DSC3_YEAST
ID DSC3_YEAST Reviewed; 292 AA.
AC Q12015; D6W2S8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=DSC E3 ubiquitin ligase complex subunit 3 {ECO:0000303|PubMed:25078903};
DE AltName: Full=Defective for SREBP cleavage protein 3 {ECO:0000303|PubMed:25078903};
GN Name=DSC3 {ECO:0000303|PubMed:25078903}; OrderedLocusNames=YOR223W;
GN ORFNames=YOR50-13;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840505;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<877::aid-yea969>3.0.co;2-s;
RA Galisson F., Dujon B.;
RT "Sequence and analysis of a 33 kb fragment from the right arm of chromosome
RT XV of the yeast Saccharomyces cerevisiae.";
RL Yeast 12:877-885(1996).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21777356; DOI=10.1111/j.1600-0854.2011.01252.x;
RA Arlt H., Perz A., Ungermann C.;
RT "An overexpression screen in Saccharomyces cerevisiae identifies novel
RT genes that affect endocytic protein trafficking.";
RL Traffic 12:1592-1603(2011).
RN [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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 tag
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 (PubMed:25078903, PubMed:29355480). Involved
CC in endocytic protein trafficking (PubMed:21777356).
CC {ECO:0000269|PubMed:21777356, 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21777356}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:21777356}.
CC -!- SIMILARITY: Belongs to the dsc3 family. {ECO:0000305}.
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DR EMBL; X92441; CAA63186.1; -; Genomic_DNA.
DR EMBL; Z75131; CAA99441.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10994.1; -; Genomic_DNA.
DR PIR; S60950; S60950.
DR RefSeq; NP_014866.3; NM_001183642.3.
DR AlphaFoldDB; Q12015; -.
DR BioGRID; 34617; 70.
DR ComplexPortal; CPX-1190; TUL1 E3 ubiquitin ligase complex.
DR IntAct; Q12015; 7.
DR STRING; 4932.YOR223W; -.
DR MaxQB; Q12015; -.
DR PaxDb; Q12015; -.
DR PRIDE; Q12015; -.
DR EnsemblFungi; YOR223W_mRNA; YOR223W; YOR223W.
DR GeneID; 854398; -.
DR KEGG; sce:YOR223W; -.
DR SGD; S000005749; YOR223W.
DR VEuPathDB; FungiDB:YOR223W; -.
DR eggNOG; ENOG502RXWC; Eukaryota.
DR HOGENOM; CLU_035821_1_1_1; -.
DR InParanoid; Q12015; -.
DR OMA; HCSLGDA; -.
DR BioCyc; YEAST:G3O-33722-MON; -.
DR PRO; PR:Q12015; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12015; protein.
DR GO; GO:0044695; C:Dsc E3 ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000328; C:fungal-type vacuole lumen; IDA: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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; 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; IPR045226; Dsc3.
DR InterPro; IPR025390; Dsc3_C.
DR InterPro; IPR019413; Dsc3_ub-like_dom.
DR PANTHER; PTHR28049; PTHR28049; 1.
DR Pfam; PF10302; DUF2407; 1.
DR Pfam; PF13373; DUF2407_C; 1.
PE 1: Evidence at protein level;
KW Endocytosis; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..292
FT /note="DSC E3 ubiquitin ligase complex subunit 3"
FT /id="PRO_0000237667"
FT TOPO_DOM 1..243
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 292 AA; 32935 MW; 5890B8E3CBBA8040 CRC64;
MSAEPLLPTH NGSQGGEVRS PDQKFIVIRF SDVSVRDLQL NISNVPFSNI NTHWLRRMCR
ELRPQQTQKR RLKFIRNGSI LNTHSKIAEE LTHYFDTANN SNVATGTSVA PEQNNYYIHC
IIGTEELTQA ELANEDLKDD ATPSNDSMTT QAIGFDRLRS VGFTEQEIEL LRQQFRATYG
DLEEEEERLA QNGNRDDEGH DIRQLEEQWM ESGSGTAQGN GAGGGNEDRF NSVPIANIKH
NKDLLLGICV GFFFGVFGIL LMKFDGLFNR RQKMAIFAGV IVNVMFCLVR GF
