ROT1_NEOFI
ID ROT1_NEOFI Reviewed; 236 AA.
AC A1DCU0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Protein rot1;
DE Flags: Precursor;
GN Name=rot1; ORFNames=NFIA_027240;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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; DS027695; EAW19650.1; -; Genomic_DNA.
DR RefSeq; XP_001261547.1; XM_001261546.1.
DR AlphaFoldDB; A1DCU0; -.
DR STRING; 36630.CADNFIAP00002331; -.
DR EnsemblFungi; EAW19650; EAW19650; NFIA_027240.
DR GeneID; 4588161; -.
DR KEGG; nfi:NFIA_027240; -.
DR VEuPathDB; FungiDB:NFIA_027240; -.
DR eggNOG; ENOG502QQTG; Eukaryota.
DR HOGENOM; CLU_071622_0_0_1; -.
DR OMA; PMHPMYL; -.
DR OrthoDB; 1494547at2759; -.
DR Proteomes; UP000006702; 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..236
FT /note="Protein rot1"
FT /id="PRO_0000333414"
FT TOPO_DOM 18..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 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 236 AA; 26194 MW; D4E1630686C9D25D CRC64;
MIVGYLLLNF LVAVVRASSV AELVGTWTTK SRTVVTGPDF YDPIDDKLLE PSLTGISYSF
TADGYYEQAY YRAVSNPTTP SCPKGIMLWQ HGKYAVMPDG SIQLTPIAVD GRQLVSDPCS
KEVAMYTRYN QTEAFSSFTV SIDSYHHVKR LDLKAFDETP MPPMYLIFKP PQMLPTTTLN
PVSSETGKSK RHIARDIGSP VGVDTLMRSD HIGDPGRWLW FGIFMTAMGG IALIYS