DSC2_YEAST
ID DSC2_YEAST Reviewed; 322 AA.
AC Q08232; D6W1Z4;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DSC E3 ubiquitin ligase complex subunit 2 {ECO:0000303|PubMed:25078903};
DE AltName: Full=Defective for SREBP cleavage protein 2 {ECO:0000303|PubMed:25078903};
GN Name=DSC2 {ECO:0000303|PubMed:25078903}; OrderedLocusNames=YOL073C;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN THE DSC E3 UBIQUITIN LIGASE COMPLEX.
RX PubMed=25078903; DOI=10.1074/mcp.m114.040774;
RA Tong Z., Kim M.S., Pandey A., Espenshade P.J.;
RT "Identification of candidate substrates for the Golgi Tul1 E3 ligase using
RT quantitative diGly proteomics in yeast.";
RL Mol. Cell. Proteomics 13:2871-2882(2014).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE DSC E3 UBIQUITIN
RP LIGASE COMPLEX.
RX PubMed=29355480; DOI=10.7554/elife.33116;
RA Yang X., Arines F.M., Zhang W., Li M.;
RT "Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome
RT system.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Component of the DSC E3 ubiquitin ligase complexes that tags
CC proteins present in Golgi, endosome and vacuole membranes and function
CC in protein homeostasis under non-stress conditions and support a role
CC in protein quality control. {ECO:0000269|PubMed:25078903,
CC ECO:0000269|PubMed:29355480}.
CC -!- SUBUNIT: Component of the DSC E3 ligase complexes composed of at least
CC TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the vacuole-localized
CC complex or GLD1 for the Golgi/endosome-localized complex.
CC {ECO:0000269|PubMed:25078903, ECO:0000269|PubMed:29355480}.
CC -!- INTERACTION:
CC Q08232; Q12229: UBX3; NbExp=6; IntAct=EBI-32978, EBI-35335;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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DR EMBL; Z74815; CAA99083.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10710.1; -; Genomic_DNA.
DR PIR; S66766; S66766.
DR RefSeq; NP_014568.1; NM_001183328.1.
DR AlphaFoldDB; Q08232; -.
DR BioGRID; 34328; 93.
DR ComplexPortal; CPX-1190; TUL1 E3 ubiquitin ligase complex.
DR DIP; DIP-4167N; -.
DR IntAct; Q08232; 3.
DR STRING; 4932.YOL073C; -.
DR iPTMnet; Q08232; -.
DR PaxDb; Q08232; -.
DR PRIDE; Q08232; -.
DR EnsemblFungi; YOL073C_mRNA; YOL073C; YOL073C.
DR GeneID; 854081; -.
DR KEGG; sce:YOL073C; -.
DR SGD; S000005434; YOL073C.
DR VEuPathDB; FungiDB:YOL073C; -.
DR eggNOG; KOG4463; Eukaryota.
DR HOGENOM; CLU_057574_1_0_1; -.
DR InParanoid; Q08232; -.
DR OMA; MYKYRIA; -.
DR BioCyc; YEAST:G3O-33478-MON; -.
DR PRO; PR:Q08232; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08232; protein.
DR GO; GO:0044695; C:Dsc E3 ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR SUPFAM; SSF144091; SSF144091; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..322
FT /note="DSC E3 ubiquitin ligase complex subunit 2"
FT /id="PRO_0000235926"
FT TOPO_DOM 1..19
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..90
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 269..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 35762 MW; E1DF412F130C43B4 CRC64;
MSMEPPVGLT AMPVTKLAMI TTLVVPLVAS IASYKHIFLL QYDPFLQTYH QYYRLLIFQF
CAINESDTVI LALIWYLFRH LERLLGSHKY LTLIVLSWAY TTLGIWGLNL IWNAFIGQYK
WLQWNNFSTG SLPIVLSLVH FYKEYTPQIY EWNIRLLGPR GGASSHNDNK REDKSAVEWK
INDQFLLNGL ILLLILNQGF AGILCGFISW MCGIFIDKGL LPGLDHWRIP FVSYFISQGP
PTRANVAIAA NAATNTAAAR ATVEAATAAT GNGNTGNSGP TSLPLRGSST TPTNTSSAGD
DEPGADEPAR PLGVQFLDTF RR
