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mRNA 3'-end-processing protein RNA14

 RNA14_YEAST             Reviewed;         677 AA.
P25298; D6VZN5;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
28-MAR-2018, entry version 150.
RecName: Full=mRNA 3'-end-processing protein RNA14;
Name=RNA14; OrderedLocusNames=YMR061W; ORFNames=YM9796.14;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 28383 / FL100 / VTT C-80102;
PubMed=1674817; DOI=10.1128/MCB.11.6.3075;
Minvielle-Sebastia L., Winsor B., Bonneaud N., Lacroute F.;
"Mutations in the yeast RNA14 and RNA15 genes result in an abnormal
mRNA decay rate; sequence analysis reveals an RNA-binding domain in
the RNA15 protein.";
Mol. Cell. Biol. 11:3075-3087(1991).
[2]
SEQUENCE REVISION.
Bonneaud N.;
Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[4]
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).
[5]
FUNCTION.
PubMed=7992054; DOI=10.1126/science.7992054;
Minvielle-Sebastia L., Preker P.J., Keller W.;
"RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end
processing factor.";
Science 266:1702-1705(1994).
[6]
COMPOSITION OF THE CFIA COMPLEX.
PubMed=8900210; DOI=10.1074/jbc.271.43.27167;
Kessler M.M., Zhao J., Moore C.L.;
"Purification of the Saccharomyces cerevisiae cleavage/polyadenylation
factor I. Separation into two components that are required for both
cleavage and polyadenylation of mRNA 3' ends.";
J. Biol. Chem. 271:27167-27175(1996).
[7]
IDENTIFICATION IN THE CFIA COMPLEX.
PubMed=9223284; DOI=10.1073/pnas.94.15.7897;
Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y.,
Keller W.;
"The major yeast poly(A)-binding protein is associated with cleavage
factor IA and functions in premessenger RNA 3'-end formation.";
Proc. Natl. Acad. Sci. U.S.A. 94:7897-7902(1997).
[8]
INTERACTION WITH FIP1; PFS2 AND YSH1.
PubMed=10619842; DOI=10.1093/emboj/19.1.37;
Ohnacker M., Barabino S.M.L., Preker P.J., Keller W.;
"The WD-repeat protein pfs2p bridges two essential factors within the
yeast pre-mRNA 3'-end-processing complex.";
EMBO J. 19:37-47(2000).
[9]
FUNCTION OF THE CFIA COMPLEX.
PubMed=11344258; DOI=10.1073/pnas.101046598;
Gross S., Moore C.;
"Five subunits are required for reconstitution of the cleavage and
polyadenylation activities of Saccharomyces cerevisiae cleavage factor
I.";
Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001).
[10]
INTERACTION WITH RBP1.
PubMed=12727883; DOI=10.1093/emboj/cdg200;
Sadowski M., Dichtl B., Huebner W., Keller W.;
"Independent functions of yeast Pcf11p in pre-mRNA 3' end processing
and in transcription termination.";
EMBO J. 22:2167-2177(2003).
[11]
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).
-!- FUNCTION: Component of the cleavage factor IA (CFIA) complex,
which is involved in the endonucleolytic cleavage during
polyadenylation-dependent pre-mRNA 3'-end formation and cooperates
with the cleavage factor NAB4/CFIB and the cleavage and
polyadenylation factor (CPF) complex.
{ECO:0000269|PubMed:11344258, ECO:0000269|PubMed:7992054}.
-!- SUBUNIT: Component of the CFIA complex, which is composed of
RNA14, RNA15, PCF11 and CLP1. Interacts with FIP1, PFS2, YSH1 and
probably also with RNA15. Probably interacts with the
phosphorylated CTD domain of RPB1/RNA polymerase II.
{ECO:0000269|PubMed:10619842, ECO:0000269|PubMed:12727883,
ECO:0000269|PubMed:9223284}.
-!- INTERACTION:
Q99383:HRP1; NbExp=2; IntAct=EBI-15632, EBI-11783;
P39081:PCF11; NbExp=10; IntAct=EBI-15632, EBI-12980;
P25299:RNA15; NbExp=12; IntAct=EBI-15632, EBI-15640;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleus and/or
cytoplasm.
-!- MISCELLANEOUS: Present with 5350 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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EMBL; M73461; AAA21300.1; -; Genomic_DNA.
EMBL; Z49703; CAA89771.1; -; Genomic_DNA.
EMBL; BK006946; DAA09959.1; -; Genomic_DNA.
PIR; S54561; S54561.
RefSeq; NP_013777.1; NM_001182559.1.
PDB; 2L9B; NMR; -; B=626-677.
PDBsum; 2L9B; -.
ProteinModelPortal; P25298; -.
SMR; P25298; -.
BioGrid; 35236; 241.
DIP; DIP-1488N; -.
IntAct; P25298; 44.
MINT; P25298; -.
STRING; 4932.YMR061W; -.
iPTMnet; P25298; -.
MaxQB; P25298; -.
PaxDb; P25298; -.
PRIDE; P25298; -.
EnsemblFungi; YMR061W; YMR061W; YMR061W.
GeneID; 855083; -.
KEGG; sce:YMR061W; -.
EuPathDB; FungiDB:YMR061W; -.
SGD; S000004665; RNA14.
GeneTree; ENSGT00390000006758; -.
HOGENOM; HOG000000753; -.
KO; K14408; -.
OMA; YTKWENE; -.
OrthoDB; EOG092C0WNE; -.
BioCyc; YEAST:G3O-32764-MONOMER; -.
Reactome; R-SCE-77595; Processing of Intronless Pre-mRNAs.
PRO; PR:P25298; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0005849; C:mRNA cleavage factor complex; IPI:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IPI:SGD.
GO; GO:0006378; P:mRNA polyadenylation; IDA:SGD.
GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IDA:SGD.
GO; GO:0072423; P:response to DNA damage checkpoint signaling; IMP:SGD.
InterPro; IPR003107; HAT.
InterPro; IPR008847; Suf.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF05843; Suf; 1.
SMART; SM00386; HAT; 8.
SUPFAM; SSF48452; SSF48452; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; mRNA processing; Nucleus;
Reference proteome; Repeat.
CHAIN 1 677 mRNA 3'-end-processing protein RNA14.
/FTId=PRO_0000205761.
REPEAT 56 88 HAT 1.
REPEAT 90 124 HAT 2.
REPEAT 138 170 HAT 3.
REPEAT 181 214 HAT 4.
REPEAT 257 289 HAT 5.
REPEAT 298 330 HAT 6.
HELIX 633 641 {ECO:0000244|PDB:2L9B}.
HELIX 645 648 {ECO:0000244|PDB:2L9B}.
HELIX 655 664 {ECO:0000244|PDB:2L9B}.
SEQUENCE 677 AA; 79960 MW; 102433295FE7CD63 CRC64;
MSSSTTPDLL YPSADKVAEP SDNIHGDELR LRERIKDNPT NILSYFQLIQ YLETQESYAK
VREVYEQFHN TFPFYSPAWT LQLKGELARD EFETVEKILA QCLSGKLENN DLSLWSTYLD
YIRRKNNLIT GGQEARAVIV KAFQLVMQKC AIFEPKSSSF WNEYLNFLEQ WKPFNKWEEQ
QRIDMLREFY KKMLCVPFDN LEKMWNRYTQ WEQEINSLTA RKFIGELSAE YMKARSLYQE
WLNVTNGLKR ASPINLRTAN KKNIPQPGTS DSNIQQLQIW LNWIKWEREN KLMLSEDMLS
QRISYVYKQG IQYMIFSAEM WYDYSMYISE NSDRQNILYT ALLANPDSPS LTFKLSECYE
LDNDSESVSN CFDKCTQTLL SQYKKIASDV NSGEDNNTEY EQELLYKQRE KLTFVFCVYM
NTMKRISGLS AARTVFGKCR KLKRILTHDV YVENAYLEFQ NQNDYKTAFK VLELGLKYFQ
NDGVYINKYL DFLIFLNKDS QIKTLFETSV EKVQDLTQLK EIYKKMISYE SKFGNLNNVY
SLEKRFFERF PQENLIEVFT SRYQIQNSNL IKKLELTYMY NEEEDSYFSS GNGDGHHGSY
NMSSSDRKRL MEETGNNGNF SNKKFKRDSE LPTEVLDLLS VIPKRQYFNT NLLDAQKLVN
FLNDQVEIPT VESTKSG


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