P38801 (LRP1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	184 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7.
Sequence similarities	Belongs to the C1D family.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Exosome Nucleus
Ligand	RNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	U4 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 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_component	nuclear exosome (RNase complex) Inferred from direct assay PubMed 19046973. Source: SGD
Molecular_function	double-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 184	184	Exosome complex protein LRP1		PRO_0000202902

Sequences

	Sequence		Length	Mass (Da)
	P38801 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 27D00668C296CC9A	FASTA	184	21,045
	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

References

	« Hide 'large scale' referencesShow '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. , 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 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. , 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: MASS SPECTROMETRY, FUNCTION, INTERACTION WITH RRP4 AND RRP6, SUCELLULAR LOCATION.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U10556 Genomic DNA. Translation: AAB68886.1. BK006934 Genomic DNA. Translation: DAA06776.1.
PIR	S46808.
RefSeq	NP_011949.1. NM_001179211.1.
3D structure databases
ProteinModelPortal	P38801.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4359N.
IntAct	P38801. 7 interactions.
MINT	MINT-499454.
STRING	4932.YHR081W.
Proteomic databases
PaxDb	P38801.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YHR081W; YHR081W; YHR081W.
GeneID	856481.
KEGG	sce:YHR081W.
Organism-specific databases
CYGD	YHR081w.
SGD	S000001123. LRP1.
Phylogenomic databases
eggNOG	NOG315595.
HOGENOM	HOG000000879.
KO	K12592.
OMA	FQGKHTK.
OrthoDB	EOG4ZPJ4T.
Enzyme and pathway databases
BioCyc	YEAST:G3O-31128-MONOMER.
Gene expression databases
Genevestigator	P38801.
GermOnline	YHR081W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011082. Exosome-assoc_fac/DNA_repair. IPR007146. Sas10/Utp3/C1D. [Graphical view]
PANTHER	PTHR15341. PTHR15341. 1 hit.
Pfam	PF04000. Sas10_Utp3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	982167.

Entry information

Entry name

LRP1_YEAST

Accession

Primary (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 29, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program