ID   RNA14_YEAST             Reviewed;         677 AA.
AC   P25298; D6VZN5;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   27-MAR-2024, entry version 182.
DE   RecName: Full=mRNA 3'-end-processing protein RNA14;
GN   Name=RNA14; OrderedLocusNames=YMR061W; ORFNames=YM9796.14;
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 28383 / FL100 / VTT C-80102;
RX   PubMed=1674817; DOI=10.1128/mcb.11.6.3075-3087.1991;
RA   Minvielle-Sebastia L., Winsor B., Bonneaud N., Lacroute F.;
RT   "Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA
RT   decay rate; sequence analysis reveals an RNA-binding domain in the RNA15
RT   protein.";
RL   Mol. Cell. Biol. 11:3075-3087(1991).
RN   [2]
RP   SEQUENCE REVISION.
RA   Bonneaud N.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [4]
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   [5]
RP   FUNCTION.
RX   PubMed=7992054; DOI=10.1126/science.7992054;
RA   Minvielle-Sebastia L., Preker P.J., Keller W.;
RT   "RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end
RT   processing factor.";
RL   Science 266:1702-1705(1994).
RN   [6]
RP   COMPOSITION OF THE CFIA COMPLEX.
RX   PubMed=8900210; DOI=10.1074/jbc.271.43.27167;
RA   Kessler M.M., Zhao J., Moore C.L.;
RT   "Purification of the Saccharomyces cerevisiae cleavage/polyadenylation
RT   factor I. Separation into two components that are required for both
RT   cleavage and polyadenylation of mRNA 3' ends.";
RL   J. Biol. Chem. 271:27167-27175(1996).
RN   [7]
RP   IDENTIFICATION IN THE CFIA COMPLEX.
RX   PubMed=9223284; DOI=10.1073/pnas.94.15.7897;
RA   Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y., Keller W.;
RT   "The major yeast poly(A)-binding protein is associated with cleavage factor
RT   IA and functions in premessenger RNA 3'-end formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7897-7902(1997).
RN   [8]
RP   INTERACTION WITH FIP1; PFS2 AND YSH1.
RX   PubMed=10619842; DOI=10.1093/emboj/19.1.37;
RA   Ohnacker M., Barabino S.M.L., Preker P.J., Keller W.;
RT   "The WD-repeat protein pfs2p bridges two essential factors within the yeast
RT   pre-mRNA 3'-end-processing complex.";
RL   EMBO J. 19:37-47(2000).
RN   [9]
RP   FUNCTION OF THE CFIA COMPLEX.
RX   PubMed=11344258; DOI=10.1073/pnas.101046598;
RA   Gross S., Moore C.;
RT   "Five subunits are required for reconstitution of the cleavage and
RT   polyadenylation activities of Saccharomyces cerevisiae cleavage factor I.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6080-6085(2001).
RN   [10]
RP   INTERACTION WITH RBP1.
RX   PubMed=12727883; DOI=10.1093/emboj/cdg200;
RA   Sadowski M., Dichtl B., Huebner W., Keller W.;
RT   "Independent functions of yeast Pcf11p in pre-mRNA 3' end processing and in
RT   transcription termination.";
RL   EMBO J. 22:2167-2177(2003).
RN   [11]
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: Component of the cleavage factor IA (CFIA) complex, which is
CC       involved in the endonucleolytic cleavage during polyadenylation-
CC       dependent pre-mRNA 3'-end formation and cooperates with the cleavage
CC       factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF)
CC       complex. {ECO:0000269|PubMed:11344258, ECO:0000269|PubMed:7992054}.
CC   -!- SUBUNIT: Component of the CFIA complex, which is composed of RNA14,
CC       RNA15, PCF11 and CLP1. Interacts with FIP1, PFS2, YSH1 and probably
CC       also with RNA15. Probably interacts with the phosphorylated CTD domain
CC       of RPB1/RNA polymerase II. {ECO:0000269|PubMed:10619842,
CC       ECO:0000269|PubMed:12727883, ECO:0000269|PubMed:9223284}.
CC   -!- INTERACTION:
CC       P25298; Q99383: HRP1; NbExp=2; IntAct=EBI-15632, EBI-11783;
CC       P25298; P39081: PCF11; NbExp=10; IntAct=EBI-15632, EBI-12980;
CC       P25298; P25299: RNA15; NbExp=10; IntAct=EBI-15632, EBI-15640;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleus and/or
CC       cytoplasm.
CC   -!- MISCELLANEOUS: Present with 5350 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; M73461; AAA21300.1; -; Genomic_DNA.
DR   EMBL; Z49703; CAA89771.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09959.1; -; Genomic_DNA.
DR   PIR; S54561; S54561.
DR   RefSeq; NP_013777.1; NM_001182559.1.
DR   PDB; 2L9B; NMR; -; B=626-677.
DR   PDBsum; 2L9B; -.
DR   AlphaFoldDB; P25298; -.
DR   BMRB; P25298; -.
DR   SMR; P25298; -.
DR   BioGRID; 35236; 265.
DR   ComplexPortal; CPX-1895; mRNA cleavage factor complex CFIA.
DR   ComplexPortal; CPX-1896; mRNA cleavage factor complex CFI.
DR   DIP; DIP-1488N; -.
DR   IntAct; P25298; 41.
DR   MINT; P25298; -.
DR   STRING; 4932.YMR061W; -.
DR   iPTMnet; P25298; -.
DR   MaxQB; P25298; -.
DR   PaxDb; 4932-YMR061W; -.
DR   PeptideAtlas; P25298; -.
DR   EnsemblFungi; YMR061W_mRNA; YMR061W; YMR061W.
DR   GeneID; 855083; -.
DR   KEGG; sce:YMR061W; -.
DR   AGR; SGD:S000004665; -.
DR   SGD; S000004665; RNA14.
DR   VEuPathDB; FungiDB:YMR061W; -.
DR   eggNOG; KOG1914; Eukaryota.
DR   GeneTree; ENSGT00390000006758; -.
DR   HOGENOM; CLU_007630_0_1_1; -.
DR   InParanoid; P25298; -.
DR   OMA; PKRQYFK; -.
DR   OrthoDB; 23291at2759; -.
DR   BioCyc; YEAST:G3O-32764-MONOMER; -.
DR   BioGRID-ORCS; 855083; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P25298; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P25298; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005849; C:mRNA cleavage factor complex; IPI:ComplexPortal.
DR   GO; GO:0005848; C:mRNA cleavage stimulating factor complex; IPI:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0006378; P:mRNA polyadenylation; IDA:ComplexPortal.
DR   GO; GO:0006397; P:mRNA processing; IDA:SGD.
DR   GO; GO:0072423; P:response to DNA damage checkpoint signaling; IMP:SGD.
DR   GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR   Gene3D; 1.25.40.1040; -; 1.
DR   Gene3D; 6.10.250.1660; -; 1.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR045243; Rna14-like.
DR   InterPro; IPR008847; Suf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR19980:SF0; CLEAVAGE STIMULATION FACTOR SUBUNIT 3; 1.
DR   PANTHER; PTHR19980; RNA CLEAVAGE STIMULATION FACTOR; 1.
DR   Pfam; PF05843; Suf; 2.
DR   SMART; SM00386; HAT; 8.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; mRNA processing; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN           1..677
FT                   /note="mRNA 3'-end-processing protein RNA14"
FT                   /id="PRO_0000205761"
FT   REPEAT          56..88
FT                   /note="HAT 1"
FT   REPEAT          90..124
FT                   /note="HAT 2"
FT   REPEAT          138..170
FT                   /note="HAT 3"
FT   REPEAT          181..214
FT                   /note="HAT 4"
FT   REPEAT          257..289
FT                   /note="HAT 5"
FT   REPEAT          298..330
FT                   /note="HAT 6"
FT   HELIX           633..641
FT                   /evidence="ECO:0007829|PDB:2L9B"
FT   HELIX           645..648
FT                   /evidence="ECO:0007829|PDB:2L9B"
FT   HELIX           655..664
FT                   /evidence="ECO:0007829|PDB:2L9B"
SQ   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
//