CUE1_CANAL
ID CUE1_CANAL Reviewed; 189 AA.
AC Q59NY7; A0A1D8PNQ0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Coupling of ubiquitin conjugation to ER degradation protein 1;
GN Name=CUE1; OrderedLocusNames=CAALFM_C503570WA; ORFNames=CaO19.6668;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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
CC {ECO:0000255|PROSITE-ProRule:PRU10138}; Single-pass membrane protein
CC {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; CP017627; AOW29769.1; -; Genomic_DNA.
DR RefSeq; XP_711420.2; XM_706328.2.
DR AlphaFoldDB; Q59NY7; -.
DR SMR; Q59NY7; -.
DR STRING; 237561.Q59NY7; -.
DR GeneID; 3646976; -.
DR KEGG; cal:CAALFM_C503570WA; -.
DR CGD; CAL0000179547; orf19.6668.
DR eggNOG; ENOG502S35Z; Eukaryota.
DR HOGENOM; CLU_115919_0_0_1; -.
DR InParanoid; Q59NY7; -.
DR OrthoDB; 1498293at2759; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR003892; CUE.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR PROSITE; PS51140; CUE; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway.
FT CHAIN 1..189
FT /note="Coupling of ubiquitin conjugation to ER degradation
FT protein 1"
FT /id="PRO_0000280670"
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..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 72..114
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 38..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 189 AA; 21236 MW; FFC72E82CE0C3317 CRC64;
MDSSTVLFIG AVAVAFIFLK WMVSPIPPQN EFTIDHLSQD QSTGSTTSSN AHQNRDTHSI
STQSHRNSRR AVSESMIEVV QSIAPMLTVE QIRYDLETTG NVEATVNRFM ELGDLPFPPG
YVRPQQPPTP SEEPKKQEVI GKRSVNLLEK YNIDAKNPKS DHNSLLHQRR QEMILGARKR
LAAQLSNEL
