ID   SIL1_YARLI              Reviewed;         426 AA.
AC   Q99158; Q6C3R5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Nucleotide exchange factor SIL1;
DE   AltName: Full=Protein SLS1;
DE   Flags: Precursor;
GN   Name=SIL1; Synonyms=SLS1; OrderedLocusNames=YALI0E32703g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 20460 / W29 / CBS 7504 / IFP29;
RX   PubMed=8662639; DOI=10.1074/jbc.271.20.11668;
RA   Boisrame A., Beckerich J.-M., Gaillardin C.;
RT   "Sls1p, an endoplasmic reticulum component, is involved in the protein
RT   translocation process in the yeast Yarrowia lipolytica.";
RL   J. Biol. Chem. 271:11668-11675(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH KAR2, AND MUTAGENESIS OF 382-PHE--ASP-387.
RX   PubMed=9812983; DOI=10.1074/jbc.273.47.30903;
RA   Boisrame A., Kabani M., Beckerich J.-M., Hartmann E., Gaillardin C.;
RT   "Interaction of Kar2p and Sls1p is required for efficient co-translational
RT   translocation of secreted proteins in the yeast Yarrowia lipolytica.";
RL   J. Biol. Chem. 273:30903-30908(1998).
CC   -!- FUNCTION: Required for protein translocation and folding in the
CC       endoplasmic reticulum (ER). Probably functions as a nucleotide exchange
CC       factor for the ER lumenal chaperone KAR2. It is not required for
CC       viability but is essential for optimal growth at elevated temperatures.
CC       {ECO:0000269|PubMed:8662639, ECO:0000269|PubMed:9812983}.
CC   -!- SUBUNIT: Interacts with KAR2. {ECO:0000269|PubMed:9812983}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138, ECO:0000269|PubMed:8662639}.
CC   -!- INDUCTION: By the unfolded protein response (UPR).
CC       {ECO:0000269|PubMed:8662639}.
CC   -!- SIMILARITY: Belongs to the SIL1 family. {ECO:0000305}.
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DR   EMBL; Z50154; CAA90516.1; -; Genomic_DNA.
DR   EMBL; CR382131; CAG80301.1; -; Genomic_DNA.
DR   PIR; S58132; S58132.
DR   RefSeq; XP_504697.1; XM_504697.1.
DR   AlphaFoldDB; Q99158; -.
DR   SMR; Q99158; -.
DR   IntAct; Q99158; 1.
DR   MINT; Q99158; -.
DR   STRING; 4952.CAG80301; -.
DR   EnsemblFungi; CAG80301; CAG80301; YALI0_E32703g.
DR   GeneID; 2911792; -.
DR   KEGG; yli:YALI0E32703g; -.
DR   VEuPathDB; FungiDB:YALI0_E32703g; -.
DR   HOGENOM; CLU_034955_0_0_1; -.
DR   InParanoid; Q99158; -.
DR   OMA; GLDIRMN; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR031884; Sil1_fungi.
DR   Pfam; PF16782; SIL1; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Protein transport; Reference proteome; Signal;
KW   Translocation; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..426
FT                   /note="Nucleotide exchange factor SIL1"
FT                   /id="PRO_0000032596"
FT   MOTIF           423..426
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   MUTAGEN         382..387
FT                   /note="FLEWLD->YY: Abrogates interaction with KAR2."
FT                   /evidence="ECO:0000269|PubMed:9812983"
FT   CONFLICT        323
FT                   /note="T -> K (in Ref. 1; CAA90516)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   426 AA;  47174 MW;  EB475653FF712BF1 CRC64;
     MKFSKTLLLA LVAGALAKGE DEICRVEKNS GKEICYPKVF VPTEEWQVVW PDQVIPAGLH
     VRMDYENGVK EAKINDPNEE VEGVAVAVGE EVPEGEVVIE DLTEENGDEG ISANEKVQRA
     IEKAIKEKRI KEGHKPNPNI PESDHQTFSD AVAALRDYKV NGQAAMLPIA LSQLEELSHE
     IDFGIALSDV DPLNALLQIL EDAKVDVESK IMAARTIGAS LRNNPHALDK VINSKVDLVK
     SLLDDLAQSS KEKADKLSSS LVYALSAVLK TPETVTRFVD LHGGDTLRQL YETGSDDVKG
     RVSTLIEDVL ATPDLHNDFS SITGAVKKRS ANWWEDELKE WSGVFQRSLP SKLSSKVKSK
     VYTSLAAIRR NFRESVDVSE EFLEWLDHPK KAAAEIGDDL VKLIKQDRGE LWGNAKARKY
     DARDEL