ID   ROT1_YARLI              Reviewed;         248 AA.
AC   Q6CFU5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Protein ROT1;
DE   Flags: Precursor;
GN   Name=ROT1; OrderedLocusNames=YALI0B03652g;
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 [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).
CC   -!- FUNCTION: Required for normal levels of the cell wall 1,6-beta-glucan.
CC       Involved in a protein folding machinery chaperoning proteins acting in
CC       various physiological processes including cell wall synthesis and lysis
CC       of autophagic bodies (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ROT1 family. {ECO:0000305}.
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DR   EMBL; CR382128; CAG82693.1; -; Genomic_DNA.
DR   RefSeq; XP_500467.1; XM_500467.1.
DR   AlphaFoldDB; Q6CFU5; -.
DR   STRING; 4952.CAG82693; -.
DR   EnsemblFungi; CAG82693; CAG82693; YALI0_B03652g.
DR   GeneID; 2907041; -.
DR   KEGG; yli:YALI0B03652g; -.
DR   VEuPathDB; FungiDB:YALI0_B03652g; -.
DR   HOGENOM; CLU_071622_0_0_1; -.
DR   InParanoid; Q6CFU5; -.
DR   OMA; PMHPMYL; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006458; P:'de novo' protein folding; IBA:GO_Central.
DR   GO; GO:0007118; P:budding cell apical bud growth; IBA:GO_Central.
DR   InterPro; IPR019623; Rot1.
DR   PANTHER; PTHR28090; PTHR28090; 1.
DR   Pfam; PF10681; Rot1; 1.
DR   PIRSF; PIRSF017290; ROT1_prd; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..248
FT                   /note="Protein ROT1"
FT                   /id="PRO_0000333419"
FT   TOPO_DOM        24..229
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        139
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   248 AA;  27690 MW;  F3C557FE43EBC5B8 CRC64;
     MKLSTISAFV TSALLATVGH TQSDSSSVDD LEGTWSSKSG AVITGPDFYD PIDELLLEPT
     LPGISYSFTK DGFFEEAIYQ VSANPKDPKC PTGVLIFQHG TYNISDNGTL TLEPYMVDGR
     QLLSDPCKQE ENAVYSRYNQ TEKFKRFSVY VDPYHGRYRL DLFQFNGAPM PPMYLAYRPA
     MMLPTVTLNP TQEASQPENT GSTRAKIRRS IDNRKVTGIK KHSVVDYNSL WWFGVSMIAA
     GGAGWYFL