RIO2_YEAST
ID RIO2_YEAST Reviewed; 425 AA.
AC P40160; D6W0Y3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Serine/threonine-protein kinase RIO2;
DE EC=2.7.11.1 {ECO:0000269|PubMed:12690111};
GN Name=RIO2; OrderedLocusNames=YNL207W; ORFNames=N1342;
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 96604 / S288c / FY1679;
RX PubMed=7725799; DOI=10.1002/yea.320101213;
RA Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT new open reading frames of unknown function.";
RL Yeast 10:1639-1645(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
RP FUNCTION, INTERACTION WITH TSR1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-73; ILE-186; TYR-210; GLU-364; ASP-371 AND ASP-417.
RX PubMed=12628929; DOI=10.1093/emboj/cdg121;
RA Schaefer T., Strauss D., Petfalski E., Tollervey D., Hurt E.;
RT "The path from nucleolar 90S to cytoplasmic 40S pre-ribosomes.";
RL EMBO J. 22:1370-1380(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND MUTAGENESIS OF LYS-105; HIS-227 AND ASP-229.
RX PubMed=12690111; DOI=10.1074/jbc.m300759200;
RA Geerlings T.H., Faber A.W., Bister M.D., Vos J.C., Raue H.A.;
RT "Rio2p, an evolutionarily conserved, low abundant protein kinase essential
RT for processing of 20 S pre-rRNA in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 278:22537-22545(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12612080; DOI=10.1128/mcb.23.6.2083-2095.2003;
RA Vanrobays E., Gelugne J.-P., Gleizes P.-E., Caizergues-Ferrer M.;
RT "Late cytoplasmic maturation of the small ribosomal subunit requires RIO
RT proteins in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 23:2083-2095(2003).
RN [7]
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).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15167894; DOI=10.1038/sj.emboj.7600252;
RA Leger-Silvestre I., Milkereit P., Ferreira-Cerca S., Saveanu C.,
RA Rousselle J.-C., Choesmel V., Guinefoleau C., Gas N., Gleizes P.-E.;
RT "The ribosomal protein Rps15p is required for nuclear exit of the 40S
RT subunit precursors in yeast.";
RL EMBO J. 23:2336-2347(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16159874; DOI=10.1074/jbc.m506916200;
RA Leger-Silvestre I., Caffrey J.M., Dawaliby R., Alvarez-Arias D.A., Gas N.,
RA Bertolone S.J., Gleizes P.E., Ellis S.R.;
RT "Specific role for yeast homologs of the Diamond Blackfan anemia-associated
RT Rps19 protein in ribosome synthesis.";
RL J. Biol. Chem. 280:38177-38185(2005).
RN [10]
RP IDENTIFICATION IN PRE-40S PARTICLE, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16738661; DOI=10.1038/nature04840;
RA Schaefer T., Maco B., Petfalski E., Tollervey D., Boettcher B., Aebi U.,
RA Hurt E.;
RT "Hrr25-dependent phosphorylation state regulates organization of the pre-
RT 40S subunit.";
RL Nature 441:651-655(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Required for the final endonucleolytic cleavage of 20S pre-
CC rRNA at site D in the cytoplasm, converting it into the mature 18S
CC rRNA. Involved in normal export of the pre-40S particles from the
CC nucleus to the cytoplasm. No longer associates with pre-40S subunits in
CC RPS19 disruptions, suggesting it acts after the ribosomal protein in
CC 18S rRNA maturation. {ECO:0000269|PubMed:12612080,
CC ECO:0000269|PubMed:12628929, ECO:0000269|PubMed:12690111,
CC ECO:0000269|PubMed:15167894, ECO:0000269|PubMed:16159874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:12690111};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:12690111};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12690111};
CC -!- SUBUNIT: Component of a late pre-40S ribosomal particle, composed of
CC the 40S ribosomal proteins and the non-ribosomal factors DIM1, DIM2,
CC ENP1, HRR25, LTV1, NOB1, RIO2 and TSR1. {ECO:0000269|PubMed:16738661}.
CC -!- INTERACTION:
CC P40160; P34078: LTV1; NbExp=4; IntAct=EBI-29124, EBI-10248;
CC P40160; P05750: RPS3; NbExp=2; IntAct=EBI-29124, EBI-16140;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC cytoplasmic.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:12690111}.
CC -!- MISCELLANEOUS: Present with 10300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; X78898; CAA55501.1; -; Genomic_DNA.
DR EMBL; Z71483; CAA96109.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10349.1; -; Genomic_DNA.
DR PIR; S50724; S50724.
DR RefSeq; NP_014192.1; NM_001183045.1.
DR PDB; 6EML; EM; 3.60 A; r=1-425.
DR PDB; 6FAI; EM; 3.40 A; l=1-425.
DR PDB; 6RBD; EM; 3.47 A; l=1-425.
DR PDB; 6Y7C; EM; 3.80 A; l=1-425.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6Y7C; -.
DR AlphaFoldDB; P40160; -.
DR SMR; P40160; -.
DR BioGRID; 35629; 226.
DR DIP; DIP-4894N; -.
DR IntAct; P40160; 50.
DR MINT; P40160; -.
DR STRING; 4932.YNL207W; -.
DR iPTMnet; P40160; -.
DR MaxQB; P40160; -.
DR PaxDb; P40160; -.
DR PRIDE; P40160; -.
DR EnsemblFungi; YNL207W_mRNA; YNL207W; YNL207W.
DR GeneID; 855514; -.
DR KEGG; sce:YNL207W; -.
DR SGD; S000005151; RIO2.
DR VEuPathDB; FungiDB:YNL207W; -.
DR eggNOG; KOG2268; Eukaryota.
DR GeneTree; ENSGT00390000003255; -.
DR HOGENOM; CLU_018693_0_0_1; -.
DR InParanoid; P40160; -.
DR OMA; GYTNFRE; -.
DR BioCyc; YEAST:G3O-33213-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P40160; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40160; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0046830; P:positive regulation of RNA import into nucleus; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd05144; RIO2_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR030484; Rio2.
DR InterPro; IPR015285; RIO2_wHTH_N.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF09202; Rio2_N; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..425
FT /note="Serine/threonine-protein kinase RIO2"
FT /id="PRO_0000213532"
FT DOMAIN 95..257
FT /note="Protein kinase"
FT REGION 350..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..400
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 73
FT /note="Y->H: In RIO2-1; nuclear export of ribosomal 40S
FT subunits impaired; when associated with V-186, H-210, D-
FT 364, G-371 and G-417."
FT /evidence="ECO:0000269|PubMed:12628929"
FT MUTAGEN 105
FT /note="K->I: No change in activity."
FT /evidence="ECO:0000269|PubMed:12690111"
FT MUTAGEN 186
FT /note="I->V: In RIO2-1; nuclear export of ribosomal 40S
FT subunits impaired; when associated with H-73, H-210, D-364,
FT G-371 and G-417."
FT /evidence="ECO:0000269|PubMed:12628929"
FT MUTAGEN 210
FT /note="Y->H: In RIO2-1; nuclear export of ribosomal 40S
FT subunits impaired; when associated with H-73, V-186, D-364,
FT G-371 and G-417."
FT /evidence="ECO:0000269|PubMed:12628929"
FT MUTAGEN 227
FT /note="H->F: No change in activity."
FT /evidence="ECO:0000269|PubMed:12690111"
FT MUTAGEN 229
FT /note="D->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:12690111"
FT MUTAGEN 364
FT /note="E->D: In RIO2-1; nuclear export of ribosomal 40S
FT subunits impaired; when associated with H-73, V-186, H-210,
FT G-371 and G-417."
FT /evidence="ECO:0000269|PubMed:12628929"
FT MUTAGEN 371
FT /note="D->G: In RIO2-1; nuclear export of ribosomal 40S
FT subunits impaired; when associated with H-73, V-186, H-210,
FT D-364 and G-417."
FT /evidence="ECO:0000269|PubMed:12628929"
FT MUTAGEN 417
FT /note="D->G: In RIO2-1; nuclear export of ribosomal 40S
FT subunits impaired; when associated with H-73, V-186, H-210,
FT D-364 and G-371."
FT /evidence="ECO:0000269|PubMed:12628929"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 149..171
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6FAI"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 206..223
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:6FAI"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 265..282
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:6FAI"
SQ SEQUENCE 425 AA; 49125 MW; 02117D0328118E8D CRC64;
MKLDTSHMRY LTTDDFRVLQ AVEQGSRSHE VVPTPLIHQI SGMRSQSGTN RAISDLAKLS
LISKMRNVKY DGYRLTYNGI DYLALKTMLN RDTVYSVGNT IGVGKESDIY KVSDKNGNPR
VMKIHRLGRT SFHSVRNNRD YLKKSNQGAN WMHLSRLAAN KEYQFMSMLY SKGFKVPEPF
DNSRHIVVME LIEGYPMRRL RKHKNIPKLY SDLMCFIVDL ANSGLIHCDF NEFNIMIKDK
LEDENDCGFV VIDFPQCISI QHQDADYYFQ RDVDCIRRFF KKKLKYEPKP DSSMLDTEGF
GDGYKYAYPD FKRDVKRTDN LDELVQASGF SKKHPGDRGL ETAVESMRNA VYNSDDDMSN
DEAEEENGEG DYSEEDEYYD SELDNESSED DSEDAQEEEN ERIIEALSSG VENLKMDKLG
NYILE
