PFS2_YEAST
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 03-AUG-2022, entry version 173.
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}.
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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 PDBsum; 6EOJ; -.
DR AlphaFoldDB; P42841; -.
DR SMR; P42841; -.
DR BioGRID; 35522; 38.
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; P42841; -.
DR PRIDE; P42841; -.
DR EnsemblFungi; YNL317W_mRNA; YNL317W; YNL317W.
DR GeneID; 855399; -.
DR KEGG; sce:YNL317W; -.
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 BioCyc; YEAST:G3O-33303-MON; -.
DR Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
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; IC:ComplexPortal.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:SGD.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:SGD.
DR GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR045245; Pfs2-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR22836; PTHR22836; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 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"
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
