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Protein

Exosome complex component MTR3

Gene

MTR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

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

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processrRNA processing

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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR158C
SGDiS000003390 MTR3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Exosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001399791 – 250Exosome complex component MTR3Add BLAST250

Proteomic databases

MaxQBiP48240
PaxDbiP48240
PRIDEiP48240

PTM databases

iPTMnetiP48240

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

Protein-protein interaction databases

BioGridi33406, 105 interactors
ComplexPortaliCPX-599 Nuclear/nucleolar exosome complex, DIS3-RRP6 variant
CPX-603 Cytoplasmic exosome complex, DIS3 variant
DIPiDIP-931N
IntActiP48240, 25 interactors
MINTiP48240
STRINGi4932.YGR158C

Structurei

Secondary structure

1250
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP48240
SMRiP48240
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi216 – 222Asp/Glu-rich (acidic)7

Sequence similaritiesi

Belongs to the RNase PH family.Curated

Phylogenomic databases

HOGENOMiHOG000113690
InParanoidiP48240
KOiK12587
OMAiIFGPRPI
OrthoDBiEOG092C4NRQ

Family and domain databases

Gene3Di3.30.230.70, 1 hit
InterProiView protein in InterPro
IPR001247 ExoRNase_PH_dom1
IPR027408 PNPase/RNase_PH_dom_sf
IPR020568 Ribosomal_S5_D2-typ_fold
PfamiView protein in Pfam
PF01138 RNase_PH, 1 hit
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:
EMBLi
GenBanki
DDBJi
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

Similar proteinsi

Entry informationi

Entry nameiMTR3_YEAST
AccessioniPrimary (citable) accession number: P48240
Secondary accession number(s): D6VUT8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 12, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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