CUE1_DEBHA
ID CUE1_DEBHA Reviewed; 206 AA.
AC Q6BKU8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Coupling of ubiquitin conjugation to ER degradation protein 1;
GN Name=CUE1; OrderedLocusNames=DEHA2F19052g;
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: Component of the endoplasmic reticulum-associated protein
CC degradation (ERAD) pathway. Recruits the soluble ubiquitin-conjugating
CC enzyme UBC7 to the cytoplasmic face of the endoplasmic reticulum
CC membrane where it functions in degradation of misfolded or regulated
CC proteins localized in the endoplasmic reticulum (ER) lumen or membrane
CC via the ubiquitin-proteasome system. Targets the E2 conjugating enzyme
CC UBC7 to the DOA10 ubiquitin ligase complex, which is part of the ERAD-C
CC pathway responsible for the rapid degradation of membrane proteins with
CC misfolded cytoplasmic domains, and to the HRD1 ubiquitin ligase
CC complex, which is part of the ERAD-L and ERAD-M pathways responsible
CC for the rapid degradation of soluble lumenal and membrane proteins with
CC misfolded lumenal domains (ERAD-L), or ER-membrane proteins with
CC misfolded transmembrane domains (ERAD-M) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with UBC7. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CUE1 family. {ECO:0000305}.
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DR EMBL; CR382138; CAG89558.1; -; Genomic_DNA.
DR RefSeq; XP_461173.1; XM_461173.1.
DR AlphaFoldDB; Q6BKU8; -.
DR SMR; Q6BKU8; -.
DR STRING; 4959.XP_461173.1; -.
DR PRIDE; Q6BKU8; -.
DR EnsemblFungi; CAG89558; CAG89558; DEHA2F19052g.
DR GeneID; 2903742; -.
DR KEGG; dha:DEHA2F19052g; -.
DR VEuPathDB; FungiDB:DEHA2F19052g; -.
DR eggNOG; ENOG502S35Z; Eukaryota.
DR HOGENOM; CLU_115919_0_0_1; -.
DR InParanoid; Q6BKU8; -.
DR OMA; WLIAPIP; -.
DR OrthoDB; 1498293at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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:0043130; F:ubiquitin binding; IEA:InterPro.
DR InterPro; IPR003892; CUE.
DR Pfam; PF02845; CUE; 1.
DR PROSITE; PS51140; CUE; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway.
FT CHAIN 1..206
FT /note="Coupling of ubiquitin conjugation to ER degradation
FT protein 1"
FT /id="PRO_0000280672"
FT TOPO_DOM 1..5
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 70..113
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 41..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 206 AA; 23059 MW; 77B5072DB94291B2 CRC64;
MDNSTIVFIA VLGVAFIFLR WLIAPIPPQL PNELNEALAN SVNNSNRPNN SNNSNSATNS
NANRRGRREP SDDMIEVVQT IAPQLTRGQI RMDLERSGSV EVTMERYMET GSLPFPPGES
AATQSYQSDI SEHSQATKKE PENLIDKYDL KSKIKGDEGE GIENIDENKW GSSKEERSSL
LNKKREEMIL QARKRLASQL QNEVAL
