CUE1_CANGA
ID CUE1_CANGA Reviewed; 203 AA.
AC Q6FS98;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Coupling of ubiquitin conjugation to ER degradation protein 1;
GN Name=CUE1; OrderedLocusNames=CAGL0H02321g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380954; CAG59829.1; -; Genomic_DNA.
DR RefSeq; XP_446896.1; XM_446896.1.
DR AlphaFoldDB; Q6FS98; -.
DR SMR; Q6FS98; -.
DR STRING; 5478.XP_446896.1; -.
DR EnsemblFungi; CAG59829; CAG59829; CAGL0H02321g.
DR GeneID; 2888868; -.
DR KEGG; cgr:CAGL0H02321g; -.
DR CGD; CAL0131762; CAGL0H02321g.
DR VEuPathDB; FungiDB:CAGL0H02321g; -.
DR eggNOG; ENOG502S35Z; Eukaryota.
DR HOGENOM; CLU_115919_0_0_1; -.
DR InParanoid; Q6FS98; -.
DR OMA; WLIAPIP; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:1990389; C:CUE1-UBC7 ubiquitin-conjugating enzyme complex; IEA:EnsemblFungi.
DR GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IEA:EnsemblFungi.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IEA:EnsemblFungi.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IEA:EnsemblFungi.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041158; Cue1_U7BR.
DR Pfam; PF02845; CUE; 1.
DR Pfam; PF18499; Cue1_U7BR; 1.
DR SMART; SM00546; 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..203
FT /note="Coupling of ubiquitin conjugation to ER degradation
FT protein 1"
FT /id="PRO_0000280671"
FT TOPO_DOM 1..4
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 70..112
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 29..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 203 AA; 22968 MW; 94A3637A32224A3F CRC64;
MEHSAAVVVA TLILGIFVVK WFAAPKEHPS AQRLPNTQLP SSSNNQQRTA GSSNGRGSQR
RVSSTSRRNI TPEMIETVRN VIPALHPEQI RYDLESTGSV EQTMERYFNG ESFPFPPGYT
PARESSANGQ HNNIDEPSDI RKRSNIRPDN LLSKFNVDMS VDMSDMSIKE LEIDERKKLL
VWEARKNMEK RLETDTELAS LIK
