ROT1_DEBHA
ID ROT1_DEBHA Reviewed; 244 AA.
AC Q6BSD5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Protein ROT1;
DE Flags: Precursor;
GN Name=ROT1; OrderedLocusNames=DEHA2D09658g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382136; CAG87037.1; -; Genomic_DNA.
DR RefSeq; XP_458885.1; XM_458885.1.
DR AlphaFoldDB; Q6BSD5; -.
DR STRING; 4959.XP_458885.1; -.
DR PRIDE; Q6BSD5; -.
DR EnsemblFungi; CAG87037; CAG87037; DEHA2D09658g.
DR GeneID; 2901336; -.
DR KEGG; dha:DEHA2D09658g; -.
DR VEuPathDB; FungiDB:DEHA2D09658g; -.
DR eggNOG; ENOG502QQTG; Eukaryota.
DR HOGENOM; CLU_071622_0_0_1; -.
DR InParanoid; Q6BSD5; -.
DR OMA; PMHPMYL; -.
DR OrthoDB; 1494547at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..244
FT /note="Protein ROT1"
FT /id="PRO_0000333410"
FT TOPO_DOM 20..222
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 244 AA; 27646 MW; 1D433FED73896529 CRC64;
MMIFSFLVTF FILGAQVLGE NMKELVGTWS SKSNTVFTGP GFYDPVSELL IEPDLPGISY
SFTEDGHYEE ALYRVTSNPK NHSCPTATLI YQHGTYEIKS NGSLFMTPIA VDGRQLLSDP
CGVDTENDAS LYSRYVQKTW FKKFQVMVDS YNGRRKLQIY QFDGSPMQPL YLAYKPPMML
PTSALNPTDS ASETKSSLRK RIKRSLENQY RTNARIETSS AKYEFWWWTA IAGIGLGSAV
IFLH