CFT2_YEAST
ID CFT2_YEAST Reviewed; 859 AA.
AC Q12102; D6VYB3; Q7LGW6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cleavage factor two protein 2;
DE AltName: Full=105 kDa protein associated with polyadenylation factor I;
GN Name=CFT2; Synonyms=YDH1; OrderedLocusNames=YLR115W; ORFNames=L2946;
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 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 RNA-BINDING.
RX PubMed=9099738; DOI=10.1074/jbc.272.16.10831;
RA Zhao J., Kessler M.M., Moore C.L.;
RT "Cleavage factor II of Saccharomyces cerevisiae contains homologues to
RT subunits of the mammalian Cleavage/ polyadenylation specificity factor and
RT exhibits sequence-specific, ATP-dependent interaction with precursor RNA.";
RL J. Biol. Chem. 272:10831-10838(1997).
RN [5]
RP RNA-BINDING, AND FUNCTION.
RX PubMed=11406596; DOI=10.1093/emboj/20.12.3197;
RA Dichtl B., Keller W.;
RT "Recognition of polyadenylation sites in yeast pre-mRNAs by cleavage and
RT polyadenylation factor.";
RL EMBO J. 20:3197-3209(2001).
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).
RN [9]
RP FUNCTION, AND INTERACTION WITH RPB1 AND PCF11.
RX PubMed=12853609; DOI=10.1093/nar/gkg478;
RA Kyburz A., Sadowski M., Dichtl B., Keller W.;
RT "The role of the yeast cleavage and polyadenylation factor subunit
RT Ydh1p/Cft2p in pre-mRNA 3'-end formation.";
RL Nucleic Acids Res. 31:3936-3945(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-717, AND ABSENCE OF ENDONUCLEASE
RP ACTIVITY.
RX PubMed=17128255; DOI=10.1038/nature05363;
RA Mandel C.R., Kaneko S., Zhang H., Gebauer D., Vethantham V., Manley J.L.,
RA Tong L.;
RT "Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing
RT endonuclease.";
RL Nature 444:953-956(2006).
CC -!- FUNCTION: RNA-binding component of the cleavage and polyadenylation
CC factor (CPF) complex, which plays a key role in polyadenylation-
CC dependent pre-mRNA 3'-end formation and cooperates with cleavage
CC factors including the CFIA complex and NAB4/CFIB. May be involved in
CC poly(A)-site recognition. May be involved in the association of the
CC CPF, CPFIA and RNA polymerase II complexes.
CC {ECO:0000269|PubMed:11406596, ECO:0000269|PubMed:12853609}.
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 the CTD domain of RPB1/RNA polymerase II; the
CC interaction is enhanced upon phosphorylation of the RPB1 CTD domain.
CC Interacts with PCF11. {ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:12853609}.
CC -!- INTERACTION:
CC Q12102; Q01329: PTA1; NbExp=5; IntAct=EBI-31412, EBI-14145;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X89514; CAA61694.1; -; Genomic_DNA.
DR EMBL; Z73287; CAA97682.1; -; Genomic_DNA.
DR EMBL; Z73288; CAA97684.1; -; Genomic_DNA.
DR EMBL; U53878; AAB67560.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82376.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09429.1; -; Genomic_DNA.
DR PIR; S64952; S64952.
DR RefSeq; NP_013216.1; NM_001182002.1.
DR PDB; 2I7X; X-ray; 2.50 A; A=1-717.
DR PDBsum; 2I7X; -.
DR AlphaFoldDB; Q12102; -.
DR SMR; Q12102; -.
DR BioGRID; 31387; 530.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR DIP; DIP-2468N; -.
DR IntAct; Q12102; 24.
DR MINT; Q12102; -.
DR STRING; 4932.YLR115W; -.
DR iPTMnet; Q12102; -.
DR MaxQB; Q12102; -.
DR PaxDb; Q12102; -.
DR PRIDE; Q12102; -.
DR EnsemblFungi; YLR115W_mRNA; YLR115W; YLR115W.
DR GeneID; 850806; -.
DR KEGG; sce:YLR115W; -.
DR SGD; S000004105; CFT2.
DR VEuPathDB; FungiDB:YLR115W; -.
DR eggNOG; KOG1135; Eukaryota.
DR GeneTree; ENSGT00910000144260; -.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; Q12102; -.
DR OMA; MELVENC; -.
DR BioCyc; YEAST:G3O-32260-MON; -.
DR Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
DR EvolutionaryTrace; Q12102; -.
DR PRO; PR:Q12102; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12102; 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:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0006379; P:mRNA cleavage; IDA:SGD.
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 CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR DisProt; DP02480; -.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR45922; PTHR45922; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SUPFAM; SSF56281; SSF56281; 2.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; Nucleus; Reference proteome.
FT CHAIN 1..859
FT /note="Cleavage factor two protein 2"
FT /id="PRO_0000076204"
FT REGION 560..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2I7X"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2I7X"
FT TURN 143..148
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 223..237
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:2I7X"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:2I7X"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 288..294
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:2I7X"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 338..344
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 375..385
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 405..417
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 631..633
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 640..651
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 653..657
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 666..672
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 679..683
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:2I7X"
FT HELIX 692..700
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 704..707
FT /evidence="ECO:0007829|PDB:2I7X"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:2I7X"
SQ SEQUENCE 859 AA; 96254 MW; 44997871ECE6225F CRC64;
MTYKYNCCDD GSGTTVGSVV RFDNVTLLID PGWNPSKVSY EQCIKYWEKV IPEIDVIILS
QPTIECLGAH SLLYYNFTSH FISRIQVYAT LPVINLGRVS TIDSYASAGV IGPYDTNKLD
LEDIEISFDH IVPLKYSQLV DLRSRYDGLT LLAYNAGVCP GGSIWCISTY SEKLVYAKRW
NHTRDNILNA ASILDATGKP LSTLMRPSAI ITTLDRFGSS QPFKKRSKIF KDTLKKGLSS
DGSVIIPVDM SGKFLDLFTQ VHELLFESTK INAHTQVPVL ILSYARGRTL TYAKSMLEWL
SPSLLKTWEN RNNTSPFEIG SRIKIIAPNE LSKYPGSKIC FVSEVGALIN EVIIKVGNSE
KTTLILTKPS FECASSLDKI LEIVEQDERN WKTFPEDGKS FLCDNYISID TIKEEPLSKE
ETEAFKVQLK EKKRDRNKKI LLVKRESKKL ANGNAIIDDT NGERAMRNQD ILVENVNGVP
PIDHIMGGDE DDDEEEENDN LLNLLKDNSE KSAAKKNTEV PVDIIIQPSA ASKHKMFPFN
PAKIKKDDYG TVVDFTMFLP DDSDNVNQNS RKRPLKDGAK TTSPVNEEDN KNEEEDGYNM
SDPISKRSKH RASRYSGFSG TGEAENFDNL DYLKIDKTLS KRTISTVNVQ LKCSVVILNL
QSLVDQRSAS IIWPSLKSRK IVLSAPKQIQ NEEITAKLIK KNIEVVNMPL NKIVEFSTTI
KTLDISIDSN LDNLLKWQRI SDSYTVATVV GRLVKESLPQ VNNHQKTASR SKLVLKPLHG
SSRSHKTGAL SIGDVRLAQL KKLLTEKNYI AEFKGEGTLV INEKVAVRKI NDAETIIDGT
PSELFDTVKK LVTDMLAKI
