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 27-MAR-2024, entry version 202. 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; GN 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}; 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; 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; 1014. 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; 4932-YJR017C; -. DR PeptideAtlas; P22696; -. DR TopDownProteomics; P22696; -. DR EnsemblFungi; YJR017C_mRNA; YJR017C; YJR017C. DR GeneID; 853475; -. DR KEGG; sce:YJR017C; -. DR AGR; SGD:S000003778; -. 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; CSSYKRG; -. DR OrthoDB; 417859at2759; -. DR BioCyc; YEAST:YJR017C-MONOMER; -. DR Reactome; R-SCE-5668599; RHO GTPases Activate NADPH Oxidases. DR Reactome; R-SCE-6811555; PI5P Regulates TP53 Acetylation. DR BioGRID-ORCS; 853475; 10 hits in 10 CRISPR screens. 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: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:2000749; P:positive regulation of rDNA heterochromatin formation; 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:0006369; P:termination of RNA polymerase II transcription; IMP:SGD. DR CDD; cd00201; WW; 1. DR Gene3D; 2.20.70.10; -; 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 PANTHER; PTHR10657; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1. DR PANTHER; PTHR10657:SF4; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1. DR Pfam; PF00639; Rotamase; 1. DR Pfam; PF00397; WW; 1. DR SMART; SM00456; WW; 1. DR SUPFAM; SSF54534; FKBP-like; 1. DR SUPFAM; SSF51045; WW domain; 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 //