ID   SIL1_ASHGO              Reviewed;         383 AA.
AC   Q758U2;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Nucleotide exchange factor SIL1;
DE   Flags: Precursor;
GN   Name=SIL1; OrderedLocusNames=AEL340W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with KAR2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SIL1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016818; AAS52344.1; -; Genomic_DNA.
DR   RefSeq; NP_984520.1; NM_209873.1.
DR   AlphaFoldDB; Q758U2; -.
DR   SMR; Q758U2; -.
DR   STRING; 33169.AAS52344; -.
DR   EnsemblFungi; AAS52344; AAS52344; AGOS_AEL340W.
DR   GeneID; 4620690; -.
DR   KEGG; ago:AGOS_AEL340W; -.
DR   eggNOG; KOG2160; Eukaryota.
DR   HOGENOM; CLU_034955_0_0_1; -.
DR   InParanoid; Q758U2; -.
DR   OMA; GLDIRMN; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR031884; Sil1_fungi.
DR   Pfam; PF16782; SIL1; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Protein transport; Reference proteome; Signal;
KW   Translocation; Transport.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..383
FT                   /note="Nucleotide exchange factor SIL1"
FT                   /id="PRO_0000223359"
FT   MOTIF           380..383
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   383 AA;  43998 MW;  BDC81E26AEB71D67 CRC64;
     MYWKKLLFAI ASAAALAAVD PETEGSELQT ICSGGECYPR LFKALQDWST IKEGQQIPPG
     LDIRVDLSTG KKQARLPIPN EASNMENGIQ VVDDSSDYEF TKEFQLVRAQ VASGAPDYNV
     VIKQLDDLVE YASDYTLGYK IITHEFTLLQ ELIFGQDVPI SVKELSSRII VACLRNNTPC
     LDFVNTRFPD FVRHLLQEAV DYGRQATDAV EARTQIKRYL SIVEPLLINE PQPINEEALK
     QLYEVNDQTV QLKVLLIMAR LYKGRSHNDD ISKRSLESTD VQRWTTELSK AIQSKHLDDF
     HVRELFHGLY ALKKEHGRAV KTYPTFLGWL AEETEARKQR MTQDKQPRDL EQMEFDRLLI
     ESRHMVFGNP MAHRIKNMEY DEL