Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P53256

- RRP46_YEAST

UniProt

P53256 - RRP46_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Exosome complex component RRP46

Gene

RRP46

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP46 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.2 Publications

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  2. ncRNA 3'-end processing Source: SGD
  3. nonfunctional rRNA decay Source: SGD
  4. nuclear polyadenylation-dependent mRNA catabolic process Source: SGD
  5. nuclear polyadenylation-dependent rRNA catabolic process Source: SGD
  6. nuclear polyadenylation-dependent tRNA catabolic process Source: SGD
  7. nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay Source: SGD
  8. nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' Source: SGD
  9. nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
  10. polyadenylation-dependent snoRNA 3'-end processing Source: SGD
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30805-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component RRP46
Alternative name(s):
Ribosomal RNA-processing protein 46
Gene namesi
Name:RRP46
Ordered Locus Names:YGR095C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR095c.
SGDiS000003327. RRP46.

Subcellular locationi

Cytoplasm 1 Publication. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytoplasmic exosome (RNase complex) Source: SGD
  2. nuclear exosome (RNase complex) Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Exosome complex component RRP46PRO_0000139978Add
BLAST

Proteomic databases

MaxQBiP53256.
PaxDbiP53256.
PeptideAtlasiP53256.

Expressioni

Gene expression databases

GenevestigatoriP53256.

Interactioni

Subunit structurei

Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which associates with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. Interacts with LRP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSL4P538597EBI-1842,EBI-1731
DIS3Q081626EBI-1842,EBI-1740
SKI6P469485EBI-1842,EBI-1788

Protein-protein interaction databases

BioGridi33338. 32 interactions.
DIPiDIP-6838N.
IntActiP53256. 23 interactions.
MINTiMINT-2732969.
STRINGi4932.YGR095C.

Structurei

Secondary structure

1
223
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi11 – 2111Combined sources
Beta strandi24 – 3411Combined sources
Turni38 – 403Combined sources
Beta strandi43 – 5311Combined sources
Beta strandi55 – 573Combined sources
Helixi61 – 7717Combined sources
Helixi80 – 823Combined sources
Beta strandi86 – 9611Combined sources
Turni101 – 1033Combined sources
Helixi106 – 12318Combined sources
Beta strandi127 – 13913Combined sources
Turni140 – 1423Combined sources
Beta strandi145 – 1484Combined sources
Helixi151 – 1555Combined sources
Beta strandi157 – 16812Combined sources
Turni169 – 1724Combined sources
Beta strandi173 – 18614Combined sources
Helixi188 – 21730Combined sources
Turni218 – 2203Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IFDX-ray2.80D1-223[»]
4OO1X-ray3.30D1-223[»]
ProteinModelPortaliP53256.
SMRiP53256. Positions 1-223.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG0689.
GeneTreeiENSGT00550000075002.
HOGENOMiHOG000248419.
InParanoidiP53256.
KOiK12590.
OMAiRRDEHAY.
OrthoDBiEOG7C8GTX.

Family and domain databases

Gene3Di3.30.230.70. 1 hit.
InterProiIPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.

Sequencei

Sequence statusi: Complete.

P53256-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVQAEIGIL DHVDGSSEFV SQDTKVICSV TGPIEPKARQ ELPTQLALEI
60 70 80 90 100
IVRPAKGVAT TREKVLEDKL RAVLTPLITR HCYPRQLCQI TCQILESGED
110 120 130 140 150
EAEFSLRELS CCINAAFLAL VDAGIALNSM CASIPIAIIK DTSDIIVDPT
160 170 180 190 200
AEQLKISLSV HTLALEFVNG GKVVKNVLLL DSNGDFNEDQ LFSLLELGEQ
210 220
KCQELVTNIR RIIQDNISPR LVV
Length:223
Mass (Da):24,407
Last modified:October 31, 2006 - v2
Checksum:iF1307E0EE4FC3133
GO

Sequence cautioni

The sequence CAA97098.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72880 Genomic DNA. Translation: CAA97098.1. Different initiation.
AY389297 mRNA. Translation: AAQ97229.1.
BK006941 Genomic DNA. Translation: DAA08188.1.
PIRiS64390.
RefSeqiNP_011609.2. NM_001181224.1.

Genome annotation databases

EnsemblFungiiYGR095C; YGR095C; YGR095C.
GeneIDi852987.
KEGGisce:YGR095C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72880 Genomic DNA. Translation: CAA97098.1 . Different initiation.
AY389297 mRNA. Translation: AAQ97229.1 .
BK006941 Genomic DNA. Translation: DAA08188.1 .
PIRi S64390.
RefSeqi NP_011609.2. NM_001181224.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IFD X-ray 2.80 D 1-223 [» ]
4OO1 X-ray 3.30 D 1-223 [» ]
ProteinModelPortali P53256.
SMRi P53256. Positions 1-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33338. 32 interactions.
DIPi DIP-6838N.
IntActi P53256. 23 interactions.
MINTi MINT-2732969.
STRINGi 4932.YGR095C.

Proteomic databases

MaxQBi P53256.
PaxDbi P53256.
PeptideAtlasi P53256.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR095C ; YGR095C ; YGR095C .
GeneIDi 852987.
KEGGi sce:YGR095C.

Organism-specific databases

CYGDi YGR095c.
SGDi S000003327. RRP46.

Phylogenomic databases

eggNOGi COG0689.
GeneTreei ENSGT00550000075002.
HOGENOMi HOG000248419.
InParanoidi P53256.
KOi K12590.
OMAi RRDEHAY.
OrthoDBi EOG7C8GTX.

Enzyme and pathway databases

BioCyci YEAST:G3O-30805-MONOMER.

Miscellaneous databases

NextBioi 972806.
PROi P53256.

Gene expression databases

Genevestigatori P53256.

Family and domain databases

Gene3Di 3.30.230.70. 1 hit.
InterProi IPR001247. ExoRNase_PH_dom1.
IPR015847. ExoRNase_PH_dom2.
IPR027408. PNPase/RNase_PH_dom.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
Pfami PF01138. RNase_PH. 1 hit.
PF03725. RNase_PH_C. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55666. SSF55666. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Kennedy M.C., Dietrich F.S.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-67.
    Strain: ATCC 204511 / S288c / AB972.
  4. "The yeast exosome and human PM-Scl are related complexes of 3'-->5' exonucleases."
    Allmang C., Petfalski E., Podtelejnikov A., Mann M., Tollervey D., Mitchell P.
    Genes Dev. 13:2148-2158(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE EXOSOME COMPLEX BY MASS SPECTROMETRY.
  5. Cited for: INTERACTION WITH LRP1.
  6. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Reconstitution, activities, and structure of the eukaryotic RNA exosome."
    Liu Q., Greimann J.C., Lima C.D.
    Cell 127:1223-1237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF THE RNA EXOSOME COMPLEX, LACK OF EXONUCLEASE ACTIVITY.
  10. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2007)
  11. "A single subunit, Dis3, is essentially responsible for yeast exosome core activity."
    Dziembowski A., Lorentzen E., Conti E., Seraphin B.
    Nat. Struct. Mol. Biol. 14:15-22(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE RNA EXOSOME COMPLEX, SUBUNIT.

Entry informationi

Entry nameiRRP46_YEAST
AccessioniPrimary (citable) accession number: P53256
Secondary accession number(s): D6VUM7, Q6TQU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 31, 2006
Last modified: October 29, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 10800 molecules/cell in log phase SD medium.1 Publication

Caution

According to PubMed:17173052 and PubMed:17174896, only DIS3/RRP44 subunit of the exosome core has exonuclease activity.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3