LRP1_YEAST
ID LRP1_YEAST Reviewed; 184 AA.
AC P38801; D3DL32;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Exosome complex protein LRP1;
DE AltName: Full=Like an rRNA processing protein 1;
DE AltName: Full=Yeast C1D domain-containing protein;
DE AltName: Full=rRNA processing protein 47;
GN Name=LRP1; Synonyms=RRP47, YC1D; OrderedLocusNames=YHR081W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 SUBCELLULAR LOCATION.
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [4]
RP FUNCTION.
RX PubMed=12421302; DOI=10.1046/j.1365-2958.2002.03224.x;
RA Erdemir T., Bilican B., Cagatay T., Goding C.R., Yavuzer U.;
RT "Saccharomyces cerevisiae C1D is implicated in both non-homologous DNA end
RT joining and homologous recombination.";
RL Mol. Microbiol. 46:947-957(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH RRP45 AND RRP46.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [6]
RP FUNCTION, INTERACTION WITH RRP4 AND RRP6, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12972615; DOI=10.1128/mcb.23.19.6982-6992.2003;
RA Mitchell P., Petfalski E., Houalla R., Podtelejnikov A., Mann M.,
RA Tollervey D.;
RT "Rrp47p is an exosome-associated protein required for the 3' processing of
RT stable RNAs.";
RL Mol. Cell. Biol. 23:6982-6992(2003).
RN [7]
RP FUNCTION, INTERACTION RRP6, AND SUBCELLULAR LOCATION.
RX PubMed=15489286; DOI=10.1101/gad.1241204;
RA Hieronymus H., Yu M.C., Silver P.A.;
RT "Genome-wide mRNA surveillance is coupled to mRNA export.";
RL Genes Dev. 18:2652-2662(2004).
RN [8]
RP FUNCTION.
RX PubMed=15161972; DOI=10.1073/pnas.0401263101;
RA Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C.,
RA Krauskopf A., Kupiec M., McEachern M.J.;
RT "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that
RT affect telomere length.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004).
RN [9]
RP IDENTIFICATION BY MASS 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 exosome-dependent processing of pre-rRNA and
CC small nucleolar RNA (snRNA) precursors. Involved in processing of 35S
CC pre-rRNA at the A0, A1 and A2 sites. Required for activity of RRP6 in
CC 7S pre-rRNA processing. Also has a role in 3'-processing of U4 and U5
CC small nuclear RNAs (snRNAs). Acts as a mRNA export factor. Mediates
CC mRNA degradation upon UV irradiation. Maintains genome integrity where
CC it is involved in both non-homologous end joining (NHEJ) and homologous
CC recombination pathway repair of double strand DNA breaks. During NHEJ,
CC required for joining 3'-overhanging ends. Also involved in telomere
CC length regulation and maintenance. {ECO:0000269|PubMed:12421302,
CC ECO:0000269|PubMed:12837249, ECO:0000269|PubMed:12972615,
CC ECO:0000269|PubMed:15161972, ECO:0000269|PubMed:15489286}.
CC -!- SUBUNIT: Associated with nuclear form of the RNA exosome complex.
CC Interacts with RRP4, RRP6, RRP45 and RRP46.
CC {ECO:0000269|PubMed:12837249, ECO:0000269|PubMed:12972615,
CC ECO:0000269|PubMed:15489286}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11914276,
CC ECO:0000269|PubMed:12972615, ECO:0000269|PubMed:15489286}.
CC -!- SIMILARITY: Belongs to the C1D family. {ECO:0000305}.
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DR EMBL; U10556; AAB68886.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06776.1; -; Genomic_DNA.
DR PIR; S46808; S46808.
DR RefSeq; NP_011949.1; NM_001179211.1.
DR PDB; 4WFC; X-ray; 2.35 A; B/D/F=1-133.
DR PDB; 4WFD; X-ray; 2.40 A; B/E/H=1-103.
DR PDB; 5C0W; X-ray; 4.60 A; L=1-184.
DR PDB; 6FSZ; EM; 4.60 A; LL=1-184.
DR PDB; 6FT6; EM; 3.90 A; LL=1-184.
DR PDB; 6LQS; EM; 3.80 A; R7=1-184.
DR PDB; 7D4I; EM; 4.00 A; R7=1-184.
DR PDBsum; 4WFC; -.
DR PDBsum; 4WFD; -.
DR PDBsum; 5C0W; -.
DR PDBsum; 6FSZ; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 7D4I; -.
DR AlphaFoldDB; P38801; -.
DR SMR; P38801; -.
DR BioGRID; 36516; 467.
DR DIP; DIP-4359N; -.
DR IntAct; P38801; 8.
DR MINT; P38801; -.
DR STRING; 4932.YHR081W; -.
DR MaxQB; P38801; -.
DR PaxDb; P38801; -.
DR PRIDE; P38801; -.
DR EnsemblFungi; YHR081W_mRNA; YHR081W; YHR081W.
DR GeneID; 856481; -.
DR KEGG; sce:YHR081W; -.
DR SGD; S000001123; LRP1.
DR VEuPathDB; FungiDB:YHR081W; -.
DR eggNOG; KOG4835; Eukaryota.
DR HOGENOM; CLU_101423_1_0_1; -.
DR InParanoid; P38801; -.
DR OMA; FQGTHTK; -.
DR BioCyc; YEAST:G3O-31128-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P38801; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38801; protein.
DR GO; GO:0000178; C:exosome (RNase complex); IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:SGD.
DR GO; GO:0030234; F:enzyme regulator activity; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0071028; P:nuclear mRNA surveillance; IMP:SGD.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IMP:SGD.
DR GO; GO:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:1901917; P:regulation of exoribonuclease activity; IDA:SGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:SGD.
DR GO; GO:0034476; P:U5 snRNA 3'-end processing; IMP:SGD.
DR DisProt; DP00788; -.
DR InterPro; IPR011082; Exosome-assoc_fac/DNA_repair.
DR InterPro; IPR007146; Sas10/Utp3/C1D.
DR PANTHER; PTHR15341; PTHR15341; 1.
DR Pfam; PF04000; Sas10_Utp3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Exosome; Nucleus; Reference proteome; RNA-binding;
KW rRNA processing.
FT CHAIN 1..184
FT /note="Exosome complex protein LRP1"
FT /id="PRO_0000202902"
FT REGION 157..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..184
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 8..28
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 43..67
FT /evidence="ECO:0007829|PDB:4WFC"
FT HELIX 74..119
FT /evidence="ECO:0007829|PDB:4WFC"
SQ SEQUENCE 184 AA; 21045 MW; 27D00668C296CC9A CRC64;
MEDIEKIKPY VRSFSKALDE LKPEIEKLTS KSLDEQLLLL SDERAKLELI NRYAYVLSSL
MFANMKVLGV KDMSPILGEL KRVKSYMDKA KQYDNRITKS NEKSQAEQEK AKNIISNVLD
GNKNQFEPSI SRSNFQGKHT KFENDELAES TTTKIIDSTD HIRKASSKKS KRLDKVGKKK
GGKK
