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Protein

U6 snRNA-associated Sm-like protein LSm7

Gene

LSM7

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

Functioni

Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by activating the decapping step. Component of the nuclear LSM2-LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 snRNP, spliceosomal U4/U6.U5 snRNP, and free U6 snRNP). It binds directly to the U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. It probably also is involved in degradation of nuclear pre-mRNA by targeting them for decapping. LSM7 binds specifically to the 3'-terminal U-tract of U6 snRNA. LSM2-LSM8 probably is involved in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA. LSM7, probably in a complex that contains LSM2-LSM7 but not LSM1 or LSM8, associates with the precursor of the RNA component of RNase P (pre-P RNA) and may be involved in maturing pre-P RNA.5 Publications

Miscellaneous

Present with 3070 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

GO - Biological processi

  • maturation of SSU-rRNA Source: SGD
  • mRNA splicing, via spliceosome Source: SGD
  • nuclear-transcribed mRNA catabolic process Source: SGD
  • tRNA processing Source: UniProtKB-KW

Keywordsi

Molecular functionRibonucleoprotein, RNA-binding
Biological processmRNA processing, mRNA splicing, rRNA processing, tRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-33165-MONOMER
ReactomeiR-SCE-430039 mRNA decay by 5' to 3' exoribonuclease

Names & Taxonomyi

Protein namesi
Recommended name:
U6 snRNA-associated Sm-like protein LSm7
Gene namesi
Name:LSM7
Ordered Locus Names:YNL147W
ORF Names:N1202, N1780
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL147W
SGDiS000005091 LSM7

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, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95R → A: Slightly reduces affinity for poly-U RNA ends. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001255811 – 115U6 snRNA-associated Sm-like protein LSm7Add BLAST115

Proteomic databases

MaxQBiP53905
PaxDbiP53905
PRIDEiP53905

Interactioni

Subunit structurei

Component of the heptameric LSM1-LSM7 complex that forms a seven-membered ring structure with a doughnut shape. The LSm subunits are arranged in the order LSM1, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. Except for LSM1, where a C-terminal helix crosses the ring structure to form additional interactions with LSM3 and LSM6, each subunit interacts only with its two neighboring subunits. The LSM1-LSM7 complex interacts with PAT1; within the complex PAT1 has direct interactions with LSM2 and LSM3. Component of the heptameric LSM2-LSM8 complex that forms a seven-membered ring structure with a doughnut shape; an RNA strand can pass through the hole in the center of the ring structure. The LSm subunits are arranged in the order LSM8, LSM2, LSM3, LSM6, LSM5, LSM7 and LSM4. LSM2-LSM8 associates with PAT1 and XRN1. A complex comprising LSM2-LSM7 without LSM1 or LSM8 may exist. Component of the spliceosome U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRP3, PRP4, PRP6, PRP8, PRP18, PRP31, PRP38, SNU13, SNU23, SNU66, SNU114, SPP381, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, LSM2, LSM3, LSM4, LSM5, LSM6, LSM7, LSM8, BRR2 and DIB1.6 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi35681, 749 interactors
ComplexPortaliCPX-112 Lsm1-7-Pat1 complex
CPX-24 U6 snRNP complex
CPX-25 U4/U6.U5 tri-snRNP complex
CPX-32 U4/U6 snRNP
CPX-44 LSM2-8 complex
CPX-45 LSM1-7 complex
CPX-46 LSM2-7 complex
DIPiDIP-1419N
IntActiP53905, 26 interactors
MINTiP53905
STRINGi4932.YNL147W

Structurei

Secondary structure

1115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 33Combined sources4
Beta strandi36 – 42Combined sources7
Turni43 – 45Combined sources3
Beta strandi47 – 55Combined sources9
Beta strandi61 – 69Combined sources9
Beta strandi86 – 94Combined sources9
Helixi96 – 98Combined sources3
Beta strandi99 – 105Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JCMelectron microscopy3.80g1-115[»]
4C8QX-ray3.70G1-115[»]
4C92X-ray2.30G1-115[»]
4M75X-ray2.95F/M1-115[»]
4M77X-ray3.11F/M1-115[»]
4M78X-ray2.79F/M1-115[»]
4M7AX-ray2.78F/M1-115[»]
4M7DX-ray2.60F/M1-115[»]
5GANelectron microscopy3.6071-115[»]
5NRLelectron microscopy7.2071-115[»]
5VSUX-ray3.10G1-115[»]
6ASOX-ray2.71G1-115[»]
ProteinModelPortaliP53905
SMRiP53905
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

GeneTreeiENSGT00510000047872
HOGENOMiHOG000223548
InParanoidiP53905
KOiK12626
OMAiGPKREAI
OrthoDBiEOG092C5VL3

Family and domain databases

CDDicd01729 LSm7, 1 hit
InterProiView protein in InterPro
IPR017132 Lsm7
IPR001163 LSM_dom_euk/arc
IPR010920 LSM_dom_sf
PfamiView protein in Pfam
PF01423 LSM, 1 hit
SMARTiView protein in SMART
SM00651 Sm, 1 hit
SUPFAMiSSF50182 SSF50182, 1 hit

Sequencei

Sequence statusi: Complete.

P53905-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHQQHSKSEN KPQQQRKKFE GPKREAILDL AKYKDSKIRV KLMGGKLVIG
60 70 80 90 100
VLKGYDQLMN LVLDDTVEYM SNPDDENNTE LISKNARKLG LTVIRGTILV
110
SLSSAEGSDV LYMQK
Length:115
Mass (Da):13,006
Last modified:June 26, 2007 - v2
Checksum:iEA1D019FC5D1B5C5
GO

Sequence cautioni

The sequence CAA86879 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAA96030 differs from that shown. Reason: Erroneous gene model prediction.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46843 Genomic DNA Translation: CAA86879.1 Sequence problems.
Z71423 Genomic DNA Translation: CAA96030.1 Sequence problems.
BK006947 Genomic DNA Translation: DAA10401.1
PIRiS55137
RefSeqiNP_014252.2, NM_001182985.1

Genome annotation databases

EnsemblFungiiYNL147W; YNL147W; YNL147W
GeneIDi855575
KEGGisce:YNL147W

Similar proteinsi

Entry informationi

Entry nameiLSM7_YEAST
AccessioniPrimary (citable) accession number: P53905
Secondary accession number(s): D6W135
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 26, 2007
Last modified: June 20, 2018
This is version 157 of the entry and version 2 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

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