ID   ROT1_ASPCL              Reviewed;         236 AA.
AC   A1CDT3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Protein rot1;
DE   Flags: Precursor;
GN   Name=rot1; ORFNames=ACLA_007690;
OS   Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS   NRRL 1 / QM 1276 / 107).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=344612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027051; EAW12010.1; -; Genomic_DNA.
DR   RefSeq; XP_001273436.1; XM_001273435.1.
DR   AlphaFoldDB; A1CDT3; -.
DR   STRING; 5057.CADACLAP00000552; -.
DR   PRIDE; A1CDT3; -.
DR   EnsemblFungi; EAW12010; EAW12010; ACLA_007690.
DR   GeneID; 4705407; -.
DR   KEGG; act:ACLA_007690; -.
DR   VEuPathDB; FungiDB:ACLA_007690; -.
DR   eggNOG; ENOG502QQTG; Eukaryota.
DR   HOGENOM; CLU_071622_0_0_1; -.
DR   OMA; PMHPMYL; -.
DR   OrthoDB; 1494547at2759; -.
DR   Proteomes; UP000006701; 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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..236
FT                   /note="Protein rot1"
FT                   /id="PRO_0000333403"
FT   TOPO_DOM        21..214
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   236 AA;  26461 MW;  FA7915A7BABAB1E4 CRC64;
     MIVEYFLFNL LVTIISASNA ADLVGTWTTK SRSVVTGPAF YDPINDIFIE PNLTGMSYSF
     TEDGHFEEAY YRALANPTEP SCPKGIMQWQ HGTYSVKSDG SIELTPIAVD GRQLVSDPCS
     KDVGMYTRYN QSETFNLFTV STDAYHHVRR LDLASFDDAP MHPMYLVYKP PQMLPTTTLN
     PASLETGKSK RHVRRDIARS ASVGGFIRSD DLINPDRWLW FGIFMTAMGG IAIIYS