ID PFS2_YEAST Reviewed; 465 AA. AC P42841; D6W0M8; Q6B1M2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 180. DE RecName: Full=Polyadenylation factor subunit 2; GN Name=PFS2; OrderedLocusNames=YNL317W; ORFNames=N0348; 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=S288c / FY1676; RX PubMed=7502583; DOI=10.1002/yea.320111109; RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.; RT "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV RT identifies six known genes, a new member of the hexose transporter family RT and ten new open reading frames."; RL Yeast 11:1077-1085(1995). 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 PROTEIN SEQUENCE OF 83-91, FUNCTION, IDENTIFICATION IN THE CPF COMPLEX, AND RP INTERACTION WITH YSH1; FIP1 AND RNA14. RX PubMed=10619842; DOI=10.1093/emboj/19.1.37; RA Ohnacker M., Barabino S.M.L., Preker P.J., Keller W.; RT "The WD-repeat protein pfs2p bridges two essential factors within the yeast RT pre-mRNA 3'-end-processing complex."; RL EMBO J. 19:37-47(2000). RN [6] RP IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=12819204; DOI=10.1074/jbc.m304454200; RA Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., RA Buratowski S., Moore C.L., Greenblatt J.; RT "Organization and function of APT, a subcomplex of the yeast cleavage and RT polyadenylation factor involved in the formation of mRNA and small RT nucleolar RNA 3'-ends."; RL J. Biol. Chem. 278:33000-33010(2003). RN [7] 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 [8] 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). CC -!- FUNCTION: Integral and essential component of the cleavage and CC polyadenylation factor (CPF) complex, which plays a key role in CC polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with CC cleavage factors including the CFIA complex and NAB4/CFIB. May bridge CC the CPF and CFIA complexes. {ECO:0000269|PubMed:10619842}. CC -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF) CC complex, which is composed of at least PTI1, SYC1, SSU72, GLC7, MPE1, CC REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and CC PAP1. Interacts with YSH1/BRR5, FIP1 and RNA14. CC {ECO:0000269|PubMed:10619842, ECO:0000269|PubMed:12819204}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204, CC ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 7810 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z46259; CAA86378.1; -; Genomic_DNA. DR EMBL; Z71593; CAA96247.1; -; Genomic_DNA. DR EMBL; AY693058; AAT93077.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10244.1; -; Genomic_DNA. DR PIR; S51295; S51295. DR RefSeq; NP_014082.1; NM_001183155.1. DR PDB; 6EOJ; EM; 3.55 A; D=1-465. DR PDB; 7ZGP; EM; 2.70 A; D=1-465. DR PDB; 7ZGQ; EM; 2.80 A; D=1-465. DR PDB; 7ZGR; EM; 2.60 A; D=1-465. DR PDBsum; 6EOJ; -. DR PDBsum; 7ZGP; -. DR PDBsum; 7ZGQ; -. DR PDBsum; 7ZGR; -. DR AlphaFoldDB; P42841; -. DR EMDB; EMD-3908; -. DR SMR; P42841; -. DR BioGRID; 35522; 44. DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex. DR DIP; DIP-5816N; -. DR IntAct; P42841; 33. DR MINT; P42841; -. DR STRING; 4932.YNL317W; -. DR MaxQB; P42841; -. DR PaxDb; 4932-YNL317W; -. DR PeptideAtlas; P42841; -. DR EnsemblFungi; YNL317W_mRNA; YNL317W; YNL317W. DR GeneID; 855399; -. DR KEGG; sce:YNL317W; -. DR AGR; SGD:S000005261; -. DR SGD; S000005261; PFS2. DR VEuPathDB; FungiDB:YNL317W; -. DR eggNOG; KOG0284; Eukaryota. DR GeneTree; ENSGT00730000111130; -. DR HOGENOM; CLU_000288_77_0_1; -. DR InParanoid; P42841; -. DR OMA; HHWDVKS; -. DR OrthoDB; 5487329at2759; -. DR BioCyc; YEAST:G3O-33303-MONOMER; -. DR Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs. DR BioGRID-ORCS; 855399; 6 hits in 10 CRISPR screens. DR PRO; PR:P42841; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P42841; Protein. DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0006378; P:mRNA polyadenylation; IDA:ComplexPortal. DR GO; GO:0006397; P:mRNA processing; IDA:SGD. DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; NAS:ComplexPortal. DR CDD; cd00200; WD40; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3. DR InterPro; IPR045245; Pfs2-like. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR22836:SF0; PRE-MRNA 3' END PROCESSING PROTEIN WDR33; 1. DR PANTHER; PTHR22836; WD40 REPEAT PROTEIN; 1. DR Pfam; PF00400; WD40; 4. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; mRNA processing; Nucleus; KW Reference proteome; Repeat; WD repeat. FT CHAIN 1..465 FT /note="Polyadenylation factor subunit 2" FT /id="PRO_0000051122" FT REPEAT 133..163 FT /note="WD 1" FT REPEAT 175..205 FT /note="WD 2" FT REPEAT 217..247 FT /note="WD 3" FT REPEAT 259..290 FT /note="WD 4" FT REPEAT 348..378 FT /note="WD 5" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 417..465 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 451..465 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 2 FT /note="D -> V (in Ref. 4; AAT93077)" FT /evidence="ECO:0000305" FT HELIX 36..47 FT /evidence="ECO:0007829|PDB:7ZGR" FT HELIX 59..64 FT /evidence="ECO:0007829|PDB:7ZGR" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:7ZGR" FT HELIX 73..79 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 83..88 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 105..111 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:7ZGP" FT STRAND 180..185 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 187..205 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 206..208 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 222..227 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 234..238 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 243..246 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 253..257 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 264..269 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 271..273 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 276..281 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 282..284 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 285..290 FT /evidence="ECO:0007829|PDB:7ZGR" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:7ZGP" FT STRAND 296..302 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 307..312 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 319..324 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 327..333 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 334..336 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 337..340 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 342..345 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 348..351 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 353..358 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 362..369 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 374..378 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 385..389 FT /evidence="ECO:0007829|PDB:7ZGR" FT TURN 391..393 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 399..402 FT /evidence="ECO:0007829|PDB:7ZGP" FT HELIX 403..407 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 409..412 FT /evidence="ECO:0007829|PDB:7ZGR" FT STRAND 417..419 FT /evidence="ECO:0007829|PDB:7ZGR" SQ SEQUENCE 465 AA; 53143 MW; 1D5A2C00F5F67104 CRC64; MDGHNQNQYQ NQNQIQQSQQ PPLKKYVTQR RSVDVSSPYI NLYYNRRHGL PNLVVEPETS YTIDIMPPNA YRGRDRVINL PSKFTHLSSN KVKHVIPAIQ WTPEGRRLVV ATYSGEFSLW NASSFTFETL MQAHDSAVTT MKYSHDSDWM ISGDADGMIK IWQPNFSMVK EIDAAHTESI RDMAFSSNDS KFVTCSDDNI LKIWNFSNGK QERVLSGHHW DVKSCDWHPE MGLIASASKD NLVKLWDPRS GNCISSILKF KHTVLKTRFQ PTKGNLLMAI SKDKSCRVFD IRYSMKELMC VRDETDYMTL EWHPINESMF TLACYDGSLK HFDLLQNLNE PILTIPYAHD KCITSLSYNP VGHIFATAAK DRTIRFWTRA RPIDPNAYDD PTYNNKKING WFFGINNDIN AVREKSEFGA APPPPATLEP HALPNMNGFI NKKPRQEIPG IDSNIKSSTL PGLSI //