YTH1_YEAST
ID YTH1_YEAST Reviewed; 208 AA.
AC Q06102; D6W4A5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=mRNA 3'-end-processing protein YTH1;
DE AltName: Full=Yeast 30 kDa homolog 1;
GN Name=YTH1; OrderedLocusNames=YPR107C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 [4]
RP IDENTIFICATION IN THE CPF COMPLEX, AND INTERACTION WITH FIP1.
RX PubMed=9224719; DOI=10.1101/gad.11.13.1703;
RA Barabino S.M.L., Huebner W., Jenny A., Minvielle-Sebastia L., Keller W.;
RT "The 30-kD subunit of mammalian cleavage and polyadenylation specificity
RT factor and its yeast homolog are RNA-binding zinc finger proteins.";
RL Genes Dev. 11:1703-1716(1997).
RN [5]
RP RNA-BINDING, AND MUTAGENESIS OF CYS-67; TRP-70; CYS-75; ASP-79; CYS-81 AND
RP HIS-142.
RX PubMed=10899131; DOI=10.1093/emboj/19.14.3778;
RA Barabino S.M., Ohnacker M., Keller W.;
RT "Distinct roles of two Yth1p domains in 3'-end cleavage and polyadenylation
RT of yeast pre-mRNAs.";
RL EMBO J. 19:3778-3787(2000).
RN [6]
RP INTERACTION WITH FIP1.
RX PubMed=11238938; DOI=10.1128/mcb.21.6.2026-2037.2001;
RA Helmling S., Zhelkovsky A., Moore C.L.;
RT "Fip1 regulates the activity of Poly(A) polymerase through multiple
RT interactions.";
RL Mol. Cell. Biol. 21:2026-2037(2001).
RN [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, AND INTERACTION WITH FIP1 AND YSH1.
RX PubMed=12626716; DOI=10.1093/nar/gkg265;
RA Tacahashi Y., Helmling S., Moore C.L.;
RT "Functional dissection of the zinc finger and flanking domains of the Yth1
RT cleavage/polyadenylation factor.";
RL Nucleic Acids Res. 31:1744-1752(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.
CC {ECO:0000269|PubMed:12626716}.
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 FIP1 and YSH1. {ECO:0000269|PubMed:11238938,
CC ECO:0000269|PubMed:12626716, ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:9224719}.
CC -!- INTERACTION:
CC Q06102; P45976: FIP1; NbExp=5; IntAct=EBI-38049, EBI-6940;
CC Q06102; Q06224: YSH1; NbExp=4; IntAct=EBI-38049, EBI-38345;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3690 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CPSF4/YTH1 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; U32445; AAB68077.1; -; Genomic_DNA.
DR EMBL; AY558061; AAS56387.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11521.1; -; Genomic_DNA.
DR PIR; S59772; S59772.
DR RefSeq; NP_015432.1; NM_001184204.1.
DR PDB; 6EOJ; EM; 3.55 A; B=2-208.
DR PDBsum; 6EOJ; -.
DR AlphaFoldDB; Q06102; -.
DR SMR; Q06102; -.
DR BioGRID; 36273; 422.
DR ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR DIP; DIP-2028N; -.
DR IntAct; Q06102; 19.
DR MINT; Q06102; -.
DR STRING; 4932.YPR107C; -.
DR MaxQB; Q06102; -.
DR PaxDb; Q06102; -.
DR PRIDE; Q06102; -.
DR EnsemblFungi; YPR107C_mRNA; YPR107C; YPR107C.
DR GeneID; 856222; -.
DR KEGG; sce:YPR107C; -.
DR SGD; S000006311; YTH1.
DR VEuPathDB; FungiDB:YPR107C; -.
DR eggNOG; KOG1040; Eukaryota.
DR GeneTree; ENSGT00940000167819; -.
DR HOGENOM; CLU_024513_1_2_1; -.
DR OMA; CKYGAHP; -.
DR BioCyc; YEAST:G3O-34247-MON; -.
DR Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
DR PRO; PR:Q06102; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06102; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; IC:ComplexPortal.
DR InterPro; IPR045348; CPSF4/Yth1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR23102; PTHR23102; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; mRNA processing; Nucleus; Reference proteome;
KW Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..208
FT /note="mRNA 3'-end-processing protein YTH1"
FT /id="PRO_0000213910"
FT ZN_FING 28..59
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 61..88
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 89..117
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 118..145
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 147..170
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT MUTAGEN 67
FT /note="C->S: Lethal."
FT /evidence="ECO:0000269|PubMed:10899131"
FT MUTAGEN 70
FT /note="W->A: Temperature- and formamide-sensitive;
FT abolishes cleavage and polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:10899131"
FT MUTAGEN 75
FT /note="C->S: Lethal."
FT /evidence="ECO:0000269|PubMed:10899131"
FT MUTAGEN 79
FT /note="D->A: Temperature- and formamide-sensitive; impaired
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:10899131"
FT MUTAGEN 81
FT /note="C->S: Lethal."
FT /evidence="ECO:0000269|PubMed:10899131"
FT MUTAGEN 142
FT /note="H->N: Temperature- and formamide-sensitive; impaired
FT polyadenylation activity."
FT /evidence="ECO:0000269|PubMed:10899131"
SQ SEQUENCE 208 AA; 24553 MW; 79C5993AE4E670EA CRC64;
MSLIHPDTAK YPFKFEPFLR QEYSFSLDPD RPICEFYNSR EGPKSCPRGP LCPKKHVLPI
FQNKIVCRHW LRGLCKKNDQ CEYLHEYNLR KMPECVFFSK NGYCTQSPDC QYLHIDPASK
IPKCENYEMG FCPLGSSCPR RHIKKVFCQR YMTGFCPLGK DECDMEHPQF IIPDEGSKLR
IKRDDEINTR KMDEEKERRL NAIINGEV
