SIL1_YEAST
ID SIL1_YEAST Reviewed; 421 AA.
AC Q08199; D6W234; Q6B1H9;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Nucleotide exchange factor SIL1;
DE AltName: Full=Protein SLS1;
DE Flags: Precursor;
GN Name=SIL1; Synonyms=PER100, SLS1; OrderedLocusNames=YOL031C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INDUCTION.
RX PubMed=10847680; DOI=10.1016/s0092-8674(00)80835-1;
RA Travers K.J., Patil C.K., Wodicka L., Lockhart D.J., Weissman J.S.,
RA Walter P.;
RT "Functional and genomic analyses reveal an essential coordination between
RT the unfolded protein response and ER-associated degradation.";
RL Cell 101:249-258(2000).
RN [5]
RP FUNCTION, AND INTERACTION WITH KAR2.
RX PubMed=11101517; DOI=10.1093/emboj/19.23.6440;
RA Tyson J.R., Stirling C.J.;
RT "LHS1 and SIL1 provide a lumenal function that is essential for protein
RT translocation into the endoplasmic reticulum.";
RL EMBO J. 19:6440-6452(2000).
RN [6]
RP FUNCTION, INTERACTION WITH KAR2, AND MUTAGENESIS OF 365-PHE--LEU-369.
RX PubMed=10958688; DOI=10.1128/mcb.20.18.6923-6934.2000;
RA Kabani M., Beckerich J.-M., Gaillardin C.;
RT "Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-
RT dependent manner in the yeast endoplasmic reticulum.";
RL Mol. Cell. Biol. 20:6923-6934(2000).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, AND INTERACTION WITH KAR2.
RX PubMed=14704430; DOI=10.1126/science.1092287;
RA Steel G.J., Fullerton D.M., Tyson J.R., Stirling C.J.;
RT "Coordinated activation of Hsp70 chaperones.";
RL Science 303:98-101(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
CC -!- FUNCTION: Required for protein translocation and folding in the
CC endoplasmic reticulum (ER). Functions as a nucleotide exchange factor
CC for the ER lumenal chaperone KAR2. {ECO:0000269|PubMed:10958688,
CC ECO:0000269|PubMed:11101517, ECO:0000269|PubMed:14704430}.
CC -!- SUBUNIT: Interacts with KAR2. {ECO:0000269|PubMed:10958688,
CC ECO:0000269|PubMed:11101517, ECO:0000269|PubMed:14704430}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- INDUCTION: By the unfolded protein response (UPR).
CC {ECO:0000269|PubMed:10847680}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
CC -!- MISCELLANEOUS: Present with 2420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SIL1 family. {ECO:0000305}.
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DR EMBL; Z74773; CAA99031.1; -; Genomic_DNA.
DR EMBL; AY693101; AAT93120.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10750.1; -; Genomic_DNA.
DR PIR; S66714; S66714.
DR RefSeq; NP_014611.1; NM_001183285.1.
DR PDB; 3QML; X-ray; 2.31 A; C/D=113-421.
DR PDBsum; 3QML; -.
DR AlphaFoldDB; Q08199; -.
DR SMR; Q08199; -.
DR BioGRID; 34369; 133.
DR DIP; DIP-2622N; -.
DR IntAct; Q08199; 6.
DR MINT; Q08199; -.
DR STRING; 4932.YOL031C; -.
DR iPTMnet; Q08199; -.
DR MaxQB; Q08199; -.
DR PaxDb; Q08199; -.
DR PRIDE; Q08199; -.
DR EnsemblFungi; YOL031C_mRNA; YOL031C; YOL031C.
DR GeneID; 854126; -.
DR KEGG; sce:YOL031C; -.
DR SGD; S000005391; SIL1.
DR VEuPathDB; FungiDB:YOL031C; -.
DR eggNOG; KOG2160; Eukaryota.
DR HOGENOM; CLU_034955_0_0_1; -.
DR InParanoid; Q08199; -.
DR OMA; GLDIRMN; -.
DR BioCyc; YEAST:G3O-33447-MON; -.
DR PRO; PR:Q08199; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08199; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR031884; Sil1_fungi.
DR Pfam; PF16782; SIL1; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycoprotein; Protein transport;
KW Reference proteome; Signal; Translocation; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..421
FT /note="Nucleotide exchange factor SIL1"
FT /id="PRO_0000223364"
FT MOTIF 418..421
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 215
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 365..369
FT /note="Missing: Abrogates interaction with KAR2."
FT /evidence="ECO:0000269|PubMed:10958688"
FT CONFLICT 51
FT /note="I -> T (in Ref. 3; AAT93120)"
FT /evidence="ECO:0000305"
FT HELIX 127..139
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 165..184
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 241..253
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:3QML"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 338..355
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 356..358
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 363..380
FT /evidence="ECO:0007829|PDB:3QML"
FT HELIX 389..402
FT /evidence="ECO:0007829|PDB:3QML"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:3QML"
SQ SEQUENCE 421 AA; 48275 MW; 4F6677F5029B6209 CRC64;
MVRILPIILS ALSSKLVAST ILHSSIHSVP SGGEIISAED LKELEISGNS ICVDNRCYPK
IFEPRHDWQP ILPGQELPGG LDIRINMDTG LKEAKLNDEK NVGDNGSHEL IVSSEDMKAS
PGDYEFSSDF KEMRNIIDSN PTLSSQDIAR LEDSFDRIME FAHDYKHGYK IITHEFALLA
NLSLNENLPL TLRELSTRVI TSCLRNNPPV VEFINESFPN FKSKIMAALS NLNDSNHRSS
NILIKRYLSI LNELPVTSED LPIYSTVVLQ NVYERNNKDK QLQIKVLELI SKILKADMYE
NDDTNLILFK RNAENWSSNL QEWANEFQEM VQNKSIDELH TRTFFDTLYN LKKIFKSDIT
INKGFLNWLA QQCKARQSNL DNGLQERDTE QDSFDKKLID SRHLIFGNPM AHRIKNFRDE
L
