ID   ROT1_AJECN              Reviewed;         273 AA.
AC   A6RBY1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Protein ROT1;
DE   Flags: Precursor;
GN   Name=ROT1; ORFNames=HCAG_07139;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(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; CH476662; EDN10678.1; -; Genomic_DNA.
DR   RefSeq; XP_001537717.1; XM_001537667.1.
DR   AlphaFoldDB; A6RBY1; -.
DR   STRING; 339724.A6RBY1; -.
DR   PRIDE; A6RBY1; -.
DR   EnsemblFungi; EDN10678; EDN10678; HCAG_07139.
DR   GeneID; 5444253; -.
DR   KEGG; aje:HCAG_07139; -.
DR   VEuPathDB; FungiDB:HCAG_07139; -.
DR   HOGENOM; CLU_071622_0_0_1; -.
DR   OMA; PMHPMYL; -.
DR   OrthoDB; 1494547at2759; -.
DR   Proteomes; UP000009297; 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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..273
FT                   /note="Protein ROT1"
FT                   /id="PRO_0000333401"
FT   TOPO_DOM        25..250
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        108
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   273 AA;  31136 MW;  D48513A6243F15C5 CRC64;
     METMMLAALP LLFLSSCFPA FVVAQGPADP RLTGTWTTKS MKVFTGSAFY DPIKDRLKEP
     LLTGISYSFT ADGFYEEAYF RAISNPTRPE CPSGIMQFQH GTYRVEPNGS MILTPFDSDG
     RQLISNRCAG KYAEYTRYTQ KEVFQRYEIL IDSYNRVERL NMFQFDGSPL NPMYLAFRQP
     QMHPTHTLNP THTTKGAPRA TAISERKVNA KRAKRSEEKA AEFGFAQSPL SKNSFVKRMN
     YYHSRMEKLS GTDKLWWVGL IMTSVGSLAL IYR