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Protein

Protein SLM4

Gene

SLM4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the GSE complex, a GTPase complex required for intracellular sorting of GAP1 out of the endosome. Component of the EGO complex, a complex involved in the regulation of microautophagy.2 Publications

GO - Biological processi

  • lysosomal microautophagy Source: SGD
  • protein transport Source: UniProtKB-KW
  • signal transduction Source: SGD
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29045-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SLM4
Alternative name(s):
EGO complex subunit 3
GSE complex subunit 1
Gene namesi
Name:SLM4
Synonyms:EGO3, GSE1
Ordered Locus Names:YBR077C
ORF Names:YBR0723
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR077C.
SGDiS000000281. SLM4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei127 – 14418HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • EGO complex Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • late endosome membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 162162Protein SLM4PRO_0000202479Add
BLAST

Proteomic databases

MaxQBiP38247.

Interactioni

Subunit structurei

Component of the GSE complex composed of GTR1, GTR2, SLM4, MEH1 and LTV1. Component of the EGO complex, at least composed of GTR2, SLM4 and MEH1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MEH1Q022054EBI-21507,EBI-27062

Protein-protein interaction databases

BioGridi32779. 75 interactions.
DIPiDIP-1763N.
IntActiP38247. 5 interactions.
MINTiMINT-397651.

Structurei

Secondary structure

1
162
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 179Combined sources
Helixi22 – 243Combined sources
Beta strandi33 – 397Combined sources
Turni40 – 423Combined sources
Beta strandi45 – 506Combined sources
Beta strandi53 – 553Combined sources
Helixi59 – 8426Combined sources
Beta strandi92 – 1009Combined sources
Beta strandi103 – 11210Combined sources
Beta strandi115 – 1217Combined sources
Beta strandi125 – 13410Combined sources
Helixi139 – 15012Combined sources
Helixi151 – 1566Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LGOX-ray2.85A1-162[»]
4FTXX-ray2.10A/B1-162[»]
4FUWX-ray2.60A/B1-162[»]
4XPMX-ray2.40C1-162[»]
ProteinModelPortaliP38247.
SMRiP38247. Positions 5-162.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38247.

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000000722.
InParanoidiP38247.
OMAiHTCVAQI.
OrthoDBiEOG783N7H.

Family and domain databases

InterProiIPR020233. Slm4.
[Graphical view]
PfamiPF16818. SLM4. 1 hit.
[Graphical view]
ProDomiPD095317. GSE/EGO_complex_su-SLM4. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P38247-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMLHSKNVK GFLENTLKPY DLHSVDFKTS SLQSSMIITA TNGGILSYAT
60 70 80 90 100
SNNDVPKNSI NEINSVNNLK MMSLLIKDKW SEDENDTEEQ HSNSCYPVEI
110 120 130 140 150
DSFKTKIYTY EMEDLHTCVA QIPNSDLLLL FIAEGSFPYG LLVIKIERAM
160
RELTDLFGYK LG
Length:162
Mass (Da):18,354
Last modified:October 1, 1994 - v1
Checksum:iD64ABDE1CDF265FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76294 Genomic DNA. Translation: CAA53934.1.
Z35946 Genomic DNA. Translation: CAA85021.1.
BK006936 Genomic DNA. Translation: DAA07196.1.
PIRiS45472.
RefSeqiNP_009633.3. NM_001178425.3.

Genome annotation databases

EnsemblFungiiYBR077C; YBR077C; YBR077C.
GeneIDi852369.
KEGGisce:YBR077C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76294 Genomic DNA. Translation: CAA53934.1.
Z35946 Genomic DNA. Translation: CAA85021.1.
BK006936 Genomic DNA. Translation: DAA07196.1.
PIRiS45472.
RefSeqiNP_009633.3. NM_001178425.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LGOX-ray2.85A1-162[»]
4FTXX-ray2.10A/B1-162[»]
4FUWX-ray2.60A/B1-162[»]
4XPMX-ray2.40C1-162[»]
ProteinModelPortaliP38247.
SMRiP38247. Positions 5-162.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32779. 75 interactions.
DIPiDIP-1763N.
IntActiP38247. 5 interactions.
MINTiMINT-397651.

Proteomic databases

MaxQBiP38247.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR077C; YBR077C; YBR077C.
GeneIDi852369.
KEGGisce:YBR077C.

Organism-specific databases

EuPathDBiFungiDB:YBR077C.
SGDiS000000281. SLM4.

Phylogenomic databases

HOGENOMiHOG000000722.
InParanoidiP38247.
OMAiHTCVAQI.
OrthoDBiEOG783N7H.

Enzyme and pathway databases

BioCyciYEAST:G3O-29045-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38247.
PROiP38247.

Family and domain databases

InterProiIPR020233. Slm4.
[Graphical view]
PfamiPF16818. SLM4. 1 hit.
[Graphical view]
ProDomiPD095317. GSE/EGO_complex_su-SLM4. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 31 kb DNA fragment from the right arm of Saccharomyces cerevisiae chromosome II."
    van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M., Steensma H.Y.
    Yeast 10:959-964(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "The TOR and EGO protein complexes orchestrate microautophagy in yeast."
    Dubouloz F., Deloche O., Wanke V., Cameroni E., De Virgilio C.
    Mol. Cell 19:15-26(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE EGO COMPLEX, SUBCELLULAR LOCATION.
  7. "A conserved GTPase-containing complex is required for intracellular sorting of the general amino-acid permease in yeast."
    Gao M., Kaiser C.A.
    Nat. Cell Biol. 8:657-667(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE GSE COMPLEX.
  8. "Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals."
    Kogan K., Spear E.D., Kaiser C.A., Fass D.
    J. Mol. Biol. 402:388-398(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), INTERACTION WITH MEH1.

Entry informationi

Entry nameiSLM4_YEAST
AccessioniPrimary (citable) accession number: P38247
Secondary accession number(s): D6VQ76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 8, 2016
This is version 110 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 3490 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.