RLP24_YEAST
ID RLP24_YEAST Reviewed; 199 AA.
AC Q07915; D6VY11;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Ribosome biogenesis protein RLP24;
DE AltName: Full=Ribosomal protein L24-like;
GN Name=RLP24; OrderedLocusNames=YLR009W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NOG1.
RX PubMed=12808088; DOI=10.1128/mcb.23.13.4449-4460.2003;
RA Saveanu C., Namane A., Gleizes P.-E., Lebreton A., Rousselle J.-C.,
RA Noaillac-Depeyre J., Gas N., Jacquier A., Fromont-Racine M.;
RT "Sequential protein association with nascent 60S ribosomal particles.";
RL Mol. Cell. Biol. 23:4449-4460(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, 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).
RN [6]
RP FUNCTION, INTERACTION WITH AFG2, AND MUTAGENESIS OF 2-ARG--ALA-146 AND
RP 146-LYS--PHE-199.
RX PubMed=23185031; DOI=10.1083/jcb.201205021;
RA Kappel L., Loibl M., Zisser G., Klein I., Fruhmann G., Gruber C.,
RA Unterweger S., Rechberger G., Pertschy B., Bergler H.;
RT "Rlp24 activates the AAA-ATPase Drg1 to initiate cytoplasmic pre-60S
RT maturation.";
RL J. Cell Biol. 199:771-782(2012).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit
CC (PubMed:12808088, PubMed:23185031). Ensures the docking of NOG1 to pre-
CC 60S ribosomal particles (PubMed:12808088). Activates and recruits
CC ATPase AFG2 to cytoplasmic pre-60S ribosomal particles
CC (PubMed:23185031). {ECO:0000269|PubMed:12808088,
CC ECO:0000269|PubMed:23185031}.
CC -!- SUBUNIT: Associated with nucleolar and cytoplasmic pre-60S particles
CC (PubMed:12808088). At the end of biogenesis it dissociates from
CC cytoplasmic pre-60S particles and is likely to be exchanged for its
CC ribosomal homolog, RPL24 (PubMed:12808088, PubMed:23185031). Interacts
CC (via C-terminus) with AFG2 (hexameric form); the interaction is direct,
CC recruits AFG2 to pre-60S ribosomal particles and promotes AFG2 ATPase
CC activity and RLP24 release from pre-60S ribosomal particles
CC (PubMed:23185031). Interacts with NOG1; the interaction is direct
CC (PubMed:12808088). {ECO:0000269|PubMed:12808088,
CC ECO:0000269|PubMed:23185031}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12808088}. Nucleus
CC {ECO:0000269|PubMed:12808088}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000269|PubMed:12808088}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.
CC {ECO:0000305}.
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DR EMBL; Z73181; CAA97531.1; -; Genomic_DNA.
DR EMBL; AY558197; AAS56523.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09327.1; -; Genomic_DNA.
DR PIR; S64831; S64831.
DR RefSeq; NP_013109.1; NM_001181896.1.
DR PDB; 3JCT; EM; 3.08 A; u=1-199.
DR PDB; 4V7F; EM; 8.70 A; p=1-199.
DR PDB; 5FL8; EM; 9.50 A; t=1-199.
DR PDB; 5JCS; EM; 9.50 A; t=1-199.
DR PDB; 6C0F; EM; 3.70 A; u=1-199.
DR PDB; 6ELZ; EM; 3.30 A; u=1-199.
DR PDB; 6EM1; EM; 3.60 A; u=1-199.
DR PDB; 6EM4; EM; 4.10 A; u=1-199.
DR PDB; 6EM5; EM; 4.30 A; u=1-199.
DR PDB; 6FT6; EM; 3.90 A; u=1-199.
DR PDB; 6M62; EM; 3.20 A; u=1-199.
DR PDB; 6N8J; EM; 3.50 A; u=1-199.
DR PDB; 6N8K; EM; 3.60 A; u=1-199.
DR PDB; 6N8L; EM; 3.60 A; u=1-199.
DR PDB; 6YLG; EM; 3.00 A; u=1-199.
DR PDB; 6YLH; EM; 3.10 A; u=1-199.
DR PDB; 6YLX; EM; 3.90 A; u=1-199.
DR PDB; 6YLY; EM; 3.80 A; u=1-199.
DR PDB; 7BT6; EM; 3.12 A; u=1-199.
DR PDB; 7BTB; EM; 3.22 A; u=1-199.
DR PDB; 7OF1; EM; 3.10 A; u=1-199.
DR PDB; 7OH3; EM; 3.40 A; u=1-199.
DR PDB; 7OHQ; EM; 3.10 A; u=1-199.
DR PDB; 7OHR; EM; 4.72 A; u=1-199.
DR PDB; 7OHS; EM; 4.38 A; u=1-199.
DR PDB; 7OHT; EM; 4.70 A; u=1-199.
DR PDB; 7OHU; EM; 3.70 A; u=1-199.
DR PDB; 7OHV; EM; 3.90 A; u=1-199.
DR PDB; 7OHX; EM; 3.30 A; u=1-199.
DR PDB; 7OHY; EM; 3.90 A; u=1-199.
DR PDBsum; 3JCT; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHT; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR AlphaFoldDB; Q07915; -.
DR SMR; Q07915; -.
DR BioGRID; 31282; 339.
DR DIP; DIP-4748N; -.
DR IntAct; Q07915; 16.
DR MINT; Q07915; -.
DR STRING; 4932.YLR009W; -.
DR iPTMnet; Q07915; -.
DR PaxDb; Q07915; -.
DR PRIDE; Q07915; -.
DR EnsemblFungi; YLR009W_mRNA; YLR009W; YLR009W.
DR GeneID; 850695; -.
DR KEGG; sce:YLR009W; -.
DR SGD; S000003999; RLP24.
DR VEuPathDB; FungiDB:YLR009W; -.
DR eggNOG; KOG1723; Eukaryota.
DR GeneTree; ENSGT00950000183105; -.
DR HOGENOM; CLU_089419_1_1_1; -.
DR InParanoid; Q07915; -.
DR OMA; HNPRKVK; -.
DR BioCyc; YEAST:G3O-32170-MON; -.
DR PRO; PR:Q07915; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07915; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IDA:SGD.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IMP:SGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IMP:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:SGD.
DR CDD; cd00472; Ribosomal_L24e_L24; 1.
DR Gene3D; 2.30.170.20; -; 1.
DR InterPro; IPR038630; L24e/L24_sf.
DR InterPro; IPR000988; Ribosomal_L24e-rel.
DR InterPro; IPR011017; TRASH_dom.
DR PANTHER; PTHR10792; PTHR10792; 1.
DR Pfam; PF01246; Ribosomal_L24e; 1.
DR SMART; SM00746; TRASH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..199
FT /note="Ribosome biogenesis protein RLP24"
FT /id="PRO_0000136910"
FT REGION 147..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..178
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 2..146
FT /note="Missing: No defect in the interaction with AFG2 or
FT in promoting AFG2 activation."
FT /evidence="ECO:0000269|PubMed:23185031"
FT MUTAGEN 147..199
FT /note="Missing: Reduces interaction with AFG2. Loss of AFG2
FT activation."
FT /evidence="ECO:0000269|PubMed:23185031"
SQ SEQUENCE 199 AA; 23975 MW; D7F1CD7EB92C6576 CRC64;
MRIYQCHFCS SPCYPGHGIM FVRNDAKEFR FCRSKCHKAF KQRRNPRKLK WTKAFRKAAG
KELAVDSTLT FAQRRNVPVR YNRELVATTL KAMARIEEIR QKRERAFYKN RMRGNKEKDF
LRDKKLVESN PELLRIREVE IARKLAKEQE RAESVSEQEE SEEEEEDMEI DSDEEEEEQL
EKQKILLKNR RRNTKKIAF
