CUE1_YEAST
ID CUE1_YEAST Reviewed; 203 AA.
AC P38428; D6W090; Q03507;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Coupling of ubiquitin conjugation to ER degradation protein 1;
DE AltName: Full=Kinetochore-defect suppressor 4;
GN Name=CUE1; Synonyms=KIS4; OrderedLocusNames=YMR264W; ORFNames=YM8156.06;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-158.
RA Manning A.M., Rosenbloom C.L., Beaudet A.L.;
RT "A large open reading frame in the yeast genome containing homology to the
RT cif1 gene.";
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 1-29, TOPOLOGY, FUNCTION, AND INTERACTION WITH UBC7.
RX PubMed=9388185; DOI=10.1126/science.278.5344.1806;
RA Biederer T., Volkwein C., Sommer T.;
RT "Role of Cue1p in ubiquitination and degradation at the ER surface.";
RL Science 278:1806-1809(1997).
RN [6]
RP FUNCTION.
RX PubMed=9335582; DOI=10.1093/genetics/147.2.409;
RA Kopski K.M., Huffaker T.C.;
RT "Suppressors of the ndc10-2 mutation: a role for the ubiquitin system in
RT Saccharomyces cerevisiae kinetochore function.";
RL Genetics 147:409-420(1997).
RN [7]
RP DOMAIN.
RX PubMed=11023840; DOI=10.1042/bj3510527;
RA Ponting C.P.;
RT "Proteins of the endoplasmic-reticulum-associated degradation pathway:
RT domain detection and function prediction.";
RL Biochem. J. 351:527-535(2000).
RN [8]
RP FUNCTION.
RX PubMed=10991948; DOI=10.1074/jbc.m006949200;
RA Lenk U., Sommer T.;
RT "Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends
RT on its cellular localization.";
RL J. Biol. Chem. 275:39403-39410(2000).
RN [9]
RP FUNCTION.
RX PubMed=10982838; DOI=10.1128/mcb.20.19.7214-7219.2000;
RA Gilon T., Chomsky O., Kulka R.G.;
RT "Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugating
RT enzyme pair.";
RL Mol. Cell. Biol. 20:7214-7219(2000).
RN [10]
RP FUNCTION.
RX PubMed=10878801; DOI=10.1038/35017001;
RA Friedlander R., Jarosch E., Urban J., Volkwein C., Sommer T.;
RT "A regulatory link between ER-associated protein degradation and the
RT unfolded-protein response.";
RL Nat. Cell Biol. 2:379-384(2000).
RN [11]
RP FUNCTION, AND INTERACTION WITH UBC7.
RX PubMed=11406589; DOI=10.1093/emboj/20.12.3124;
RA Walter J., Urban J., Volkwein C., Sommer T.;
RT "Sec61p-independent degradation of the tail-anchored ER membrane protein
RT Ubc6p.";
RL EMBO J. 20:3124-3131(2001).
RN [12]
RP FUNCTION.
RX PubMed=11390656; DOI=10.1128/mcb.21.13.4276-4291.2001;
RA Gardner R.G., Shearer A.G., Hampton R.Y.;
RT "In vivo action of the HRD ubiquitin ligase complex: mechanisms of
RT endoplasmic reticulum quality control and sterol regulation.";
RL Mol. Cell. Biol. 21:4276-4291(2001).
RN [13]
RP FUNCTION.
RX PubMed=12399372; DOI=10.1093/genetics/162.2.567;
RA McBratney S., Winey M.;
RT "Mutant membrane protein of the budding yeast spindle pole body is targeted
RT to the endoplasmic reticulum degradation pathway.";
RL Genetics 162:567-578(2002).
RN [14]
RP DOMAIN.
RX PubMed=12628920; DOI=10.1093/emboj/cdg140;
RA Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L.;
RT "A ubiquitin-binding motif required for intramolecular monoubiquitylation,
RT the CUE domain.";
RL EMBO J. 22:1273-1281(2003).
RN [15]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [16]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [17]
RP FUNCTION, AND INTERACTION WITH SSM4 AND UBX2.
RX PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
RA Carvalho P., Goder V., Rapoport T.A.;
RT "Distinct ubiquitin-ligase complexes define convergent pathways for the
RT degradation of ER proteins.";
RL Cell 126:361-373(2006).
RN [18]
RP FUNCTION.
RX PubMed=16607018; DOI=10.1128/ec.5.4.712-722.2006;
RA Loertscher J., Larson L.L., Matson C.K., Parrish M.L., Felthauser A.,
RA Sturm A., Tachibana C., Bard M., Wright R.;
RT "Endoplasmic reticulum-associated degradation is required for cold
RT adaptation and regulation of sterol biosynthesis in the yeast Saccharomyces
RT cerevisiae.";
RL Eukaryot. Cell 5:712-722(2006).
RN [19]
RP FUNCTION.
RX PubMed=16556771; DOI=10.1124/mol.105.021816;
RA Liao M., Faouzi S., Karyakin A., Correia M.A.;
RT "Endoplasmic reticulum-associated degradation of cytochrome P450 CYP3A4 in
RT Saccharomyces cerevisiae: further characterization of cellular participants
RT and structural determinants.";
RL Mol. Pharmacol. 69:1897-1904(2006).
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). Has also a role in cold
CC adaptation, perhaps through effects on sterol biosynthesis.
CC {ECO:0000269|PubMed:10878801, ECO:0000269|PubMed:10982838,
CC ECO:0000269|PubMed:10991948, ECO:0000269|PubMed:11390656,
CC ECO:0000269|PubMed:11406589, ECO:0000269|PubMed:12399372,
CC ECO:0000269|PubMed:16556771, ECO:0000269|PubMed:16607018,
CC ECO:0000269|PubMed:16873066, ECO:0000269|PubMed:9335582,
CC ECO:0000269|PubMed:9388185}.
CC -!- SUBUNIT: Forms a heterodimer with UBC7. Interacts with SSM4/DOA10 and
CC UBX2/SEL1. {ECO:0000269|PubMed:11406589, ECO:0000269|PubMed:16873066,
CC ECO:0000269|PubMed:9388185}.
CC -!- INTERACTION:
CC P38428; P40318: SSM4; NbExp=2; IntAct=EBI-27580, EBI-18208;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CUE1 family. {ECO:0000305}.
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DR EMBL; Z49260; CAA89247.1; -; Genomic_DNA.
DR EMBL; AY557973; AAS56299.1; -; Genomic_DNA.
DR EMBL; M88172; AAA35221.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10164.1; -; Genomic_DNA.
DR PIR; S54476; S54476.
DR RefSeq; NP_013991.1; NM_001182771.1.
DR PDB; 2MYX; NMR; -; A=45-115.
DR PDB; 4JQU; X-ray; 1.81 A; B=151-203.
DR PDBsum; 2MYX; -.
DR PDBsum; 4JQU; -.
DR AlphaFoldDB; P38428; -.
DR SMR; P38428; -.
DR BioGRID; 35442; 177.
DR ComplexPortal; CPX-2948; CUE1-UBC7 ubiquitin-conjugating enzyme complex.
DR DIP; DIP-4399N; -.
DR IntAct; P38428; 8.
DR MINT; P38428; -.
DR STRING; 4932.YMR264W; -.
DR iPTMnet; P38428; -.
DR MaxQB; P38428; -.
DR PaxDb; P38428; -.
DR PRIDE; P38428; -.
DR EnsemblFungi; YMR264W_mRNA; YMR264W; YMR264W.
DR GeneID; 855306; -.
DR KEGG; sce:YMR264W; -.
DR SGD; S000004877; CUE1.
DR VEuPathDB; FungiDB:YMR264W; -.
DR eggNOG; ENOG502S35Z; Eukaryota.
DR HOGENOM; CLU_115919_0_0_1; -.
DR InParanoid; P38428; -.
DR OMA; WLIAPIP; -.
DR BioCyc; YEAST:G3O-32938-MON; -.
DR PRO; PR:P38428; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P38428; protein.
DR GO; GO:1990389; C:CUE1-UBC7 ubiquitin-conjugating enzyme complex; IPI:ComplexPortal.
DR GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0097027; F:ubiquitin-protein transferase activator activity; IDA:SGD.
DR GO; GO:0097051; P:establishment of protein localization to endoplasmic reticulum membrane; IMP:SGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway.
FT CHAIN 1..203
FT /note="Coupling of ubiquitin conjugation to ER degradation
FT protein 1"
FT /id="PRO_0000203346"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:9388185"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9388185"
FT DOMAIN 65..107
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 35..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 48
FT /note="S -> P (in Ref. 4; AAA35221)"
FT /evidence="ECO:0000305"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:2MYX"
FT HELIX 82..92
FT /evidence="ECO:0007829|PDB:2MYX"
FT HELIX 95..103
FT /evidence="ECO:0007829|PDB:2MYX"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:2MYX"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4JQU"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4JQU"
FT HELIX 173..192
FT /evidence="ECO:0007829|PDB:4JQU"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:4JQU"
SQ SEQUENCE 203 AA; 22763 MW; 3F795BD78DAC3D5B CRC64;
MEDSRLLITL ILVFGVIFLK KFFQSNQHPS AQRLSATGVN AHGRPQGSTQ NALRRTGRVN
GGHPVTTQMV ETVQNLAPNL HPEQIRYSLE NTGSVEETVE RYLRGDEFSF PPGFEPSRAP
MGANAAVDNN AAGGGEFNDP RKKNMICAEN LLDKFHVDLN EDMSNLSFKD LDIEERKRLL
VWQARKNLET KLQSDKDLQS LLT
