ID   ROT1_PICGU              Reviewed;         241 AA.
AC   A5DN48;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Protein ROT1;
DE   Flags: Precursor;
GN   Name=ROT1; ORFNames=PGUG_04699;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408160; EDK40601.2; -; Genomic_DNA.
DR   RefSeq; XP_001482744.1; XM_001482694.1.
DR   AlphaFoldDB; A5DN48; -.
DR   STRING; 4929.XP_001482744.1; -.
DR   EnsemblFungi; EDK40601; EDK40601; PGUG_04699.
DR   GeneID; 5124896; -.
DR   KEGG; pgu:PGUG_04699; -.
DR   VEuPathDB; FungiDB:PGUG_04699; -.
DR   eggNOG; ENOG502QQTG; Eukaryota.
DR   HOGENOM; CLU_071622_0_0_1; -.
DR   InParanoid; A5DN48; -.
DR   OMA; PMHPMYL; -.
DR   OrthoDB; 1494547at2759; -.
DR   Proteomes; UP000001997; Unassembled WGS sequence.
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:0006458; P:'de novo' protein folding; IEA:InterPro.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..241
FT                   /note="Protein ROT1"
FT                   /id="PRO_0000333415"
FT   TOPO_DOM        18..222
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   241 AA;  27262 MW;  ACA45583E08AE439 CRC64;
     MWSILWVVTT LISIVAADPN MKELAGTWTS KSNTVFTGPG FYDPVDELLI QPDLPGISYS
     FTEDGHYEEA LYRVTSNSQN HSCATAVLIY QHGTYEILNN GSLVMTPIAV DGRQLLSDPC
     GYSETESQYT RYVQPTWFKA YYVQVDSYSG KMKLQIYQFD GSLMQPLYLA YSPPLMLPTK
     ALNPTDKASE TKSSLRRKVK RSLENQYRTT AVKSFNYEKY DKYWWAAVGV IGIASASVFL
     H