RLP7_YEAST
ID RLP7_YEAST Reviewed; 322 AA.
AC P40693; D6W1H5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Ribosome biogenesis protein RLP7;
DE AltName: Full=Ribosomal protein L7-like;
GN Name=RLP7; Synonyms=RPL7; OrderedLocusNames=YNL002C; ORFNames=N2014;
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=S288c / GRF88;
RX PubMed=8402262;
RA Lalo D., Stettler S., Mariotte S., Slonimski P.P., Thuriaux P.;
RT "Two yeast chromosomes are related by a fossil duplication of their
RT centromeric regions.";
RL C. R. Acad. Sci. III, Sci. Vie 316:367-373(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=8256515; DOI=10.1002/yea.320091007;
RA Lalo D., Mariotte S., Thuriaux P.;
RT "Two distinct yeast proteins are related to the mammalian ribosomal
RT polypeptide L7.";
RL Yeast 9:1085-1091(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / GRF88;
RX PubMed=7941739; DOI=10.1002/yea.320100412;
RA Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.;
RT "Organization of the centromeric region of chromosome XIV in Saccharomyces
RT cerevisiae.";
RL Yeast 10:523-533(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7985421; DOI=10.1002/yea.320100709;
RA Verhasselt P., Aert R., Voet M., Volckaert G.;
RT "Nucleotide sequence analysis of an 8887 bp region of the left arm of yeast
RT chromosome XIV, encompassing the centromere sequence.";
RL Yeast 10:945-951(1994).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11087857; DOI=10.1073/pnas.97.24.13027;
RA Dunbar D.A., Dragon F., Lee S.J., Baserga S.J.;
RT "A nucleolar protein related to ribosomal protein L7 is required for an
RT early step in large ribosomal subunit biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13027-13032(2000).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-120 AND SER-278, AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120, 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May
CC act as a specificity factor that binds precursor rRNAs and tethers the
CC enzymes that carry out the early 5' to 3' exonucleolytic reactions that
CC generate the mature rRNAs. {ECO:0000269|PubMed:11087857}.
CC -!- INTERACTION:
CC P40693; P38779: CIC1; NbExp=3; IntAct=EBI-15415, EBI-24538;
CC P40693; P32892: DRS1; NbExp=3; IntAct=EBI-15415, EBI-6170;
CC P40693; Q03532: HAS1; NbExp=3; IntAct=EBI-15415, EBI-8170;
CC P40693; Q12176: MAK21; NbExp=3; IntAct=EBI-15415, EBI-10944;
CC P40693; P38112: MAK5; NbExp=3; IntAct=EBI-15415, EBI-10394;
CC P40693; P39744: NOC2; NbExp=3; IntAct=EBI-15415, EBI-29259;
CC P40693; Q02892: NOG1; NbExp=3; IntAct=EBI-15415, EBI-12105;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11087857}.
CC -!- MISCELLANEOUS: Present with 7720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC {ECO:0000305}.
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DR EMBL; L19167; AAA34982.1; -; Genomic_DNA.
DR EMBL; X77114; CAA54376.1; -; Genomic_DNA.
DR EMBL; Z71278; CAA95861.1; -; Genomic_DNA.
DR EMBL; AY693031; AAT93050.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10541.1; -; Genomic_DNA.
DR PIR; S38194; S38194.
DR RefSeq; NP_014396.3; NM_001182841.3.
DR PDB; 3JCT; EM; 3.08 A; t=1-322.
DR PDB; 4V7F; EM; 8.70 A; r/s=1-322.
DR PDB; 5Z3G; EM; 3.65 A; D=1-322.
DR PDB; 6C0F; EM; 3.70 A; t=1-322.
DR PDB; 6CB1; EM; 4.60 A; t=1-322.
DR PDB; 6ELZ; EM; 3.30 A; t=1-322.
DR PDB; 6EM1; EM; 3.60 A; t=1-322.
DR PDB; 6EM3; EM; 3.20 A; t=1-322.
DR PDB; 6EM4; EM; 4.10 A; t=1-322.
DR PDB; 6EM5; EM; 4.30 A; t=1-322.
DR PDB; 6M62; EM; 3.20 A; t=1-322.
DR PDB; 6YLX; EM; 3.90 A; t=1-322.
DR PDB; 6YLY; EM; 3.80 A; t=1-322.
DR PDB; 7BTB; EM; 3.22 A; t=1-322.
DR PDB; 7OHP; EM; 3.90 A; t=1-322.
DR PDB; 7OHQ; EM; 3.10 A; t=1-322.
DR PDB; 7OHR; EM; 4.72 A; t=1-322.
DR PDB; 7OHS; EM; 4.38 A; t=1-322.
DR PDB; 7OHV; EM; 3.90 A; t=1-322.
DR PDB; 7OHW; EM; 3.50 A; t=1-322.
DR PDB; 7OHX; EM; 3.30 A; t=1-322.
DR PDBsum; 3JCT; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; P40693; -.
DR SMR; P40693; -.
DR BioGRID; 35823; 450.
DR DIP; DIP-6476N; -.
DR IntAct; P40693; 42.
DR MINT; P40693; -.
DR STRING; 4932.YNL002C; -.
DR iPTMnet; P40693; -.
DR MaxQB; P40693; -.
DR PaxDb; P40693; -.
DR PRIDE; P40693; -.
DR EnsemblFungi; YNL002C_mRNA; YNL002C; YNL002C.
DR GeneID; 855730; -.
DR KEGG; sce:YNL002C; -.
DR SGD; S000004947; RLP7.
DR VEuPathDB; FungiDB:YNL002C; -.
DR eggNOG; KOG3184; Eukaryota.
DR GeneTree; ENSGT00950000182878; -.
DR HOGENOM; CLU_055156_1_0_1; -.
DR InParanoid; P40693; -.
DR OMA; CMEDIIH; -.
DR BioCyc; YEAST:G3O-33044-MON; -.
DR PRO; PR:P40693; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40693; protein.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0000465; P:exonucleolytic trimming to generate mature 5'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:SGD.
DR CDD; cd01657; Ribosomal_L7_archeal_euk; 1.
DR Gene3D; 3.30.1390.20; -; 1.
DR InterPro; IPR036919; L30_ferredoxin-like_sf.
DR InterPro; IPR018038; Ribosomal_L30_CS.
DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR InterPro; IPR039699; Ribosomal_L7/L30.
DR InterPro; IPR035808; Ribosomal_L7_euk_arc.
DR PANTHER; PTHR11524; PTHR11524; 1.
DR Pfam; PF00327; Ribosomal_L30; 1.
DR SUPFAM; SSF55129; SSF55129; 1.
DR PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..322
FT /note="Ribosome biogenesis protein RLP7"
FT /id="PRO_0000104658"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 278
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT HELIX 58..86
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 282..298
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 322 AA; 36559 MW; 64714DDFAFB90B5D CRC64;
MSSTQDSKAQ TLNSNPEILL RKRRNADRTR IERQELAKKK REEQIKKKRS NKNKFVRAES
IVAKTLATSR EKERIKRVSI LEDKKAKNET QHIASGKDFI LKITEKANGA EENSVDLEET
EEEEDDGLIR EKTTYDGKPA LLFIVRVRGP LAVNIPNKAF KILSLLRLVE TNTGVFVKLT
KNVYPLLKVI APYVVIGKPS LSSIRSLIQK RGRIIYKGEN EAEPHEIVLN DNNIVEEQLG
DHGIICVEDI IHEIATMGES FSVCNFFLQP FKLNREVSGF GSLNRLRKIK QREAESRTRQ
FSNAATAPVI EVDIDSLLAK LN
