RNA14_YEAST
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 03-AUG-2022, entry version 176.
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; 263.
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; P25298; -.
DR PRIDE; P25298; -.
DR EnsemblFungi; YMR061W_mRNA; YMR061W; YMR061W.
DR GeneID; 855083; -.
DR KEGG; sce:YMR061W; -.
DR SGD; S000004665; RNA14.
DR VEuPathDB; FungiDB:YMR061W; -.
DR eggNOG; KOG1914; Eukaryota.
DR GeneTree; ENSGT00390000006758; -.
DR HOGENOM; CLU_007630_0_1_1; -.
DR OMA; PKRQYFK; -.
DR BioCyc; YEAST:G3O-32764-MON; -.
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: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:SGD.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; 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 InterPro; IPR003107; HAT.
DR InterPro; IPR045243; Rna14-like.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR19980; PTHR19980; 1.
DR Pfam; PF05843; Suf; 2.
DR SMART; SM00386; HAT; 8.
DR SUPFAM; SSF48452; SSF48452; 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
