LCP5_YEAST
ID LCP5_YEAST Reviewed; 357 AA.
AC P40079; D3DM33;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=U3 small nucleolar ribonucleoprotein protein LCP5;
GN Name=LCP5; OrderedLocusNames=YER127W; ORFNames=SYGP-ORF43;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 CHARACTERIZATION.
RX PubMed=9814757; DOI=10.1017/s1355838298980955;
RA Wiederkehr T., Pretot R.F., Minvielle-Sebastia L.;
RT "Synthetic lethal interactions with conditional poly(A) polymerase alleles
RT identify LCP5, a gene involved in 18S rRNA maturation.";
RL RNA 4:1357-1372(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
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 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 [7]
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: Component of the U3 small nucleolar ribonucleoprotein.
CC Required for the early cleavages at sites A0, A1 and A2 of the pre-
CC ribosomal RNA. Participates in ribosome biogenesis.
CC -!- INTERACTION:
CC P40079; Q06631: BFR2; NbExp=6; IntAct=EBI-10103, EBI-36432;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC -!- MISCELLANEOUS: Present with 1430 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U18916; AAC03225.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07787.1; -; Genomic_DNA.
DR PIR; S43220; S43220.
DR RefSeq; NP_011053.1; NM_001179017.1.
DR PDB; 5WLC; EM; 3.80 A; NC=1-357.
DR PDB; 6KE6; EM; 3.40 A; RB=1-357.
DR PDB; 6LQP; EM; 3.20 A; RB=1-357.
DR PDB; 6LQQ; EM; 4.10 A; RB=1-357.
DR PDB; 6LQR; EM; 8.60 A; RB=1-357.
DR PDB; 6LQU; EM; 3.70 A; RB=1-357.
DR PDB; 6LQV; EM; 4.80 A; RB=1-357.
DR PDB; 6ZQB; EM; 3.90 A; JE=1-357.
DR PDB; 7D63; EM; 12.30 A; RB=1-357.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; P40079; -.
DR SMR; P40079; -.
DR BioGRID; 36871; 213.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-1410N; -.
DR IntAct; P40079; 22.
DR MINT; P40079; -.
DR STRING; 4932.YER127W; -.
DR iPTMnet; P40079; -.
DR MaxQB; P40079; -.
DR PaxDb; P40079; -.
DR PRIDE; P40079; -.
DR EnsemblFungi; YER127W_mRNA; YER127W; YER127W.
DR GeneID; 856864; -.
DR KEGG; sce:YER127W; -.
DR SGD; S000000929; LCP5.
DR VEuPathDB; FungiDB:YER127W; -.
DR eggNOG; KOG3117; Eukaryota.
DR GeneTree; ENSGT00500000044922; -.
DR HOGENOM; CLU_065858_0_0_1; -.
DR InParanoid; P40079; -.
DR OMA; GYGGEEW; -.
DR BioCyc; YEAST:G3O-30290-MON; -.
DR PRO; PR:P40079; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40079; protein.
DR GO; GO:0005730; C:nucleolus; IDA:GO_Central.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; TAS:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:GO_Central.
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:GO_Central.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR PANTHER; PTHR13237; PTHR13237; 1.
DR Pfam; PF04000; Sas10_Utp3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosome biogenesis; rRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..357
FT /note="U3 small nucleolar ribonucleoprotein protein LCP5"
FT /id="PRO_0000084370"
FT REGION 146..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..357
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"
SQ SEQUENCE 357 AA; 40794 MW; 77B7F3F126036489 CRC64;
MSELNALLKD INGSLTATSE SLERLSGIYS NSATDEIPES NQLHEHLFYD AKKPAEKVSL
LSLKNGSMLG YINSLLMLIG NRLDDECKDP SAMDARERSI QHRVVLERGV KPLEKKLAYQ
LDKLTRAYVK MEKEYKDAEK RALEKSTLVN HSGNDDSEDD ESSEDEIAYR PNTSGIINTN
KKSSAYRVEE TAKQENGEEN DDNETGVYKP PKITAVLPPQ QTHFEDRFDA REHKDRSNKS
RMQAMEEYIR ESSDQPDWSA SIGADIVNHG RGGIKSLRDT EKERRVTSFE EDNFTRLNIT
NKAEKRKQKQ RERNARMNVI GGEDFGIFSS KRKLEDSTSR RGAKKTRSAW DRAQRRL
