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P38801 (LRP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exosome complex protein LRP1
Alternative name(s):
Like an rRNA processing protein 1
Yeast C1D domain-containing protein
rRNA processing protein 47
Gene names
Name:LRP1
Synonyms:RRP47, YC1D
Ordered Locus Names:YHR081W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites. Required for activity of RRP6 in 7S pre-rRNA processing. Also has a role in 3'-processing of U4 and U5 small nuclear RNAs (snRNAs). Acts as a mRNA export factor. Mediates mRNA degradation upon UV irradiation. Maintains genome integrity where it is involved in both non-homologous end joining (NHEJ) and homologous recombination pathway repair of double strand DNA breaks. During NHEJ, required for joining 3'-overhanging ends. Also involved in telomere length regulation and maintenance. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subunit structure

Associated with nuclear form of the RNA exosome complex. Interacts with RRP4, RRP6, RRP45 and RRP46. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus Ref.3 Ref.6 Ref.7.

Sequence similarities

Belongs to the C1D family.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentExosome
Nucleus
   LigandRNA-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processU4 snRNA 3'-end processing

Inferred from mutant phenotype Ref.6. Source: SGD

U5 snRNA 3'-end processing

Inferred from mutant phenotype Ref.6. Source: SGD

exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from mutant phenotype Ref.6. Source: SGD

nuclear mRNA surveillance

Inferred from mutant phenotype PubMed 16652390. Source: SGD

nuclear polyadenylation-dependent CUT catabolic process

Inferred from mutant phenotype PubMed 16973436PubMed 18591258. Source: SGD

nuclear polyadenylation-dependent rRNA catabolic process

Inferred from mutant phenotype Ref.6. Source: SGD

nuclear retention of pre-mRNA at the site of transcription

Inferred from genetic interaction PubMed 17410208. Source: SGD

polyadenylation-dependent snoRNA 3'-end processing

Inferred from mutant phenotype Ref.6. Source: SGD

posttranscriptional tethering of RNA polymerase II gene DNA at nuclear periphery

Inferred from mutant phenotype PubMed 18614049. Source: SGD

   Cellular_componentexosome (RNase complex)

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay PubMed 23580640. Source: SGD

   Molecular_functiondouble-stranded DNA binding

Inferred from direct assay PubMed 17704127. Source: SGD

double-stranded RNA binding

Inferred from direct assay PubMed 17704127. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Exosome complex protein LRP1
PRO_0000202902

Sequences

Sequence LengthMass (Da)Tools
P38801 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 27D00668C296CC9A

FASTA18421,045
        10         20         30         40         50         60 
MEDIEKIKPY VRSFSKALDE LKPEIEKLTS KSLDEQLLLL SDERAKLELI NRYAYVLSSL 

        70         80         90        100        110        120 
MFANMKVLGV KDMSPILGEL KRVKSYMDKA KQYDNRITKS NEKSQAEQEK AKNIISNVLD 

       130        140        150        160        170        180 
GNKNQFEPSI SRSNFQGKHT KFENDELAES TTTKIIDSTD HIRKASSKKS KRLDKVGKKK 


GGKK 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII."
Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. expand/collapse author list , Louis E.J., Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R., Vaudin M.
Science 265:2077-2082(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Subcellular localization of the yeast proteome."
Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S., Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P., Gerstein M., Roeder G.S., Snyder M.
Genes Dev. 16:707-719(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[4]"Saccharomyces cerevisiae C1D is implicated in both non-homologous DNA end joining and homologous recombination."
Erdemir T., Bilican B., Cagatay T., Goding C.R., Yavuzer U.
Mol. Microbiol. 46:947-957(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"A panoramic view of yeast noncoding RNA processing."
Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G., Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N., Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P., Beattie B. expand/collapse author list , Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A., Greenblatt J.F., Hughes T.R.
Cell 113:919-933(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RRP45 AND RRP46.
[6]"Rrp47p is an exosome-associated protein required for the 3' processing of stable RNAs."
Mitchell P., Petfalski E., Houalla R., Podtelejnikov A., Mann M., Tollervey D.
Mol. Cell. Biol. 23:6982-6992(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RRP4 AND RRP6, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"Genome-wide mRNA surveillance is coupled to mRNA export."
Hieronymus H., Yu M.C., Silver P.A.
Genes Dev. 18:2652-2662(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION RRP6, SUBCELLULAR LOCATION.
[8]"A genome-wide screen for Saccharomyces cerevisiae deletion mutants that affect telomere length."
Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C., Krauskopf A., Kupiec M., McEachern M.J.
Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10556 Genomic DNA. Translation: AAB68886.1.
BK006934 Genomic DNA. Translation: DAA06776.1.
PIRS46808.
RefSeqNP_011949.1. NM_001179211.1.

3D structure databases

ProteinModelPortalP38801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36516. 261 interactions.
DIPDIP-4359N.
IntActP38801. 7 interactions.
MINTMINT-499454.
STRING4932.YHR081W.

Proteomic databases

MaxQBP38801.
PaxDbP38801.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYHR081W; YHR081W; YHR081W.
GeneID856481.
KEGGsce:YHR081W.

Organism-specific databases

CYGDYHR081w.
SGDS000001123. LRP1.

Phylogenomic databases

eggNOGNOG315595.
HOGENOMHOG000000879.
KOK12592.
OMAFENDELA.
OrthoDBEOG7RFTW7.

Enzyme and pathway databases

BioCycYEAST:G3O-31128-MONOMER.

Gene expression databases

GenevestigatorP38801.

Family and domain databases

InterProIPR011082. Exosome-assoc_fac/DNA_repair.
IPR007146. Sas10/Utp3/C1D.
[Graphical view]
PANTHERPTHR15341. PTHR15341. 1 hit.
PfamPF04000. Sas10_Utp3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982167.
PROP38801.

Entry information

Entry nameLRP1_YEAST
AccessionPrimary (citable) accession number: P38801
Secondary accession number(s): D3DL32
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families