RSSA2_YEAST
ID RSSA2_YEAST Reviewed; 252 AA.
AC P46654; D6VY50;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=40S ribosomal protein S0-B {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000303|PubMed:9559554};
DE AltName: Full=Nucleic acid-binding protein NAB1B;
DE AltName: Full=Small ribosomal subunit protein uS2-B {ECO:0000303|PubMed:24524803};
GN Name=RPS0B {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000303|PubMed:9559554};
GN Synonyms=NAB1B, NAB4, YST2; OrderedLocusNames=YLR048W; ORFNames=L2118;
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].
RX PubMed=8626693; DOI=10.1074/jbc.271.19.11383;
RA Demianova M.A., Formosa T.G., Ellis S.R.;
RT "Yeast proteins related to the p40/laminin receptor precursor are essential
RT components of the 40 S ribosomal subunit.";
RL J. Biol. Chem. 271:11383-11391(1996).
RN [2]
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 [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 PROTEIN SEQUENCE OF 2-27; 63-79 AND 89-134, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 53-56; 102-111 AND 135-146.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA Norbeck J., Blomberg A.;
RT "Metabolic and regulatory changes associated with growth of Saccharomyces
RT cerevisiae in 1.4 M NaCl. Evidence for osmotic induction of glycerol
RT dissimilation via the dihydroxyacetone pathway.";
RL J. Biol. Chem. 272:5544-5554(1997).
RN [6]
RP GENE EVOLUTION.
RX PubMed=9718729; DOI=10.1093/oxfordjournals.molbev.a026000;
RA Ardini E., Pesole G., Tagliabue E., Magnifico A., Castronovo V.,
RA Sobel M.E., Colnaghi M.I., Menard S.;
RT "The 67-kDa laminin receptor originated from a ribosomal protein that
RT acquired a dual function during evolution.";
RL Mol. Biol. Evol. 15:1017-1025(1998).
RN [7]
RP NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=9973221;
RA Ford C.L., Randal-Whitis L., Ellis S.R.;
RT "Yeast proteins related to the p40/laminin receptor precursor are required
RT for 20S ribosomal RNA processing and the maturation of 40S ribosomal
RT subunits.";
RL Cancer Res. 59:704-710(1999).
RN [9]
RP CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
RX PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
RA Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
RT "The action of N-terminal acetyltransferases on yeast ribosomal proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14627813; DOI=10.1093/nar/gkg899;
RA Tabb-Massey A., Caffrey J.M., Logsden P., Taylor S., Trent J.O.,
RA Ellis S.R.;
RT "Ribosomal proteins Rps0 and Rps21 of Saccharomyces cerevisiae have
RT overlapping functions in the maturation of the 3' end of 18S rRNA.";
RL Nucleic Acids Res. 31:6798-6805(2003).
RN [13]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
RN [14]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel (PubMed:22096102). uS2 is required for the assembly and/or
CC stability of the 40S ribosomal subunit. Required for the processing of
CC the 20S rRNA-precursor to mature 18S rRNA in a late step of the
CC maturation of 40S ribosomal subunits (PubMed:9973221, PubMed:14627813).
CC {ECO:0000269|PubMed:14627813, ECO:0000269|PubMed:9973221,
CC ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14627813,
CC ECO:0000269|PubMed:22096102}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4}.
CC -!- DISRUPTION PHENOTYPE: Reduction in growth rate, a decrease in free 40S
CC subunits, an increase in the amount of free 60S subunits and a decrease
CC in polysome size. {ECO:0000269|PubMed:14627813}.
CC -!- MISCELLANEOUS: Present with 60900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for uS2 in yeast. {ECO:0000305}.
CC -!- MISCELLANEOUS: This protein appears to have acquired a second function
CC as a laminin receptor specifically in the vertebrate lineage. This
CC protein does not bind laminin. {ECO:0000305|PubMed:9718729}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000255|HAMAP-Rule:MF_03015}.
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DR EMBL; U33756; AAC49276.1; -; Genomic_DNA.
DR EMBL; X94607; CAA64295.1; -; Genomic_DNA.
DR EMBL; Z73220; CAA97578.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09366.1; -; Genomic_DNA.
DR PIR; S59364; S59364.
DR RefSeq; NP_013149.1; NM_001181935.1.
DR PDB; 6WOO; EM; 2.90 A; AA=2-207.
DR PDBsum; 6WOO; -.
DR AlphaFoldDB; P46654; -.
DR SMR; P46654; -.
DR BioGRID; 31323; 337.
DR IntAct; P46654; 91.
DR MINT; P46654; -.
DR STRING; 4932.YLR048W; -.
DR iPTMnet; P46654; -.
DR MaxQB; P46654; -.
DR PaxDb; P46654; -.
DR PRIDE; P46654; -.
DR EnsemblFungi; YLR048W_mRNA; YLR048W; YLR048W.
DR GeneID; 850737; -.
DR KEGG; sce:YLR048W; -.
DR SGD; S000004038; RPS0B.
DR VEuPathDB; FungiDB:YLR048W; -.
DR eggNOG; KOG0830; Eukaryota.
DR GeneTree; ENSGT00950000183099; -.
DR HOGENOM; CLU_058171_2_0_1; -.
DR InParanoid; P46654; -.
DR OMA; QQKTKDM; -.
DR BioCyc; YEAST:G3O-32204-MON; -.
DR PRO; PR:P46654; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P46654; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
DR GO; GO:0006407; P:rRNA export from nucleus; IGI:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR CDD; cd01425; RPS2; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR InterPro; IPR001865; Ribosomal_S2.
DR InterPro; IPR018130; Ribosomal_S2_CS.
DR InterPro; IPR027498; Ribosomal_S2_euk.
DR InterPro; IPR005707; Ribosomal_S2_euk/arc.
DR InterPro; IPR023591; Ribosomal_S2_flav_dom_sf.
DR PANTHER; PTHR11489; PTHR11489; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF52313; SSF52313; 1.
DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ribosome biogenesis; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03015,
FT ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4"
FT CHAIN 2..252
FT /note="40S ribosomal protein S0-B"
FT /id="PRO_0000134371"
FT REGION 213..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03015,
FT ECO:0000269|PubMed:10601260, ECO:0000269|Ref.4"
SQ SEQUENCE 252 AA; 27962 MW; B9B7CDFB335EFAC3 CRC64;
MSLPATFDLT PEDAQLLLAA NTHLGARNVQ VHQEPYVFNA RPDGVHVINV GKTWEKLVLA
ARIIAAIPNP EDVVAISSRT YGQRAVLKFA AHTGATPIAG RFTPGSFTNY ITRSFKEPRL
VIVTDPRLDA QAIKEASYVN IPVIALTDLD SPSEFVDVAI PCNNRGKHSI GLIWYLLARE
VLRLRGALVD RTQPWSIMPD LYFYRNPEEV EQVAEEAAAA EEGEEEEVKE EVTEGQAEAT
EWAEENADNV EW
