ID   ROT1_CANGA              Reviewed;         263 AA.
AC   Q6FKL3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Protein ROT1;
DE   Flags: Precursor;
GN   Name=ROT1; OrderedLocusNames=CAGL0L10670g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380958; CAG62205.1; -; Genomic_DNA.
DR   RefSeq; XP_449231.1; XM_449231.1.
DR   AlphaFoldDB; Q6FKL3; -.
DR   STRING; 5478.XP_449231.1; -.
DR   EnsemblFungi; CAG62205; CAG62205; CAGL0L10670g.
DR   GeneID; 2891042; -.
DR   KEGG; cgr:CAGL0L10670g; -.
DR   CGD; CAL0135740; CAGL0L10670g.
DR   VEuPathDB; FungiDB:CAGL0L10670g; -.
DR   eggNOG; ENOG502QQTG; Eukaryota.
DR   HOGENOM; CLU_071622_0_0_1; -.
DR   InParanoid; Q6FKL3; -.
DR   OMA; WFEEATY; -.
DR   Proteomes; UP000002428; Chromosome L.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0006458; P:'de novo' protein folding; IEA:EnsemblFungi.
DR   GO; GO:0007118; P:budding cell apical bud growth; IEA:EnsemblFungi.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IEA:EnsemblFungi.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:EnsemblFungi.
DR   GO; GO:0034975; P:protein folding in endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IEA:EnsemblFungi.
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..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..263
FT                   /note="Protein ROT1"
FT                   /id="PRO_0000333408"
FT   TOPO_DOM        22..241
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          177..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   263 AA;  29129 MW;  FC45FCB3792BEDF5 CRC64;
     MVRSLLFALL SVAGLVAGDA ADLVGTWSSK SNQVFTGPGF YDPIDELLIE PALPGISYSF
     TEDGWFEEAS YQVSGNPKNP ACPKASLIYQ HGKFELLDNG TLILHPIEVD GRQLFSDPCS
     DNGISTYTRY NQTEVFKSFE TFIDPYHGVY TLQLYQFNGA PLPPLYLAYR PPMMLPTETL
     NPTDGSTGSH PTGSSESESQ ESDDTSKRSL LKKRSLREHV KRSLENRYKT NAVKKSDSIF
     NAAFVWYTSF FLVGAGSLIF ISS