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Q08199

- SIL1_YEAST

UniProt

Q08199 - SIL1_YEAST

Protein

Nucleotide exchange factor SIL1

Gene

SIL1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2.3 Publications

    GO - Molecular functioni

    1. adenyl-nucleotide exchange factor activity Source: SGD

    GO - Biological processi

    1. regulation of catalytic activity Source: GOC
    2. SRP-dependent cotranslational protein targeting to membrane, translocation Source: SGD

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33447-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleotide exchange factor SIL1
    Alternative name(s):
    Protein SLS1
    Gene namesi
    Name:SIL1
    Synonyms:PER100, SLS1
    Ordered Locus Names:YOL031C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL031c.
    SGDiS000005391. SIL1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: SGD
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi365 – 3695Missing: Abrogates interaction with KAR2. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 421402Nucleotide exchange factor SIL1PRO_0000223364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    N-glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ08199.
    PaxDbiQ08199.
    PeptideAtlasiQ08199.

    Expressioni

    Inductioni

    By the unfolded protein response (UPR).1 Publication

    Gene expression databases

    GenevestigatoriQ08199.

    Interactioni

    Subunit structurei

    Interacts with KAR2.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KAR2P164741EBI-38850,EBI-7876

    Protein-protein interaction databases

    BioGridi34369. 61 interactions.
    DIPiDIP-2622N.
    IntActiQ08199. 6 interactions.
    MINTiMINT-558162.
    STRINGi4932.YOL031C.

    Structurei

    Secondary structure

    1
    421
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi127 – 13913
    Helixi145 – 15814
    Helixi159 – 1613
    Helixi165 – 18420
    Helixi190 – 20415
    Helixi208 – 21710
    Helixi221 – 23313
    Helixi241 – 25313
    Helixi266 – 27510
    Turni276 – 2783
    Helixi280 – 29718
    Helixi321 – 33111
    Helixi338 – 35518
    Helixi356 – 3583
    Helixi363 – 38018
    Helixi389 – 40214
    Turni403 – 4053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QMLX-ray2.31C/D113-421[»]
    ProteinModelPortaliQ08199.
    SMRiQ08199. Positions 125-406.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi418 – 4214Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the SIL1 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG244873.
    HOGENOMiHOG000154325.
    KOiK14001.
    OMAiSHDIEFG.
    OrthoDBiEOG7V1G2Q.

    Family and domain databases

    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q08199-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVRILPIILS ALSSKLVAST ILHSSIHSVP SGGEIISAED LKELEISGNS    50
    ICVDNRCYPK IFEPRHDWQP ILPGQELPGG LDIRINMDTG LKEAKLNDEK 100
    NVGDNGSHEL IVSSEDMKAS PGDYEFSSDF KEMRNIIDSN PTLSSQDIAR 150
    LEDSFDRIME FAHDYKHGYK IITHEFALLA NLSLNENLPL TLRELSTRVI 200
    TSCLRNNPPV VEFINESFPN FKSKIMAALS NLNDSNHRSS NILIKRYLSI 250
    LNELPVTSED LPIYSTVVLQ NVYERNNKDK QLQIKVLELI SKILKADMYE 300
    NDDTNLILFK RNAENWSSNL QEWANEFQEM VQNKSIDELH TRTFFDTLYN 350
    LKKIFKSDIT INKGFLNWLA QQCKARQSNL DNGLQERDTE QDSFDKKLID 400
    SRHLIFGNPM AHRIKNFRDE L 421
    Length:421
    Mass (Da):48,275
    Last modified:November 1, 1996 - v1
    Checksum:i4F6677F5029B6209
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511I → T in AAT93120. (PubMed:17322287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74773 Genomic DNA. Translation: CAA99031.1.
    AY693101 Genomic DNA. Translation: AAT93120.1.
    BK006948 Genomic DNA. Translation: DAA10750.1.
    PIRiS66714.
    RefSeqiNP_014611.1. NM_001183285.1.

    Genome annotation databases

    EnsemblFungiiYOL031C; YOL031C; YOL031C.
    GeneIDi854126.
    KEGGisce:YOL031C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z74773 Genomic DNA. Translation: CAA99031.1 .
    AY693101 Genomic DNA. Translation: AAT93120.1 .
    BK006948 Genomic DNA. Translation: DAA10750.1 .
    PIRi S66714.
    RefSeqi NP_014611.1. NM_001183285.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QML X-ray 2.31 C/D 113-421 [» ]
    ProteinModelPortali Q08199.
    SMRi Q08199. Positions 125-406.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34369. 61 interactions.
    DIPi DIP-2622N.
    IntActi Q08199. 6 interactions.
    MINTi MINT-558162.
    STRINGi 4932.YOL031C.

    Proteomic databases

    MaxQBi Q08199.
    PaxDbi Q08199.
    PeptideAtlasi Q08199.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL031C ; YOL031C ; YOL031C .
    GeneIDi 854126.
    KEGGi sce:YOL031C.

    Organism-specific databases

    CYGDi YOL031c.
    SGDi S000005391. SIL1.

    Phylogenomic databases

    eggNOGi NOG244873.
    HOGENOMi HOG000154325.
    KOi K14001.
    OMAi SHDIEFG.
    OrthoDBi EOG7V1G2Q.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33447-MONOMER.

    Miscellaneous databases

    NextBioi 975837.

    Gene expression databases

    Genevestigatori Q08199.

    Family and domain databases

    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation."
      Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S., Walter P.
      Cell 101:249-258(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    5. "LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum."
      Tyson J.R., Stirling C.J.
      EMBO J. 19:6440-6452(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KAR2.
    6. "Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum."
      Kabani M., Beckerich J.-M., Gaillardin C.
      Mol. Cell. Biol. 20:6923-6934(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KAR2, MUTAGENESIS OF 365-PHE--LEU-369.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. Cited for: FUNCTION, INTERACTION WITH KAR2.
    9. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
      Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
      Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSIL1_YEAST
    AccessioniPrimary (citable) accession number: Q08199
    Secondary accession number(s): D6W234, Q6B1H9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 93 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 2420 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. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3