CUE1_KLULA
ID CUE1_KLULA Reviewed; 218 AA.
AC Q6CNN5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Coupling of ubiquitin conjugation to ER degradation protein 1;
GN Name=CUE1; OrderedLocusNames=KLLA0E11165g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382125; CAG99541.1; -; Genomic_DNA.
DR RefSeq; XP_454454.1; XM_454454.1.
DR AlphaFoldDB; Q6CNN5; -.
DR SMR; Q6CNN5; -.
DR STRING; 28985.XP_454454.1; -.
DR EnsemblFungi; CAG99541; CAG99541; KLLA0_E11199g.
DR GeneID; 2893773; -.
DR KEGG; kla:KLLA0_E11199g; -.
DR eggNOG; ENOG502S35Z; Eukaryota.
DR HOGENOM; CLU_115919_0_0_1; -.
DR InParanoid; Q6CNN5; -.
DR OMA; WLIAPIP; -.
DR Proteomes; UP000000598; Chromosome E.
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..218
FT /note="Coupling of ubiquitin conjugation to ER degradation
FT protein 1"
FT /id="PRO_0000280673"
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..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 69..111
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 35..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 24368 MW; 93BEDC7E385DEB21 CRC64;
MADQSFTLFI ILAIAGYIAV KWFLSNNEQH PSIQINGFSS QSDSATASGT AASSNAASRQ
TRRRIRRRVN DDMIEVVQSL APHLHPEQIR YDLEQTGSVE TTVERYLSGR DMPFPPDYVP
ESETGGNSSN GQNQSTGSSV TTGNNTNNNS TSTDPRKRSN IKADNLLKKF NVDPQEDLSN
LNPNDLSIEE RKRLMVWQAR KSMELKVENS EYLQSLLK
