PACC_YEAST
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 03-AUG-2022, entry version 190.
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}.
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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; 476.
DR DIP; DIP-1564N; -.
DR IntAct; P33400; 10.
DR MINT; P33400; -.
DR STRING; 4932.YHL027W; -.
DR iPTMnet; P33400; -.
DR MaxQB; P33400; -.
DR PaxDb; P33400; -.
DR PRIDE; P33400; -.
DR EnsemblFungi; YHL027W_mRNA; YHL027W; YHL027W.
DR GeneID; 856358; -.
DR KEGG; sce:YHL027W; -.
DR SGD; S000001019; RIM101.
DR VEuPathDB; FungiDB:YHL027W; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_029652_0_0_1; -.
DR InParanoid; P33400; -.
DR OMA; TIANATQ; -.
DR BioCyc; YEAST:G3O-31047-MON; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 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 13..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..125
FT /note="Polar residues"
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
