Skip Header

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

P48240

- MTR3_YEAST

UniProt

P48240 - MTR3_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 MTR3

Gene

MTR3

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. MTR3 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation.3 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. nonfunctional rRNA decay Source: SGD
  3. nuclear mRNA surveillance Source: SGD
  4. nuclear polyadenylation-dependent CUT catabolic process Source: SGD
  5. nuclear polyadenylation-dependent mRNA catabolic process Source: SGD
  6. nuclear polyadenylation-dependent rRNA catabolic process Source: SGD
  7. nuclear polyadenylation-dependent tRNA catabolic process Source: SGD
  8. nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay Source: SGD
  9. nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' Source: SGD
  10. nuclear-transcribed mRNA catabolic process, non-stop decay Source: SGD
  11. polyadenylation-dependent snoRNA 3'-end processing Source: SGD
  12. U4 snRNA 3'-end processing Source: SGD
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30858-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Exosome complex component MTR3
Alternative name(s):
mRNA transport regulator 3
Gene namesi
Name:MTR3
Ordered Locus Names:YGR158C
ORF Names:G6676
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR158c.
SGDiS000003390. MTR3.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Exosome complex component MTR3PRO_0000139979Add
BLAST

Proteomic databases

MaxQBiP48240.
PaxDbiP48240.
PeptideAtlasiP48240.

Expressioni

Gene expression databases

GenevestigatoriP48240.

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CSL4P538598EBI-1749,EBI-1731
RRP42Q122773EBI-1749,EBI-1765
SKI6P469484EBI-1749,EBI-1788
YLR345WQ061373EBI-1749,EBI-33827

Protein-protein interaction databases

BioGridi33406. 29 interactions.
DIPiDIP-931N.
IntActiP48240. 25 interactions.
MINTiMINT-409300.
STRINGi4932.YGR158C.

Structurei

Secondary structure

1
250
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Beta strandi45 – 506Combined sources
Beta strandi56 – 6611Combined sources
Beta strandi69 – 8214Combined sources
Beta strandi92 – 998Combined sources
Helixi107 – 12115Combined sources
Turni122 – 1243Combined sources
Helixi127 – 1293Combined sources
Beta strandi133 – 14614Combined sources
Helixi164 – 1674Combined sources
Helixi169 – 18315Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi192 – 1965Combined sources
Beta strandi199 – 2046Combined sources
Helixi205 – 2073Combined sources
Beta strandi209 – 2157Combined sources
Helixi223 – 24725Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IFDX-ray2.80F1-250[»]
4OO1X-ray3.30F1-250[»]
ProteinModelPortaliP48240.
SMRiP48240. Positions 4-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi216 – 2227Asp/Glu-rich (acidic)

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

eggNOGiCOG0689.
HOGENOMiHOG000113690.
InParanoidiP48240.
KOiK12587.
OMAiMNVQDRR.
OrthoDBiEOG776T1F.

Family and domain databases

InterProiIPR001247. ExoRNase_PH_dom1.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PfamiPF01138. RNase_PH. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.

Sequencei

Sequence statusi: Complete.

P48240-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNVQDRRRLL GPAAAKPMAF SNTTTHVPEK KSTDLTPKGN ESEQELSLHT
60 70 80 90 100
GFIENCNGSA LVEARSLGHQ TSLITAVYGP RSIRGSFTSQ GTISIQLKNG
110 120 130 140 150
LLEKYNTNEL KEVSSFLMGI FNSVVNLSRY PKSGIDIFVY LTYDKDLTNN
160 170 180 190 200
PQDDDSQSKM MSSQISSLIP HCITSITLAL ADAGIELVDM AGAGEANGTV
210 220 230 240 250
VSFIKNGEEI VGFWKDDGDD EDLLECLDRC KEQYNRYRDL MISCLMNQET
Length:250
Mass (Da):27,577
Last modified:February 1, 1996 - v1
Checksum:i2FA07ABB4A1115E0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85807 Genomic DNA. Translation: CAA59815.1.
S80548 Genomic DNA. Translation: AAB35850.1.
Z72943 Genomic DNA. Translation: CAA97172.1.
BK006941 Genomic DNA. Translation: DAA08249.1.
PIRiS58362.
RefSeqiNP_011674.3. NM_001181287.3.

Genome annotation databases

EnsemblFungiiYGR158C; YGR158C; YGR158C.
GeneIDi853062.
KEGGisce:YGR158C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X85807 Genomic DNA. Translation: CAA59815.1 .
S80548 Genomic DNA. Translation: AAB35850.1 .
Z72943 Genomic DNA. Translation: CAA97172.1 .
BK006941 Genomic DNA. Translation: DAA08249.1 .
PIRi S58362.
RefSeqi NP_011674.3. NM_001181287.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IFD X-ray 2.80 F 1-250 [» ]
4OO1 X-ray 3.30 F 1-250 [» ]
ProteinModelPortali P48240.
SMRi P48240. Positions 4-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33406. 29 interactions.
DIPi DIP-931N.
IntActi P48240. 25 interactions.
MINTi MINT-409300.
STRINGi 4932.YGR158C.

Proteomic databases

MaxQBi P48240.
PaxDbi P48240.
PeptideAtlasi P48240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR158C ; YGR158C ; YGR158C .
GeneIDi 853062.
KEGGi sce:YGR158C.

Organism-specific databases

CYGDi YGR158c.
SGDi S000003390. MTR3.

Phylogenomic databases

eggNOGi COG0689.
HOGENOMi HOG000113690.
InParanoidi P48240.
KOi K12587.
OMAi MNVQDRR.
OrthoDBi EOG776T1F.

Enzyme and pathway databases

BioCyci YEAST:G3O-30858-MONOMER.

Miscellaneous databases

NextBioi 973001.

Gene expression databases

Genevestigatori P48240.

Family and domain databases

InterProi IPR001247. ExoRNase_PH_dom1.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
Pfami PF01138. RNase_PH. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of a 27 kb segment on the right arm of chromosome VII from Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2, NSR1 genes and ten new open reading frames."
    Skala J., Nawrocki A., Goffeau A.
    Yeast 11:1421-1427(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Mutations in nucleolar proteins lead to nucleolar accumulation of polyA+ RNA in Saccharomyces cerevisiae."
    Kadowaki T., Schneiter R., Hitomi M., Tartakoff A.M.
    Mol. Biol. Cell 6:1103-1110(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "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 RNA EXOSOME COMPLEX BY MASS SPECTROMETRY.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "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.
  9. Erratum
    Liu Q., Greimann J.C., Lima C.D.
    Cell 131:188-189(2007)
  10. "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 nameiMTR3_YEAST
AccessioniPrimary (citable) accession number: P48240
Secondary accession number(s): D6VUT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7380 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