RRP1_YEAST
ID RRP1_YEAST Reviewed; 278 AA.
AC P35178; D6VS74;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ribosomal RNA-processing protein 1;
GN Name=RRP1; OrderedLocusNames=YDR087C; ORFNames=D4478;
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=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 [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] OF 146-278.
RX PubMed=8223425; DOI=10.1002/j.1460-2075.1993.tb06092.x;
RA Esnault Y., Blondel M.-O., Deshaies R.J., Schekman R., Kepes F.;
RT "The yeast SSS1 gene is essential for secretory protein translocation and
RT encodes a conserved protein of the endoplasmic reticulum.";
RL EMBO J. 12:4083-4093(1993).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10341208; DOI=10.1242/jcs.112.12.1889;
RA Savino T.M., Bastos R., Jansen E., Hernandez-Verdun D.;
RT "The nucleolar antigen Nop52, the human homologue of the yeast ribosomal
RT RNA processing RRP1, is recruited at late stages of nucleologenesis.";
RL J. Cell Sci. 112:1889-1900(1999).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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: Required for 27S rRNA processing to 25S and 5.8S.
CC -!- INTERACTION:
CC P35178; P39744: NOC2; NbExp=3; IntAct=EBI-16002, EBI-29259;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- MISCELLANEOUS: Present with 6960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RRP1 family. {ECO:0000305}.
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DR EMBL; Z46796; CAA86809.1; -; Genomic_DNA.
DR EMBL; Z74383; CAA98907.1; -; Genomic_DNA.
DR EMBL; X82086; CAA57616.1; -; Genomic_DNA.
DR EMBL; X74499; CAA52607.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11934.1; -; Genomic_DNA.
DR PIR; S48776; S48776.
DR RefSeq; NP_010372.3; NM_001180395.3.
DR PDB; 5Z3G; EM; 3.65 A; X=1-278.
DR PDB; 6C0F; EM; 3.70 A; z=1-278.
DR PDB; 6CB1; EM; 4.60 A; z=1-278.
DR PDB; 6EM1; EM; 3.60 A; 4=1-278.
DR PDB; 6EM3; EM; 3.20 A; 4=1-278.
DR PDB; 6EM4; EM; 4.10 A; 4=1-278.
DR PDB; 6EM5; EM; 4.30 A; 4=1-278.
DR PDB; 7OHS; EM; 4.38 A; 4=1-278.
DR PDB; 7OHW; EM; 3.50 A; 4=1-278.
DR PDB; 7OHX; EM; 3.30 A; 4=1-278.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR AlphaFoldDB; P35178; -.
DR SMR; P35178; -.
DR BioGRID; 32143; 469.
DR DIP; DIP-4622N; -.
DR IntAct; P35178; 18.
DR MINT; P35178; -.
DR STRING; 4932.YDR087C; -.
DR iPTMnet; P35178; -.
DR MaxQB; P35178; -.
DR PaxDb; P35178; -.
DR PRIDE; P35178; -.
DR EnsemblFungi; YDR087C_mRNA; YDR087C; YDR087C.
DR GeneID; 851660; -.
DR KEGG; sce:YDR087C; -.
DR SGD; S000002494; RRP1.
DR VEuPathDB; FungiDB:YDR087C; -.
DR eggNOG; KOG3911; Eukaryota.
DR GeneTree; ENSGT00390000011821; -.
DR HOGENOM; CLU_022876_0_2_1; -.
DR InParanoid; P35178; -.
DR OMA; MWFSDRP; -.
DR BioCyc; YEAST:G3O-29692-MON; -.
DR PRO; PR:P35178; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P35178; protein.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR InterPro; IPR010301; RRP1-like.
DR PANTHER; PTHR13026; PTHR13026; 1.
DR Pfam; PF05997; Nop52; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; rRNA processing.
FT CHAIN 1..278
FT /note="Ribosomal RNA-processing protein 1"
FT /id="PRO_0000097452"
FT REGION 255..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 15..30
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 39..54
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 95..109
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 177..183
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 278 AA; 33203 MW; 7E906A028ADAE8A6 CRC64;
METSNFVKQL SSNNRKTRVN ALEALKKYLT AKQFKENKQI EFNKLWKGLY YAMWFSDRPR
PQQRLANELG ELHGLYFDPK DNSTADELTT NDKAFIKFSR GFWKVMCFEW FNIDRYRLDK
YLLLIRRVLF SQLKYLQSRN WDKKLVDEYI KKVLRWLPLS GSPKVYTGIP IHIVDILLDE
WERLLKDGDE DDEDEENKEE EMRKIAESAK KTPLADVIAI FQDIVADYNN SKVLREKIKE
DLFSDTRLVS WDILEGETQH NDSSNESEEE EEEEWKGF
