ID   SIL1_CANAL              Reviewed;         414 AA.
AC   Q5A360; A0A1D8PTR0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Nucleotide exchange factor SIL1;
DE   Flags: Precursor;
GN   Name=SIL1; OrderedLocusNames=CAALFM_CR08350WA;
GN   ORFNames=CaO19.13761, CaO19.6403;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- SIMILARITY: Belongs to the SIL1 family. {ECO:0000305}.
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DR   EMBL; CP017630; AOW31516.1; -; Genomic_DNA.
DR   RefSeq; XP_716242.1; XM_711149.1.
DR   AlphaFoldDB; Q5A360; -.
DR   SMR; Q5A360; -.
DR   STRING; 237561.Q5A360; -.
DR   GlyCosmos; Q5A360; 2 sites, No reported glycans.
DR   EnsemblFungi; CR_08350W_A-T; CR_08350W_A-T-p1; CR_08350W_A.
DR   GeneID; 3642082; -.
DR   KEGG; cal:CAALFM_CR08350WA; -.
DR   CGD; CAL0000176393; orf19.13761.
DR   VEuPathDB; FungiDB:CR_08350W_A; -.
DR   eggNOG; KOG2160; Eukaryota.
DR   HOGENOM; CLU_034955_0_0_1; -.
DR   InParanoid; Q5A360; -.
DR   OrthoDB; 67078at2759; -.
DR   PRO; PR:Q5A360; -.
DR   Proteomes; UP000000559; Chromosome R.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR031884; Sil1_fungi.
DR   PANTHER; PTHR19316:SF35; NUCLEOTIDE EXCHANGE FACTOR SIL1; 1.
DR   PANTHER; PTHR19316; PROTEIN FOLDING REGULATOR; 1.
DR   Pfam; PF16782; SIL1; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Protein transport; Reference proteome;
KW   Signal; Translocation; Transport.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..414
FT                   /note="Nucleotide exchange factor SIL1"
FT                   /id="PRO_0000223360"
FT   MOTIF           411..414
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   CARBOHYD        17
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  47067 MW;  E907BBD67BBC2E3C CRC64;
     MKFSVLVLLA SYLVGVNSSI VDTSEELICP DPENPLDCYP KLFVPTNEWQ TIKPGQDIPP
     GLHVRLNIDT LEKEAKLMSA DEKDEPVQEV VVGGELQDHS REAITENLQK LHESKHPEVK
     QEHAHRTKVS QGDLSNFDAA CSEIESFKPH ESDVERLHLA LDTLEELSHD IEFGVKLTSD
     KAIFQSLVNI ANGASDPKIT EKVYRVMGSS LRNNPEAISN ILTNFDKSYV DNLFEQLANE
     NDVLQKRILG IIQALVQNSH FVRQYFSFDH SSGLNDLIAI FPKLGPNSKS RASNILEDLQ
     LFPVTNDRRS LEDQDPESQV SKFIQNSFVG NKLDEKNFKS YFDQLVNLHQ SNKSLRPSGD
     FLNWLAEEVE SRKENKKRDD YSQEDKDFDE YMLRARHEVF GNPMGLRKAI ADEL
//