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mRNA 3'-end-processing protein YTH1 (Yeast 30 kDa homolog 1)

 YTH1_YEAST              Reviewed;         208 AA.
Q06102; D6W4A5;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 143.
RecName: Full=mRNA 3'-end-processing protein YTH1;
AltName: Full=Yeast 30 kDa homolog 1;
Name=YTH1; OrderedLocusNames=YPR107C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
IDENTIFICATION IN THE CPF COMPLEX, AND INTERACTION WITH FIP1.
PubMed=9224719; DOI=10.1101/gad.11.13.1703;
Barabino S.M.L., Huebner W., Jenny A., Minvielle-Sebastia L.,
Keller W.;
"The 30-kD subunit of mammalian cleavage and polyadenylation
specificity factor and its yeast homolog are RNA-binding zinc finger
proteins.";
Genes Dev. 11:1703-1716(1997).
[5]
RNA-BINDING, AND MUTAGENESIS OF CYS-67; TRP-70; CYS-75; ASP-79; CYS-81
AND HIS-142.
PubMed=10899131; DOI=10.1093/emboj/19.14.3778;
Barabino S.M., Ohnacker M., Keller W.;
"Distinct roles of two Yth1p domains in 3'-end cleavage and
polyadenylation of yeast pre-mRNAs.";
EMBO J. 19:3778-3787(2000).
[6]
INTERACTION WITH FIP1.
PubMed=11238938; DOI=10.1128/MCB.21.6.2026-2037.2001;
Helmling S., Zhelkovsky A., Moore C.L.;
"Fip1 regulates the activity of Poly(A) polymerase through multiple
interactions.";
Mol. Cell. Biol. 21:2026-2037(2001).
[7]
IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12819204; DOI=10.1074/jbc.M304454200;
Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V.,
Hughes T., Buratowski S., Moore C.L., Greenblatt J.;
"Organization and function of APT, a subcomplex of the yeast cleavage
and polyadenylation factor involved in the formation of mRNA and small
nucleolar RNA 3'-ends.";
J. Biol. Chem. 278:33000-33010(2003).
[8]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[9]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[10]
FUNCTION, AND INTERACTION WITH FIP1 AND YSH1.
PubMed=12626716; DOI=10.1093/nar/gkg265;
Tacahashi Y., Helmling S., Moore C.L.;
"Functional dissection of the zinc finger and flanking domains of the
Yth1 cleavage/polyadenylation factor.";
Nucleic Acids Res. 31:1744-1752(2003).
-!- FUNCTION: RNA-binding component of the cleavage and
polyadenylation factor (CPF) complex, which plays a key role in
polyadenylation-dependent pre-mRNA 3'-end formation and cooperates
with cleavage factors including the CFIA complex and NAB4/CFIB.
{ECO:0000269|PubMed:12626716}.
-!- SUBUNIT: Component of the cleavage and polyadenylation factor
(CPF) complex, which is composed of at least PTI1, SYC1, SSU72,
GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1,
CFT1/YHH1, FIP1 and PAP1. Interacts with FIP1 and YSH1.
{ECO:0000269|PubMed:11238938, ECO:0000269|PubMed:12626716,
ECO:0000269|PubMed:12819204, ECO:0000269|PubMed:9224719}.
-!- INTERACTION:
Q06632:CFT1; NbExp=5; IntAct=EBI-38049, EBI-32872;
Q12102:CFT2; NbExp=6; IntAct=EBI-38049, EBI-31412;
P45976:FIP1; NbExp=9; IntAct=EBI-38049, EBI-6940;
Q6UN15:FIP1L1 (xeno); NbExp=3; IntAct=EBI-38049, EBI-1021914;
P35728:MPE1; NbExp=5; IntAct=EBI-38049, EBI-26710;
P29468:PAP1; NbExp=6; IntAct=EBI-38049, EBI-12917;
P42841:PFS2; NbExp=4; IntAct=EBI-38049, EBI-28378;
Q01329:PTA1; NbExp=5; IntAct=EBI-38049, EBI-14145;
P39927:PTI1; NbExp=3; IntAct=EBI-38049, EBI-23382;
P42073:REF2; NbExp=4; IntAct=EBI-38049, EBI-14915;
P10592:SSA2; NbExp=3; IntAct=EBI-38049, EBI-8603;
P36104:SWD2; NbExp=4; IntAct=EBI-38049, EBI-26608;
Q06224:YSH1; NbExp=7; IntAct=EBI-38049, EBI-38345;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204,
ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 3690 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the CPSF4/YTH1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U32445; AAB68077.1; -; Genomic_DNA.
EMBL; AY558061; AAS56387.1; -; Genomic_DNA.
EMBL; BK006949; DAA11521.1; -; Genomic_DNA.
PIR; S59772; S59772.
RefSeq; NP_015432.1; NM_001184204.1.
PDB; 6EOJ; EM; 3.55 A; B=2-208.
PDBsum; 6EOJ; -.
ProteinModelPortal; Q06102; -.
SMR; Q06102; -.
BioGrid; 36273; 420.
DIP; DIP-2028N; -.
IntAct; Q06102; 25.
MINT; Q06102; -.
STRING; 4932.YPR107C; -.
MaxQB; Q06102; -.
PaxDb; Q06102; -.
PRIDE; Q06102; -.
EnsemblFungi; YPR107C; YPR107C; YPR107C.
GeneID; 856222; -.
KEGG; sce:YPR107C; -.
EuPathDB; FungiDB:YPR107C; -.
SGD; S000006311; YTH1.
GeneTree; ENSGT00390000009627; -.
HOGENOM; HOG000212457; -.
KO; K14404; -.
OMA; GLCKKND; -.
OrthoDB; EOG092C59NU; -.
BioCyc; YEAST:G3O-34247-MONOMER; -.
Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
PRO; PR:Q06102; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:SGD.
GO; GO:0006378; P:mRNA polyadenylation; IDA:SGD.
GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:SGD.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
SMART; SM00356; ZnF_C3H1; 5.
SUPFAM; SSF90229; SSF90229; 2.
PROSITE; PS50103; ZF_C3H1; 5.
1: Evidence at protein level;
3D-structure; Complete proteome; Metal-binding; mRNA processing;
Nucleus; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
CHAIN 1 208 mRNA 3'-end-processing protein YTH1.
/FTId=PRO_0000213910.
ZN_FING 28 59 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 61 88 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 89 117 C3H1-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 118 145 C3H1-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 147 170 C3H1-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
MUTAGEN 67 67 C->S: Lethal.
{ECO:0000269|PubMed:10899131}.
MUTAGEN 70 70 W->A: Temperature- and formamide-
sensitive; abolishes cleavage and
polyadenylation activity.
{ECO:0000269|PubMed:10899131}.
MUTAGEN 75 75 C->S: Lethal.
{ECO:0000269|PubMed:10899131}.
MUTAGEN 79 79 D->A: Temperature- and formamide-
sensitive; impaired polyadenylation
activity. {ECO:0000269|PubMed:10899131}.
MUTAGEN 81 81 C->S: Lethal.
{ECO:0000269|PubMed:10899131}.
MUTAGEN 142 142 H->N: Temperature- and formamide-
sensitive; impaired polyadenylation
activity. {ECO:0000269|PubMed:10899131}.
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


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