assembly; IGI:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR FunFam; 3.30.160.60:FF:001369; pH-response transcription factor pacC/RIM101; 1. DR FunFam; 3.30.160.60:FF:000340; zinc finger protein 473 isoform X1; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2. DR InterPro; IPR050806; pacC/RIM101. DR InterPro; IPR048420; Zap1-like_Znf1. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR47257; PH-RESPONSE TRANSCRIPTION FACTOR PACC/RIM101; 1. DR PANTHER; PTHR47257:SF1; PH-RESPONSE TRANSCRIPTION FACTOR PACC_RIM101; 1. DR Pfam; PF21816; Zap1_zf1; 1. DR Pfam; PF00096; zf-C2H2; 1. DR SMART; SM00355; ZnF_C2H2; 3. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. PE 1: Evidence at protein level; KW Activator; Cytoplasm; DNA-binding; Meiosis; Metal-binding; Nucleus; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..625 FT /note="pH-response transcription factor pacC/RIM101" FT /id="PRO_0000046847" FT ZN_FING 146..171 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 182..206 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 212..234 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..138 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 228..234 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250" FT MOTIF 450..453 FT /note="YPX[LI] motif 1" FT MOTIF 620..623 FT /note="YPX[LI] motif 2" FT COMPBIAS 77..94 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 107..121 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 153 FT /note="C->S: Abolishes transcriptional activation of target FT genes." FT /evidence="ECO:0000269|PubMed:8367297" FT MUTAGEN 189 FT /note="C->S: Abolishes transcriptional activation of target FT genes." FT /evidence="ECO:0000269|PubMed:8367297" FT MUTAGEN 217 FT /note="C->S: Abolishes transcriptional activation of target FT genes." FT /evidence="ECO:0000269|PubMed:8367297" FT MUTAGEN 255 FT /note="S->A: Reduces transcriptional activation of target FT genes." FT /evidence="ECO:0000269|PubMed:8367297" FT CONFLICT 68 FT /note="N -> K (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 90 FT /note="T -> S (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 111 FT /note="S -> P (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 249 FT /note="W -> L (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 261 FT /note="C -> S (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="A -> G (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 308 FT /note="Q -> QQQQ (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 358 FT /note="R -> Q (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 486 FT /note="V -> I (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" FT CONFLICT 519 FT /note="G -> E (in Ref. 1; CAA51462)" FT /evidence="ECO:0000305" SQ SEQUENCE 625 AA; 68232 MW; AD71E7B2D679E17E CRC64; MVPLEDLLNK ENGTAAPQHS RESIVENGTD VSNVTKKDGL PSPNLSKRSS DCSKRPRIRC TTEAIGLNGQ EDERMSPGST SSSCLPYHST SHLNTPPYDL LGASAVSPTT SSSSDSSSSS PLAQAHNPAG DDDDADNDGD SEDITLYCKW DNCGMIFNQP ELLYNHLCHD HVGRKSHKNL QLNCHWGDCT TKTEKRDHIT SHLRVHVPLK PFGCSTCSKK FKRPQDLKKH LKIHLESGGI LKRKRGPKWG SKRTSKKNKS CASDAVSSCS ASVPSAIAGS FKSHSTSPQI LPPLPVGISQ HLPSQQQQRA ISLNQLCSDE LSQYKPVYSP QLSARLQTIL PPLYYNNGST VSQGANSRSM NVYEDGCSNK TIANATQFFT KLSRNMTNNY ILQQSGGSTE SSSSSGRIPV AQTSYVQPPN APSYQSVQGG SSISATANTA TYVPVRLAKY PTGPSLTEHL PPLHSNTAGG VFNRQSQYAM PHYPSVRAAP SYSSSGCSIL PPLQSKIPML PSRRTMAGGT SLKPNWEFSL NQKSCTNDII MSKLAIEEVD DESEIEDDFV EMLGIVNIIK DYLLCCVMED LDDEESEDKD EENAFLQESL EKLSLQNQMG TNSVRILTKY PKILV //