ID   RLA1_YEAST              Reviewed;         106 AA.
AC   P05318; D6VRR8;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 4.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=Large ribosomal subunit protein P1A {ECO:0000303|PubMed:24524803};
DE            Short=P1A;
DE   AltName: Full=60S acidic ribosomal protein P1-alpha {ECO:0000303|PubMed:9559554};
DE            Short=A1;
DE   AltName: Full=L12eIIA;
DE   AltName: Full=YP1alpha;
GN   Name=RPP1A {ECO:0000303|PubMed:9559554};
GN   Synonyms=L12EIIA, RPA1, RPLA1; OrderedLocusNames=YDL081C;
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 [MRNA].
RC   STRAIN=IFO 40028;
RX   PubMed=3287328; DOI=10.1093/nar/16.8.3574;
RA   Tsurugi K., Mitsui K.;
RT   "cDNA and deduced amino acid sequence of acidic ribosomal protein A1 from
RT   Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 16:3574-3574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IFO 40028;
RX   PubMed=2662969; DOI=10.1016/0006-291x(89)91342-9;
RA   Mitsui K., Tsurugi K.;
RT   "Identification of A1 protein as the fourth member of 13 kDa-type acidic
RT   ribosomal protein family in yeast Saccharomyces cerevisiae.";
RL   Biochem. Biophys. Res. Commun. 161:1001-1006(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SR26-12C;
RX   PubMed=2404943; DOI=10.1128/jb.172.2.579-588.1990;
RA   Newton C.H., Shimmin L.C., Yee J., Dennis P.P.;
RT   "A family of genes encode the multiple forms of the Saccharomyces
RT   cerevisiae ribosomal proteins equivalent to the Escherichia coli L12
RT   protein and a single form of the L10-equivalent ribosomal protein.";
RL   J. Bacteriol. 172:579-588(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [5]
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   [6]
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   [7]
RP   PROTEIN SEQUENCE OF 2-5, ACETYLATION AT SER-2, AND PHOSPHORYLATION.
RX   PubMed=8476850; DOI=10.1021/bi00067a010;
RA   Santos C., Ortiz-Reyes B., Naranda T., Remacha M., Ballesta J.P.G.;
RT   "The acidic phosphoproteins from Saccharomyces cerevisiae ribosomes. NH2-
RT   terminal acetylation is a conserved difference between P1 and P2
RT   proteins.";
RL   Biochemistry 32:4231-4236(1993).
RN   [8]
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   [9]
RP   INTERACTION WITH RPP0 AND RPP2B.
RX   PubMed=16573688; DOI=10.1111/j.1365-2958.2006.05117.x;
RA   Krokowski D., Boguszewska A., Abramczyk D., Liljas A., Tchorzewski M.,
RA   Grankowski N.;
RT   "Yeast ribosomal P0 protein has two separate binding sites for P1/P2
RT   proteins.";
RL   Mol. Microbiol. 60:386-400(2006).
RN   [10]
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   [11]
RP   INTERACTION WITH RPP2B.
RX   PubMed=11431471; DOI=10.1074/jbc.m103229200;
RA   Guarinos E., Remacha M., Ballesta J.P.G.;
RT   "Asymmetric interactions between the acidic P1 and P2 proteins in the
RT   Saccharomyces cerevisiae ribosomal stalk.";
RL   J. Biol. Chem. 276:32474-32479(2001).
RN   [12]
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [15]
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   [16]
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. {ECO:0000305|PubMed:22096102}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU). 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). The 5
CC       acidic ribosomal P-proteins form the stalk structure of the 60S
CC       subunit. They are organized as a pentameric complex in which uL10/P0
CC       interacts with 2 heterodimers, P1A-P2B and P1B-P2A (PubMed:16573688,
CC       PubMed:11431471). {ECO:0000269|PubMed:11431471,
CC       ECO:0000269|PubMed:16573688, ECO:0000269|PubMed:22096102,
CC       ECO:0000305|PubMed:9559554}.
CC   -!- INTERACTION:
CC       P05318; P05317: RPP0; NbExp=3; IntAct=EBI-15452, EBI-15447;
CC       P05318; P02400: RPP2B; NbExp=2; IntAct=EBI-15452, EBI-15464;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:22096102}.
CC   -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC       {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:8476850}.
CC   -!- MISCELLANEOUS: The 4 small acidic ribosomal P-proteins from yeast can
CC       be classified into two couples of similar but not identical sequences.
CC       Each couple (P1A/P1B and P2A/P2B) is distinctly related to one of the
CC       two acidic ribosomal P-proteins P1/P2 present in multicellular
CC       organisms. {ECO:0000305|PubMed:2404943}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein P1/P2 family.
CC       {ECO:0000305}.
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DR   EMBL; X06957; CAA30027.1; -; mRNA.
DR   EMBL; X13682; CAA31976.1; -; Genomic_DNA.
DR   EMBL; D90072; BAA14113.1; -; Genomic_DNA.
DR   EMBL; M26504; AAA34733.1; -; Genomic_DNA.
DR   EMBL; Z74129; CAA98647.1; -; Genomic_DNA.
DR   EMBL; AY558526; AAS56852.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11778.1; -; Genomic_DNA.
DR   PIR; S67617; R5BY2A.
DR   RefSeq; NP_010202.1; NM_001180140.1.
DR   PDB; 4V6I; EM; 8.80 A; Bt/Bu=1-106.
DR   PDB; 5DGE; X-ray; 3.45 A; p1/p2=1-106.
DR   PDB; 5DGF; X-ray; 3.30 A; p1/p2=1-106.
DR   PDBsum; 4V6I; -.
DR   PDBsum; 5DGE; -.
DR   PDBsum; 5DGF; -.
DR   AlphaFoldDB; P05318; -.
DR   BioGRID; 31980; 478.
DR   DIP; DIP-1583N; -.
DR   IntAct; P05318; 19.
DR   MINT; P05318; -.
DR   STRING; 4932.YDL081C; -.
DR   iPTMnet; P05318; -.
DR   MaxQB; P05318; -.
DR   PaxDb; 4932-YDL081C; -.
DR   PeptideAtlas; P05318; -.
DR   EnsemblFungi; YDL081C_mRNA; YDL081C; YDL081C.
DR   GeneID; 851478; -.
DR   KEGG; sce:YDL081C; -.
DR   AGR; SGD:S000002239; -.
DR   SGD; S000002239; RPP1A.
DR   VEuPathDB; FungiDB:YDL081C; -.
DR   eggNOG; KOG1762; Eukaryota.
DR   GeneTree; ENSGT00940000170577; -.
DR   HOGENOM; CLU_114656_1_0_1; -.
DR   InParanoid; P05318; -.
DR   OMA; SMILFDG; -.
DR   OrthoDB; 26483at2759; -.
DR   BioCyc; YEAST:G3O-29490-MONOMER; -.
DR   Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 851478; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P05318; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P05318; Protein.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:SGD.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR   GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR   CDD; cd05831; Ribosomal_P1; 1.
DR   DisProt; DP00164; -.
DR   Gene3D; 1.10.10.1410; -; 1.
DR   HAMAP; MF_01478; Ribosomal_L12_arch; 1.
DR   InterPro; IPR038716; P1/P2_N_sf.
DR   InterPro; IPR027534; Ribosomal_P1/P2.
DR   PANTHER; PTHR45696; 60S ACIDIC RIBOSOMAL PROTEIN P1; 1.
DR   PANTHER; PTHR45696:SF10; 60S ACIDIC RIBOSOMAL PROTEIN P1-RELATED; 1.
DR   Pfam; PF00428; Ribosomal_60s; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10601260,
FT                   ECO:0000269|PubMed:8476850"
FT   CHAIN           2..106
FT                   /note="Large ribosomal subunit protein P1A"
FT                   /id="PRO_0000157705"
FT   REGION          73..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..97
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:10601260,
FT                   ECO:0000269|PubMed:8476850"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CONFLICT        37
FT                   /note="V -> D (in Ref. 1; CAA30027 and 2;
FT                   CAA31976/BAA14113)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   106 AA;  10908 MW;  9A2FE94D28640ACC CRC64;
     MSTESALSYA ALILADSEIE ISSEKLLTLT NAANVPVENI WADIFAKALD GQNLKDLLVN
     FSAGAAAPAG VAGGVAGGEA GEAEAEKEEE EAKEESDDDM GFGLFD
//