ID   ROT1_VANPO              Reviewed;         255 AA.
AC   A7TDM0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Protein ROT1;
DE   Flags: Precursor;
GN   Name=ROT1; ORFNames=Kpol_1018p18;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480378; EDO19490.1; -; Genomic_DNA.
DR   RefSeq; XP_001647348.1; XM_001647298.1.
DR   AlphaFoldDB; A7TDM0; -.
DR   STRING; 436907.A7TDM0; -.
DR   EnsemblFungi; EDO19490; EDO19490; Kpol_1018p18.
DR   GeneID; 5547838; -.
DR   KEGG; vpo:Kpol_1018p18; -.
DR   eggNOG; ENOG502QQTG; Eukaryota.
DR   HOGENOM; CLU_071622_0_0_1; -.
DR   InParanoid; A7TDM0; -.
DR   OMA; WFEEATY; -.
DR   OrthoDB; 1494547at2759; -.
DR   PhylomeDB; A7TDM0; -.
DR   Proteomes; UP000000267; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..255
FT                   /note="Protein ROT1"
FT                   /id="PRO_0000333418"
FT   TOPO_DOM        23..230
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..255
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   255 AA;  28325 MW;  25CDF7A82B302218 CRC64;
     MFGMRLLPFL ANAVILFNFA IGDNDAASLS GTWSSKSNQV FTGPGFYDPV DELLIEPALP
     GISYSFTEDG YFEEAQYRVV ANPRNIGCPQ AVLIYQHGKY EILTNGTLIL TPFEVDGRQL
     LSDPCNDDGV STYSRYNQSE TFLSFDISID DYHGIYKLQL NQFDGSPLQP LYLAYRPPMM
     LPTITLNPTA TNDPTDAVGK GSVSKRSLRQ IVKRNLENKH KQLATKKYSG ILVSPYLWYV
     CTGVIGVGSA LFLFS