CFT1_YEAST
ID CFT1_YEAST Reviewed; 1357 AA.
AC Q06632; D6VST0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein CFT1;
DE AltName: Full=Cleavage factor two protein 1;
GN Name=CFT1; Synonyms=YHH1; OrderedLocusNames=YDR301W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=8929410; DOI=10.1126/science.274.5292.1517;
RA Stumpf G., Domdey H.;
RT "Dependence of yeast pre-mRNA 3'-end processing on CFT1: a sequence homolog
RT of the mammalian AAUAAA binding factor.";
RL Science 274:1517-1520(1996).
RN [4]
RP FUNCTION, RNA-BINDING, AND INTERACTION WITH RPB1.
RX PubMed=12145212; DOI=10.1093/emboj/cdf390;
RA Dichtl B., Blank D., Sadowski M., Hubner W., Weiser S., Keller W.;
RT "Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II
RT transcription termination.";
RL EMBO J. 21:4125-4135(2002).
RN [5]
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 [6]
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 [7]
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: 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. Involved in poly(A)
CC site recognition. May be involved in coupling transcription termination
CC and mRNA 3'-end formation. {ECO:0000269|PubMed:12145212,
CC ECO:0000269|PubMed:8929410}.
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 phosphorylated CTD domain of RPB1/RNA
CC polymerase II. {ECO:0000269|PubMed:12145212,
CC ECO:0000269|PubMed:12819204}.
CC -!- INTERACTION:
CC Q06632; P35728: MPE1; NbExp=5; IntAct=EBI-32872, EBI-26710;
CC Q06632; P29468: PAP1; NbExp=5; IntAct=EBI-32872, EBI-12917;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CFT1 family. {ECO:0000305}.
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DR EMBL; U28374; AAB64737.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12140.1; -; Genomic_DNA.
DR PIR; S61187; S61187.
DR RefSeq; NP_010587.1; NM_001180609.1.
DR PDB; 6EOJ; EM; 3.55 A; A=1-1357.
DR PDBsum; 6EOJ; -.
DR AlphaFoldDB; Q06632; -.
DR SMR; Q06632; -.
DR BioGRID; 32353; 108.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR DIP; DIP-2467N; -.
DR IntAct; Q06632; 34.
DR MINT; Q06632; -.
DR STRING; 4932.YDR301W; -.
DR iPTMnet; Q06632; -.
DR MaxQB; Q06632; -.
DR PaxDb; Q06632; -.
DR PRIDE; Q06632; -.
DR EnsemblFungi; YDR301W_mRNA; YDR301W; YDR301W.
DR GeneID; 851895; -.
DR KEGG; sce:YDR301W; -.
DR SGD; S000002709; CFT1.
DR VEuPathDB; FungiDB:YDR301W; -.
DR eggNOG; KOG1896; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_002414_0_0_1; -.
DR InParanoid; Q06632; -.
DR OMA; PMTKFKL; -.
DR BioCyc; YEAST:G3O-29861-MON; -.
DR Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q06632; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06632; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; 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:0006369; P:termination of RNA polymerase II transcription; IMP: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; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..1357
FT /note="Protein CFT1"
FT /id="PRO_0000076203"
FT REGION 445..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1357 AA; 153405 MW; BC50D3770E9E758E CRC64;
MNVYDDVLDA TVVSHSLATH FTTSDYEELL VVRTNILSVY RPTRDGKLYL TDEFKFHGLI
TDIGLIPQKD SPLSCLLLCT GVAKISILKF NTLTNSIDTL SLHYYEGKFK GKSLVELAKI
STLRMDPGSS CALLFNNDII AFLPFHVNKN DDDEEEEDED ENIDDSELIH SMNQKSQGTN
TFNKRKRTKL GDKFTAPSVV LVASELYEGA KNIIDIQFLK NFTKPTIALL YQPKLVWAGN
TTISKLPTQY VILTLNIQPA ESATKIESTT IAFVKELPWD LHTIVPVSNG AIIVGTNELA
FLDNTGVLQS TVLLNSFADK ELQKTKIINN SSLEIMFREK NTTSIWIPSS KSKNGGSNND
ETLLLMDLKS NIYYIQMEAE GRLLIKFDIF KLPIVNDLLK ENSNPKCITR LNATNSNKNM
DLFIGFGSGN ALVLRLNNLK STIETREAHN PSSGTNSLMD INDDDDEEMD DLYADEAPEN
GLTTNDSKGT VETVQPFDIE LLSSLRNVGP ITSLTVGKVS SIDDVVKGLP NPNKNEYSLV
ATSGNGSGSH LTVIQTSVQP EIELALKFIS ITQIWNLKIK GRDRYLITTD STKSRSDIYE
SDNNFKLHKG GRLRRDATTV YISMFGEEKR IIQVTTNHLY LYDTHFRRLT TIKFDYEVIH
VSVMDPYILV TVSRGDIKIF ELEEKNKRKL LKVDLPEILN EMVITSGLIL KSNMCNEFLI
GLSKSQEEQL LFTFVTADNQ IIFFTKDHND RIFQLNGVDQ LNESLYISTY QLGDEIVPDP
SIKQVMINKL GHDNKEEYLT ILTFGGEIYQ YRKLPQRRSR FYRNVTRNDL AITGAPDNAY
AKGVSSIERI MHYFPDYNGY SVIFVTGSVP YILIKEDDST PKIFKFGNIP LVSVTPWSER
SVMCVDDIKN ARVYTLTTDN MYYGNKLPLK QIKISNVLDD YKTLQKLVYH ERAQLFLVSY
CKRVPYEALG EDGEKVIGYD ENVPHAEGFQ SGILLINPKS WKVIDKIDFP KNSVVNEMRS
SMIQINSKTK RKREYIIAGV ANATTEDTPP TGAFHIYDVI EVVPEPGKPD TNYKLKEIFQ
EEVSGTVSTV CEVSGRFMIS QSQKVLVRDI QEDNSVIPVA FLDIPVFVTD SKSFGNLLII
GDAMQGFQFI GFDAEPYRMI SLGRSMSKFQ TMSLEFLVNG GDMYFAATDA DRNVHVLKYA
PDEPNSLSGQ RLVHCSSFTL HSTNSCMMLL PRNEEFGSPQ VPSFQNVGGQ VDGSVFKIVP
LSEEKYRRLY VIQQQIIDRE LQLGGLNPRM ERLANDFYQM GHSMRPMLDF NVIRRFCGLA
IDRRKSIAQK AGRHAHFEAW RDIINIEFSM RSLCQGK
