ESS1_YEAST
ID ESS1_YEAST Reviewed; 170 AA.
AC P22696; D6VWJ3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase ESS1;
DE Short=PPIase ESS1;
DE EC=5.2.1.8;
DE AltName: Full=Parvulin ESS1;
DE AltName: Full=Processing/termination factor 1;
GN Name=ESS1; Synonyms=PIN1, PTF1; OrderedLocusNames=YJR017C; ORFNames=J1452;
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].
RC STRAIN=DBY864;
RX PubMed=2648698; DOI=10.1002/yea.320050108;
RA Hanes S.D., Shank P.R., Bostian K.A.;
RT "Sequence and mutational analysis of ESS1, a gene essential for growth in
RT Saccharomyces cerevisiae.";
RL Yeast 5:55-72(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DH484;
RX PubMed=7781779; DOI=10.1016/0014-5793(95)00471-k;
RA Hani J., Stumpf G., Domdey H.;
RT "PTF1 encodes an essential protein in Saccharomyces cerevisiae, which shows
RT strong homology with a new putative family of PPIases.";
RL FEBS Lett. 365:198-202(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 ACTIVITY REGULATION.
RX PubMed=9558330; DOI=10.1021/bi973162p;
RA Hennig L., Christner C., Kipping M., Schelbert B., Ruecknagel K.P.,
RA Grabley S., Kuellertz G., Fischer G.;
RT "Selective inactivation of parvulin-like peptidyl-prolyl cis/trans
RT isomerases by juglone.";
RL Biochemistry 37:5953-5960(1998).
RN [6]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-127 AND GLY-162.
RX PubMed=9867817; DOI=10.1074/jbc.274.1.108;
RA Hani J., Schelbert B., Bernhardt A., Domdey H., Fischer G., Wiebauer K.,
RA Rahfeld J.-U.;
RT "Mutations in a peptidylprolyl-cis/trans-isomerase gene lead to a defect in
RT 3'-end formation of a pre-mRNA in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:108-116(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH RPB1.
RX PubMed=10531363; DOI=10.1074/jbc.274.44.31583;
RA Morris D.P., Phatnani H.P., Greenleaf A.L.;
RT "Phospho-carboxyl-terminal domain binding and the role of a prolyl
RT isomerase in pre-mRNA 3'-End formation.";
RL J. Biol. Chem. 274:31583-31587(1999).
RN [8]
RP INTERACTION WITH SIN3.
RX PubMed=10899127; DOI=10.1093/emboj/19.14.3739;
RA Arevalo-Rodriguez M., Cardenas M.E., Wu X., Hanes S.D., Heitman J.;
RT "Cyclophilin A and Ess1 interact with and regulate silencing by the Sin3-
RT Rpd3 histone deacetylase.";
RL EMBO J. 19:3739-3749(2000).
RN [9]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [10]
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 [11]
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 [12]
RP MUTAGENESIS OF CYS-120; SER-122 AND HIS-164.
RX PubMed=15728580; DOI=10.1074/jbc.m412172200;
RA Gemmill T.R., Wu X., Hanes S.D.;
RT "Vanishingly low levels of Ess1 prolyl-isomerase activity are sufficient
RT for growth in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:15510-15517(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Essential PPIase specific for phosphoserine and
CC phosphothreonine N-terminal to the proline residue. Required for
CC efficient pre-mRNA 3'-end processing and transcription termination,
CC probably by inducing conformational changes by proline-directed
CC isomerization in the C-terminal domain (CTD) of RPB1, thereby altering
CC cofactor binding with the RNA polymerase II transcription complex. Also
CC targets the SIN3-RPD3 histone deacetylase complex (HDAC).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:9867817};
CC -!- ACTIVITY REGULATION: Inhibited by 5-hydroxy-1,4-naphthoquinone
CC (juglone), but not by FK506 or cyclosporin A.
CC {ECO:0000269|PubMed:9558330}.
CC -!- SUBUNIT: Interacts with the RNA polymerase II largest subunit (RPB1)
CC and with the SIN1-RDP3 HDAC subunit SIN3. {ECO:0000269|PubMed:10531363,
CC ECO:0000269|PubMed:10899127}.
CC -!- INTERACTION:
CC P22696; P07278: BCY1; NbExp=2; IntAct=EBI-6679, EBI-9475;
CC P22696; P10592: SSA2; NbExp=2; IntAct=EBI-6679, EBI-8603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The WW domain binds to the phosphorylated tandem 7 residues
CC repeats of RPB1.
CC -!- MISCELLANEOUS: Present with 4401 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA60941.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA89541.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=Ref.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X85972; CAA59961.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60941.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z49517; CAA89541.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006943; DAA08809.1; -; Genomic_DNA.
DR PIR; S52764; S52764.
DR RefSeq; NP_012551.2; NM_001181675.1.
DR PDB; 7KKF; X-ray; 2.40 A; A/B=1-170.
DR PDBsum; 7KKF; -.
DR AlphaFoldDB; P22696; -.
DR SMR; P22696; -.
DR BioGRID; 33773; 1012.
DR DIP; DIP-3856N; -.
DR ELM; P22696; -.
DR IntAct; P22696; 115.
DR MINT; P22696; -.
DR STRING; 4932.YJR017C; -.
DR BindingDB; P22696; -.
DR iPTMnet; P22696; -.
DR MaxQB; P22696; -.
DR PaxDb; P22696; -.
DR PRIDE; P22696; -.
DR TopDownProteomics; P22696; -.
DR EnsemblFungi; YJR017C_mRNA; YJR017C; YJR017C.
DR GeneID; 853475; -.
DR KEGG; sce:YJR017C; -.
DR SGD; S000003778; ESS1.
DR VEuPathDB; FungiDB:YJR017C; -.
DR eggNOG; KOG3259; Eukaryota.
DR GeneTree; ENSGT00640000091578; -.
DR HOGENOM; CLU_090028_0_1_1; -.
DR InParanoid; P22696; -.
DR OMA; DEVQCLH; -.
DR BioCyc; YEAST:YJR017C-MON; -.
DR Reactome; R-SCE-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-SCE-6811555; PI5P Regulates TP53 Acetylation.
DR PRO; PR:P22696; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P22696; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:SGD.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD.
DR GO; GO:0031064; P:negative regulation of histone deacetylation; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:SGD.
DR GO; GO:2000749; P:positive regulation of rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IGI:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:1901407; P:regulation of phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00639; Rotamase; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isomerase; Nucleus; Phosphoprotein;
KW Reference proteome; Rotamase.
FT CHAIN 1..170
FT /note="Peptidyl-prolyl cis-trans isomerase ESS1"
FT /id="PRO_0000193433"
FT DOMAIN 9..43
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 57..170
FT /note="PpiC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
FT REGION 30..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 120
FT /note="C->R: Abolishes PPIase activity."
FT /evidence="ECO:0000269|PubMed:15728580"
FT MUTAGEN 122
FT /note="S->P: Abolishes PPIase activity."
FT /evidence="ECO:0000269|PubMed:15728580"
FT MUTAGEN 127
FT /note="G->D: In PTF1-2; decreases the catalytic efficiency
FT 20-fold."
FT /evidence="ECO:0000269|PubMed:9867817"
FT MUTAGEN 162
FT /note="G->S: In PTF1-5; decreases the catalytic efficiency
FT 12-fold."
FT /evidence="ECO:0000269|PubMed:9867817"
FT MUTAGEN 164
FT /note="H->R: Abolishes PPIase activity."
FT /evidence="ECO:0000269|PubMed:15728580"
FT CONFLICT 8
FT /note="R -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="V -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="D -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:7KKF"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:7KKF"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:7KKF"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:7KKF"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:7KKF"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:7KKF"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:7KKF"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:7KKF"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:7KKF"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:7KKF"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:7KKF"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:7KKF"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:7KKF"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7KKF"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:7KKF"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:7KKF"
SQ SEQUENCE 170 AA; 19405 MW; 18D3EC02E8395175 CRC64;
MPSDVASRTG LPTPWTVRYS KSKKREYFFN PETKHSQWEE PEGTNKDQLH KHLRDHPVRV
RCLHILIKHK DSRRPASHRS ENITISKQDA TDELKTLITR LDDDSKTNSF EALAKERSDC
SSYKRGGDLG WFGRGEMQPS FEDAAFQLKV GEVSDIVESG SGVHVIKRVG
