ID POP2_YEAST Reviewed; 433 AA. AC P39008; D6W1M7; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 27-MAR-2024, entry version 200. DE RecName: Full=Poly(A) ribonuclease POP2; DE EC=3.1.13.4; DE AltName: Full=CCR4-associated factor 1; GN Name=POP2; Synonyms=CAF1; OrderedLocusNames=YNR052C; ORFNames=N3470; 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=ATCC 204508 / S288c, and ATCC 204626 / S288c / A364A; RX PubMed=1475183; DOI=10.1093/nar/20.23.6227; RA Sakai A., Chibazakura T., Shimizu Y., Hishinuma F.; RT "Molecular analysis of POP2 gene, a gene required for glucose-derepression RT of gene expression in Saccharomyces cerevisiae."; RL Nucleic Acids Res. 20:6227-6233(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-433. RA Cusick M.E.; RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases. RN [6] RP CHARACTERIZATION. RX PubMed=7791755; DOI=10.1128/mcb.15.7.3487; RA Draper M.P., Salvadore C., Denis C.L.; RT "Identification of a mouse protein whose homolog in Saccharomyces RT cerevisiae is a component of the CCR4 transcriptional regulatory complex."; RL Mol. Cell. Biol. 15:3487-3495(1995). RN [7] RP IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX, AND FUNCTION OF THE CCR4-NOT RP CORE COMPLEX IN TRANSCRIPTIONAL REGULATION. RX PubMed=9463387; DOI=10.1093/emboj/17.4.1096; RA Liu H.Y., Badarinarayana V., Audino D.C., Rappsilber J., Mann M., RA Denis C.L.; RT "The NOT proteins are part of the CCR4 transcriptional complex and affect RT gene expression both positively and negatively."; RL EMBO J. 17:1096-1106(1998). RN [8] RP INTERACTION WITH NOT1. RX PubMed=10490603; DOI=10.1128/mcb.19.10.6642; RA Bai Y., Salvadore C., Chiang Y.C., Collart M.A., Liu H.Y., Denis C.L.; RT "The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and RT functionally separated from NOT2, NOT4, and NOT5."; RL Mol. Cell. Biol. 19:6642-6651(1999). RN [9] RP FUNCTION IN MRNA DEADENYLATION, AND SUBCELLULAR LOCATION. RX PubMed=11239395; DOI=10.1016/s0092-8674(01)00225-2; RA Tucker M., Valencia-Sanchez M.A., Staples R.R., Chen J., Denis C.L., RA Parker R.; RT "The transcription factor associated Ccr4 and Caf1 proteins are components RT of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae."; RL Cell 104:377-386(2001). RN [10] RP IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX. RX PubMed=11733989; DOI=10.1006/jmbi.2001.5162; RA Chen J., Rappsilber J., Chiang Y.C., Russell P., Mann M., Denis C.L.; RT "Purification and characterization of the 1.0 MDa CCR4-NOT complex RT identifies two novel components of the complex."; RL J. Mol. Biol. 314:683-694(2001). RN [11] RP FUNCTION IN MRNA DEADENYLATION. RX PubMed=11410650; DOI=10.1093/nar/29.12.2448; RA Daugeron M.-C., Mauxion F., Seraphin B.; RT "The yeast POP2 gene encodes a nuclease involved in mRNA deadenylation."; RL Nucleic Acids Res. 29:2448-2455(2001). RN [12] RP PHOSPHORYLATION AT THR-97, AND MUTAGENESIS OF THR-97. RX PubMed=11358866; DOI=10.1101/gad.884001; RA Moriya H., Shimizu-Yoshida Y., Omori A., Iwashita S., Katoh M., Sakai A.; RT "Yak1p, a DYRK family kinase, translocates to the nucleus and RT phosphorylates yeast Pop2p in response to a glucose signal."; RL Genes Dev. 15:1217-1228(2001). RN [13] 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 [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 147-433 IN COMPLEX WITH METAL RP IONS, FUNCTION IN MRNA DEADENYLATION, AND MUTAGENESIS OF SER-188 AND RP GLU-190. RX PubMed=14618157; DOI=10.1038/sj.embor.7400020; RA Thore S., Mauxion F., Seraphin B., Suck D.; RT "X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit RT of the mRNA deadenylase complex."; RL EMBO Rep. 4:1150-1155(2003). CC -!- FUNCTION: Acts as a probably catalytic component of the CCR4-NOT core CC complex, which in the nucleus seems to be a general transcription CC factor, and in the cytoplasm the major mRNA deadenylase involved in CC mRNA turnover. In vitro, POP2 has 3'-exoribonuclease activity with a CC preference for poly(A) RNAs, but also degrades poly(U) and poly(C) CC RNAs. Is part of a glucose-sensing system involved in growth control in CC response to glucose availability. {ECO:0000269|PubMed:11239395, CC ECO:0000269|PubMed:11410650, ECO:0000269|PubMed:14618157, CC ECO:0000269|PubMed:9463387}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Divalent metal cations. Mg(2+) is the most probable.; CC -!- SUBUNIT: Subunit of the 1.0 MDa CCR4-NOT core complex that contains CC CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the CC complex interacts with NOT1. The core complex probably is part of a CC less characterized 1.9 MDa CCR4-NOT complex. CC {ECO:0000269|PubMed:10490603, ECO:0000269|PubMed:11733989, CC ECO:0000269|PubMed:14618157, ECO:0000269|PubMed:9463387}. CC -!- INTERACTION: CC P39008; P53829: CAF40; NbExp=8; IntAct=EBI-13629, EBI-28306; CC P39008; P31384: CCR4; NbExp=9; IntAct=EBI-13629, EBI-4396; CC P39008; P25655: CDC39; NbExp=10; IntAct=EBI-13629, EBI-12139; CC P39008; P39517: DHH1; NbExp=3; IntAct=EBI-13629, EBI-158; CC P39008; P40484: MOB1; NbExp=2; IntAct=EBI-13629, EBI-11119; CC P39008; P34909: MOT2; NbExp=3; IntAct=EBI-13629, EBI-12174; CC P39008; P39016: MPT5; NbExp=4; IntAct=EBI-13629, EBI-2052996; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11239395}. Nucleus CC {ECO:0000269|PubMed:11239395}. CC -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the CAF1 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; D12807; BAA02246.1; -; Genomic_DNA. DR EMBL; D12808; BAA02247.1; -; Genomic_DNA. DR EMBL; Z71667; CAA96333.1; -; Genomic_DNA. DR EMBL; AY692792; AAT92811.1; -; Genomic_DNA. DR EMBL; M88607; AAA34832.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10593.1; -; Genomic_DNA. DR PIR; S63383; S63383. DR RefSeq; NP_014450.3; NM_001183229.3. DR PDB; 1UOC; X-ray; 2.30 A; A/B=147-433. DR PDB; 4B8A; X-ray; 2.40 A; B=151-433. DR PDB; 4B8C; X-ray; 3.41 A; A/C/E/F=146-433. DR PDBsum; 1UOC; -. DR PDBsum; 4B8A; -. DR PDBsum; 4B8C; -. DR AlphaFoldDB; P39008; -. DR SMR; P39008; -. DR BioGRID; 35877; 275. DR ComplexPortal; CPX-1800; CCR4-NOT mRNA deadenylase complex. DR DIP; DIP-1957N; -. DR IntAct; P39008; 41. DR MINT; P39008; -. DR STRING; 4932.YNR052C; -. DR iPTMnet; P39008; -. DR MaxQB; P39008; -. DR PaxDb; 4932-YNR052C; -. DR PeptideAtlas; P39008; -. DR EnsemblFungi; YNR052C_mRNA; YNR052C; YNR052C. DR GeneID; 855788; -. DR KEGG; sce:YNR052C; -. DR AGR; SGD:S000005335; -. DR SGD; S000005335; POP2. DR VEuPathDB; FungiDB:YNR052C; -. DR eggNOG; KOG0304; Eukaryota. DR GeneTree; ENSGT00390000000080; -. DR HOGENOM; CLU_027974_3_1_1; -. DR InParanoid; P39008; -. DR OMA; WQFNFLY; -. DR OrthoDB; 341493at2759; -. DR BioCyc; YEAST:G3O-33358-MONOMER; -. DR BioGRID-ORCS; 855788; 3 hits in 10 CRISPR screens. DR EvolutionaryTrace; P39008; -. DR PRO; PR:P39008; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P39008; Protein. DR GO; GO:0030015; C:CCR4-NOT core complex; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0043332; C:mating projection tip; HDA:SGD. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0000932; C:P-body; IDA:SGD. DR GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IDA:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:SGD. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:SGD. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IMP:SGD. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1. DR InterPro; IPR039637; CNOT7/CNOT8/Pop2. DR InterPro; IPR006941; RNase_CAF1. DR InterPro; IPR012337; RNaseH-like_sf. DR InterPro; IPR036397; RNaseH_sf. DR PANTHER; PTHR10797; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT; 1. DR PANTHER; PTHR10797:SF0; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 7; 1. DR Pfam; PF04857; CAF1; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Cytoplasm; Exonuclease; Hydrolase; KW Magnesium; Metal-binding; Nuclease; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; RNA-binding; Transcription; KW Transcription regulation. FT CHAIN 1..433 FT /note="Poly(A) ribonuclease POP2" FT /id="PRO_0000212849" FT REGION 78..98 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 188 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 190 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 310 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT BINDING 394 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 97 FT /note="Phosphothreonine; by YAK1" FT /evidence="ECO:0000269|PubMed:11358866" FT VARIANT 41 FT /note="K -> Q (in strain: A364A)" FT VARIANT 91 FT /note="Q -> QQQQQQQQQQQQQQQQQQ (in strain: A364A)" FT VARIANT 118..122 FT /note="Missing (in strain: A364A)" FT VARIANT 278 FT /note="L -> S (in strain: A364A)" FT VARIANT 412 FT /note="K -> M" FT MUTAGEN 97 FT /note="T->A: No cell-cycle stop in response to glucose FT deprivation." FT /evidence="ECO:0000269|PubMed:11358866" FT MUTAGEN 188 FT /note="S->A: Abolishes poly(A) RNA degradation; when FT associated with A-190." FT /evidence="ECO:0000269|PubMed:14618157" FT MUTAGEN 190 FT /note="E->A: Abolishes poly(A) RNA degradation; when FT associated with A-188." FT /evidence="ECO:0000269|PubMed:14618157" FT HELIX 155..158 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:1UOC" FT TURN 165..167 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 168..178 FT /evidence="ECO:0007829|PDB:1UOC" FT TURN 179..181 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 184..192 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 197..200 FT /evidence="ECO:0007829|PDB:4B8C" FT HELIX 205..217 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 221..230 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 242..248 FT /evidence="ECO:0007829|PDB:1UOC" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:4B8A" FT HELIX 259..267 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 272..278 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 282..290 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 292..296 FT /evidence="ECO:0007829|PDB:4B8A" FT STRAND 300..306 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 309..318 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 327..337 FT /evidence="ECO:0007829|PDB:1UOC" FT STRAND 339..343 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 344..351 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:4B8A" FT HELIX 373..379 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 386..389 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 391..408 FT /evidence="ECO:0007829|PDB:1UOC" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:1UOC" FT HELIX 419..422 FT /evidence="ECO:0007829|PDB:1UOC" SQ SEQUENCE 433 AA; 49682 MW; F3CAF97106A65933 CRC64; MQSMNVQPRV LAVGGEQFFS QRQASEQHQQ QNMGPQVYSP KVNRARMFPQ GMPVNTINGS VNQEMNNAYL LKQKNEPLLT QQQQQQQQQQ QPFNIGTPVS VASLPPGLNV LQQQQQQQQQ QQQQQQGVGL NRPLASQLPK HLTNQSMPPI FLPPPNYLFV RDVWKSNLYS EFAVIRQLVS QYNHVSISTE FVGTLARPIG TFRSKVDYHY QTMRANVDFL NPIQLGLSLS DANGNKPDNG PSTWQFNFEF DPKKEIMSTE SLELLRKSGI NFEKHENLGI DVFEFSQLLM DSGLMMDDSV TWITYHAAYD LGFLINILMN DSMPNNKEDF EWWVHQYMPN FYDLNLVYKI IQEFKNPQLQ QSSQQQQQQQ YSLTTLADEL GLPRFSIFTT TGGQSLLMLL SFCQLSKLSM HKFPNGTDFA KYQGVIYGID GDQ //