GID8_YEAST
ID GID8_YEAST Reviewed; 455 AA.
AC P40208; D6VZV8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glucose-induced degradation protein 8;
DE AltName: Full=Dosage-dependent cell cycle regulator 1;
GN Name=GID8; Synonyms=DCR1 {ECO:0000303|PubMed:15590836};
GN OrderedLocusNames=YMR135C; ORFNames=YM9375.04C;
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 FUNCTION.
RX PubMed=12686616; DOI=10.1091/mbc.e02-08-0456;
RA Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D.,
RA Thumm M., Wolf D.H.;
RT "Catabolite degradation of fructose-1,6-bisphosphatase in the yeast
RT Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID
RT genes and indicates the existence of two degradation pathways.";
RL Mol. Biol. Cell 14:1652-1663(2003).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=15590836; DOI=10.1128/ec.3.6.1627-1638.2004;
RA Pathak R., Bogomolnaya L.M., Guo J., Polymenis M.;
RT "Gid8p (Dcr1p) and Dcr2p function in a common pathway to promote START
RT completion in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 3:1627-1638(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP SUBUNIT, AND INTERACTION WITH VID30 AND FYV10.
RX PubMed=22645139; DOI=10.1074/jbc.m112.363762;
RA Menssen R., Schweiggert J., Schreiner J., Kusevic D., Reuther J., Braun B.,
RA Wolf D.H.;
RT "Exploring the topology of the Gid complex, the E3 ubiquitin ligase
RT involved in catabolite-induced degradation of gluconeogenic enzymes.";
RL J. Biol. Chem. 287:25602-25614(2012).
CC -!- FUNCTION: Required for the adaptation to the presence of glucose in the
CC growth medium; mediates the degradation of enzymes involved in
CC gluconeogenesis when cells are shifted to glucose-containing medium
CC (PubMed:12686616). Required for proteasome-dependent catabolite
CC degradation of fructose-1,6-bisphosphatase (FBP1) (PubMed:12686616).
CC Required also for cell cycle progression. Positively controls G1 and
CC the timing of START (PubMed:15590836). {ECO:0000269|PubMed:12686616,
CC ECO:0000269|PubMed:15590836}.
CC -!- SUBUNIT: Identified in the GID complex. In the absence of glucose, the
CC complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2,
CC VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to
CC glucose-containing medium, VID24/GID4 is induced and becomes part of
CC the complex (PubMed:22645139). Within the GID complex, interacts
CC directly with VID30/GID1, RMD5/GID2 and FYV10/GID9 (PubMed:22645139).
CC {ECO:0000269|PubMed:22645139}.
CC -!- INTERACTION:
CC P40208; P53076: VID30; NbExp=14; IntAct=EBI-27276, EBI-24173;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GID8 family. {ECO:0000305}.
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DR EMBL; Z47071; CAA87349.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10032.1; -; Genomic_DNA.
DR PIR; S50391; S50391.
DR RefSeq; NP_013854.1; NM_001182636.1.
DR PDB; 6SWY; EM; 3.20 A; 8=1-455.
DR PDB; 7NS3; EM; 3.50 A; 8=1-455.
DR PDB; 7NSB; EM; 3.70 A; h=1-455.
DR PDBsum; 6SWY; -.
DR PDBsum; 7NS3; -.
DR PDBsum; 7NSB; -.
DR AlphaFoldDB; P40208; -.
DR SMR; P40208; -.
DR BioGRID; 35312; 142.
DR ComplexPortal; CPX-301; GID ubiquitin ligase complex.
DR DIP; DIP-6457N; -.
DR IntAct; P40208; 9.
DR MINT; P40208; -.
DR STRING; 4932.YMR135C; -.
DR iPTMnet; P40208; -.
DR MaxQB; P40208; -.
DR PaxDb; P40208; -.
DR PRIDE; P40208; -.
DR EnsemblFungi; YMR135C_mRNA; YMR135C; YMR135C.
DR GeneID; 855166; -.
DR KEGG; sce:YMR135C; -.
DR SGD; S000004742; GID8.
DR VEuPathDB; FungiDB:YMR135C; -.
DR eggNOG; KOG2659; Eukaryota.
DR HOGENOM; CLU_055870_0_0_1; -.
DR InParanoid; P40208; -.
DR OMA; LWCWCEN; -.
DR BioCyc; YEAST:G3O-32828-MON; -.
DR PHI-base; PHI:6193; -.
DR PRO; PR:P40208; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40208; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0034657; C:GID complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR Pfam; PF10607; CLTH; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR PROSITE; PS50897; CTLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cytoplasm; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..455
FT /note="Glucose-induced degradation protein 8"
FT /id="PRO_0000087486"
FT DOMAIN 85..116
FT /note="LisH"
FT DOMAIN 130..213
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 243..256
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 274..277
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 281..307
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 428..445
FT /evidence="ECO:0007829|PDB:6SWY"
SQ SEQUENCE 455 AA; 51729 MW; 813215E400E65DBA CRC64;
MTISTLSNET TKSGSCSGQG KNGGKDFTYG KKCFTKEEWK EQVAKYSAMG ELYANKTIHY
PLKIQPNSSG GSQDEGFATI QTTPIEPTLP RLLLNYFVSM AYEDSSIRMA KELGFIRNNK
DIAVFNDLYK IKERFHIKHL IKLGRINEAM EEINSIFGLE VLEETFNATG SYTGRTDRQQ
QQQQQQFDID GDLHFKLLLL NLIEMIRSHH QQENITKDSN DFILNLIQYS QNKLAIKASS
SVKKMQELEL AMTLLLFPLS DSADSGSIKL PKSLQNLYSI SLRSKIADLV NEKLLKFIHP
RIQFEISNNN SKFPDLLNSD KKIITQNFTV YNNNLVNGSN GTKITHISSD QPINEKMSSN
EVTAAANSVW LNQRDGNVGT GSAATTFHNL ENKNYWNQTS ELLSSSNGKE KGLEFNNYYS
SEFPYEPRLT QIMKLWCWCE NQLHHNQIGV PRVEN
