RNA15_YEAST
ID RNA15_YEAST Reviewed; 296 AA.
AC P25299; D6VU95;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=mRNA 3'-end-processing protein RNA15;
GN Name=RNA15; OrderedLocusNames=YGL044C;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 INTERACTION WITH PAB1.
RX PubMed=9199303; DOI=10.1128/mcb.17.7.3694;
RA Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F.;
RT "Yeast Pab1 interacts with Rna15 and participates in the control of the
RT poly(A) tail length in vitro.";
RL Mol. Cell. Biol. 17:3694-3701(1997).
RN [7]
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 [8]
RP RNA-BINDING.
RX PubMed=11689695; DOI=10.1128/mcb.21.23.8045-8055.2001;
RA Gross S., Moore C.L.;
RT "Rna15 interaction with the A-rich yeast polyadenylation signal is an
RT essential step in mRNA 3'-end formation.";
RL Mol. Cell. Biol. 21:8045-8055(2001).
RN [9]
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 [10]
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: RNA-binding component of the cleavage factor IA (CFIA)
CC complex, which is involved in the endonucleolytic cleavage during
CC polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with
CC the cleavage factor NAB4/CFIB and the cleavage and polyadenylation
CC factor (CPF) complex. Binds to A-rich RNA sequence elements.
CC {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 directly with RNA14. Interacts with
CC polyadenylate-binding protein PAB1. {ECO:0000269|PubMed:9199303}.
CC -!- INTERACTION:
CC P25299; P39081: PCF11; NbExp=8; IntAct=EBI-15640, EBI-12980;
CC P25299; P25298: RNA14; NbExp=10; IntAct=EBI-15640, EBI-15632;
CC P25299; P54000: SUB1; NbExp=2; IntAct=EBI-15640, EBI-18492;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 6350 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M73462; AAA34984.1; -; Genomic_DNA.
DR EMBL; Z72566; CAA96746.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08056.1; -; Genomic_DNA.
DR PIR; B40257; B40257.
DR RefSeq; NP_011471.1; NM_001180909.1.
DR PDB; 2KM8; NMR; -; B=14-97.
DR PDB; 2L9B; NMR; -; A=127-232.
DR PDB; 2X1A; X-ray; 2.05 A; A=16-111.
DR PDB; 2X1B; X-ray; 1.80 A; A=16-111.
DR PDB; 2X1F; X-ray; 1.60 A; A=16-103.
DR PDBsum; 2KM8; -.
DR PDBsum; 2L9B; -.
DR PDBsum; 2X1A; -.
DR PDBsum; 2X1B; -.
DR PDBsum; 2X1F; -.
DR AlphaFoldDB; P25299; -.
DR BMRB; P25299; -.
DR SMR; P25299; -.
DR BioGRID; 33204; 318.
DR ComplexPortal; CPX-1895; mRNA cleavage factor complex CFIA.
DR ComplexPortal; CPX-1896; mRNA cleavage factor complex CFI.
DR DIP; DIP-1489N; -.
DR IntAct; P25299; 10.
DR MINT; P25299; -.
DR STRING; 4932.YGL044C; -.
DR iPTMnet; P25299; -.
DR MaxQB; P25299; -.
DR PaxDb; P25299; -.
DR PRIDE; P25299; -.
DR EnsemblFungi; YGL044C_mRNA; YGL044C; YGL044C.
DR GeneID; 852838; -.
DR KEGG; sce:YGL044C; -.
DR SGD; S000003012; RNA15.
DR VEuPathDB; FungiDB:YGL044C; -.
DR eggNOG; KOG0108; Eukaryota.
DR GeneTree; ENSGT00940000168465; -.
DR HOGENOM; CLU_028601_0_1_1; -.
DR OMA; TKFRLMI; -.
DR BioCyc; YEAST:G3O-30555-MON; -.
DR EvolutionaryTrace; P25299; -.
DR PRO; PR:P25299; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P25299; protein.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IPI:SGD.
DR GO; GO:0003729; F:mRNA 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:0072423; P:response to DNA damage checkpoint signaling; IMP:SGD.
DR DisProt; DP02761; -.
DR Gene3D; 1.10.20.70; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR026896; CSTF_C.
DR InterPro; IPR038192; CSTF_C_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF14304; CSTF_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..296
FT /note="mRNA 3'-end-processing protein RNA15"
FT /id="PRO_0000081807"
FT DOMAIN 18..96
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 99..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:2X1F"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:2X1F"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:2X1F"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:2X1F"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:2X1F"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:2X1F"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2KM8"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2X1F"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2X1F"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:2X1F"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:2L9B"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2L9B"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:2L9B"
FT HELIX 174..190
FT /evidence="ECO:0007829|PDB:2L9B"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:2L9B"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:2L9B"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2L9B"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2L9B"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:2L9B"
SQ SEQUENCE 296 AA; 32791 MW; 10053B8648A71ECB CRC64;
MNRQSGVNAG VQNNPPSRVV YLGSIPYDQT EEQILDLCSN VGPVINLKMM FDPQTGRSKG
YAFIEFRDLE SSASAVRNLN GYQLGSRFLK CGYSSNSDIS GVSQQQQQQY NNINGNNNNN
GNNNNNSNGP DFQNSGNANF LSQKFPELPS GIDVNINMTT PAMMISSELA KKPKEVQLKF
LQKFQEWTRA HPEDAVSLLE LCPQLSFVTA ELLLTNGICK VDDLIPLASR PQEEASATNN
NSVNEVVDPA VLNKQKELLK QVLQLNDSQI SILPDDERMA IWDLKQKALR GEFGAF
