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Q08199 (SIL1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleotide exchange factor SIL1
Alternative name(s):
Protein SLS1
Gene names
Name:SIL1
Synonyms:PER100, SLS1
Ordered Locus Names:YOL031C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone KAR2. Ref.5 Ref.6 Ref.8

Subunit structure

Interacts with KAR2. Ref.5 Ref.6 Ref.8

Subcellular location

Endoplasmic reticulum lumen.

Induction

By the unfolded protein response (UPR). Ref.4

Post-translational modification

N-glycosylated.

Miscellaneous

Present with 2420 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SIL1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KAR2P164741EBI-38850,EBI-7876

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 421402Nucleotide exchange factor SIL1
PRO_0000223364

Regions

Motif418 – 4214Prevents secretion from ER Potential

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1811N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis365 – 3695Missing: Abrogates interaction with KAR2. Ref.6
Sequence conflict511I → T in AAT93120. Ref.3

Secondary structure

............................... 421
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08199 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4F6677F5029B6209

FASTA42148,275
        10         20         30         40         50         60 
MVRILPIILS ALSSKLVAST ILHSSIHSVP SGGEIISAED LKELEISGNS ICVDNRCYPK 

        70         80         90        100        110        120 
IFEPRHDWQP ILPGQELPGG LDIRINMDTG LKEAKLNDEK NVGDNGSHEL IVSSEDMKAS 

       130        140        150        160        170        180 
PGDYEFSSDF KEMRNIIDSN PTLSSQDIAR LEDSFDRIME FAHDYKHGYK IITHEFALLA 

       190        200        210        220        230        240 
NLSLNENLPL TLRELSTRVI TSCLRNNPPV VEFINESFPN FKSKIMAALS NLNDSNHRSS 

       250        260        270        280        290        300 
NILIKRYLSI LNELPVTSED LPIYSTVVLQ NVYERNNKDK QLQIKVLELI SKILKADMYE 

       310        320        330        340        350        360 
NDDTNLILFK RNAENWSSNL QEWANEFQEM VQNKSIDELH TRTFFDTLYN LKKIFKSDIT 

       370        380        390        400        410        420 
INKGFLNWLA QQCKARQSNL DNGLQERDTE QDSFDKKLID SRHLIFGNPM AHRIKNFRDE 


L 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]"Coordinated activation of Hsp70 chaperones."
Steel G.J., Fullerton D.M., Tyson J.R., Stirling C.J.
Science 303:98-101(2004) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74773 Genomic DNA. Translation: CAA99031.1.
AY693101 Genomic DNA. Translation: AAT93120.1.
BK006948 Genomic DNA. Translation: DAA10750.1.
PIRS66714.
RefSeqNP_014611.1. NM_001183285.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QMLX-ray2.31C/D113-421[»]
ProteinModelPortalQ08199.
SMRQ08199. Positions 125-406.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid34369. 61 interactions.
DIPDIP-2622N.
IntActQ08199. 6 interactions.
MINTMINT-558162.
STRING4932.YOL031C.

Proteomic databases

PaxDbQ08199.
PeptideAtlasQ08199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL031C; YOL031C; YOL031C.
GeneID854126.
KEGGsce:YOL031C.

Organism-specific databases

CYGDYOL031c.
SGDS000005391. SIL1.

Phylogenomic databases

eggNOGNOG244873.
HOGENOMHOG000154325.
KOK14001.
OMASHDIEFG.
OrthoDBEOG7V1G2Q.

Enzyme and pathway databases

BioCycYEAST:G3O-33447-MONOMER.

Gene expression databases

GenevestigatorQ08199.

Family and domain databases

PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975837.

Entry information

Entry nameSIL1_YEAST
AccessionPrimary (citable) accession number: Q08199
Secondary accession number(s): D6W234, Q6B1H9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XV

Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references