ID   ROT1_ASPTN              Reviewed;         236 AA.
AC   Q0CJ00;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Protein rot1;
DE   Flags: Precursor;
GN   Name=rot1; ORFNames=ATEG_06334;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476602; EAU32878.1; -; Genomic_DNA.
DR   RefSeq; XP_001215512.1; XM_001215512.1.
DR   AlphaFoldDB; Q0CJ00; -.
DR   STRING; 341663.Q0CJ00; -.
DR   EnsemblFungi; EAU32878; EAU32878; ATEG_06334.
DR   GeneID; 4322283; -.
DR   VEuPathDB; FungiDB:ATEG_06334; -.
DR   eggNOG; ENOG502QQTG; Eukaryota.
DR   HOGENOM; CLU_071622_0_0_1; -.
DR   OMA; PMHPMYL; -.
DR   OrthoDB; 1494547at2759; -.
DR   Proteomes; UP000007963; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..236
FT                   /note="Protein rot1"
FT                   /id="PRO_0000333405"
FT   TOPO_DOM        19..217
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   236 AA;  27009 MW;  02875DE082F8590E CRC64;
     MVHAGYFVLG LLTTTVSAVN NVADLVGTWS TKSRNVLTGP GFYDPIQDKL LEPNLTGISY
     SFTADGYYEE AYYRALANPT NPECPRGIMQ WQHGSYVVDS GGVLRLTPIE VDGRQLLSDP
     CAADKGIYTR YNQTETFNSF KVYVDSYHNV QRLDLQKFDD SFMHPMYLVY RPPQMLPTET
     LNPVSHSKKK RHVTRETHGW FRLTDLVKRE EILNPDRWLW LGLFMTAVGG FTFIYS