ID   GID7_YEAST              Reviewed;         745 AA.
AC   P25569; D6VQX6;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   27-MAR-2024, entry version 187.
DE   RecName: Full=Glucose-induced degradation protein 7;
GN   Name=GID7; Synonyms=MOH2; OrderedLocusNames=YCL039W;
GN   ORFNames=YCL311, YCL39W;
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].
RX   PubMed=1523890; DOI=10.1002/yea.320080709;
RA   Scherens B., Messenguy F., Gigot D., Dubois E.;
RT   "The complete sequence of a 9,543 bp segment on the left arm of chromosome
RT   III reveals five open reading frames including glucokinase and the protein
RT   disulfide isomerase.";
RL   Yeast 8:577-586(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
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   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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
RP   SUBUNIT, AND INTERACTION WITH VID30.
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       {ECO:0000269|PubMed:12686616}.
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 with
CC       VID30/GID1; the interaction is direct (PubMed:22645139).
CC       {ECO:0000269|PubMed:22645139}.
CC   -!- INTERACTION:
CC       P25569; P53076: VID30; NbExp=6; IntAct=EBI-21727, EBI-24173;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X59720; CAA42377.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07445.1; -; Genomic_DNA.
DR   PIR; S74281; S74281.
DR   RefSeq; NP_009891.1; NM_001178684.1.
DR   PDB; 7NSB; EM; 3.70 A; 7/g=1-745.
DR   PDBsum; 7NSB; -.
DR   AlphaFoldDB; P25569; -.
DR   EMDB; EMD-12563; -.
DR   SMR; P25569; -.
DR   BioGRID; 30944; 119.
DR   ComplexPortal; CPX-301; GID E3 ubiquitin ligase complex, GID4 variant.
DR   ComplexPortal; CPX-7884; GID E3 ubiquitin ligase complex, GID10 variant.
DR   ComplexPortal; CPX-7885; GID E3 ubiquitin ligase complex, GID11 variant.
DR   DIP; DIP-4496N; -.
DR   IntAct; P25569; 22.
DR   MINT; P25569; -.
DR   STRING; 4932.YCL039W; -.
DR   iPTMnet; P25569; -.
DR   MaxQB; P25569; -.
DR   PaxDb; 4932-YCL039W; -.
DR   PeptideAtlas; P25569; -.
DR   TopDownProteomics; P25569; -.
DR   EnsemblFungi; YCL039W_mRNA; YCL039W; YCL039W.
DR   GeneID; 850318; -.
DR   KEGG; sce:YCL039W; -.
DR   AGR; SGD:S000000544; -.
DR   SGD; S000000544; GID7.
DR   VEuPathDB; FungiDB:YCL039W; -.
DR   eggNOG; KOG0293; Eukaryota.
DR   GeneTree; ENSGT00940000153634; -.
DR   HOGENOM; CLU_020885_0_0_1; -.
DR   InParanoid; P25569; -.
DR   OMA; KNMTCIS; -.
DR   OrthoDB; 5491841at2759; -.
DR   BioCyc; YEAST:G3O-29298-MONOMER; -.
DR   BioGRID-ORCS; 850318; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P25569; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25569; 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:0045721; P:negative regulation of gluconeogenesis; IMP:SGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR22838; WD REPEAT PROTEIN 26-RELATED; 1.
DR   PANTHER; PTHR22838:SF0; WD REPEAT-CONTAINING PROTEIN 26; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW   Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..745
FT                   /note="Glucose-induced degradation protein 7"
FT                   /id="PRO_0000051006"
FT   REPEAT          167..209
FT                   /note="WD 1"
FT   REPEAT          322..365
FT                   /note="WD 2"
FT   REPEAT          369..408
FT                   /note="WD 3"
FT   REPEAT          540..579
FT                   /note="WD 4"
FT   REPEAT          613..652
FT                   /note="WD 5"
FT   REPEAT          657..696
FT                   /note="WD 6"
FT   REPEAT          710..745
FT                   /note="WD 7"
FT   REGION          433..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   745 AA;  84517 MW;  558D538AD27E3B71 CRC64;
     MSHTNKIAYV LNNDTEETAS PSSVGCFDKK QLTKLLIHTL KELGYDSAAN QLLLESGGYQ
     NESNHIQTFF KLIKTGQFHL INWQIVCSLP LAHSSPLRSE WLQRLLIPTP TPATTSLFDH
     MLLQLQYLQQ LMSSVNSSTC SDAEIATLRN YVEIMILVNR QIFLEFFHPV TNSASHKGPH
     TALPVLYLRK ILKNFIEIWD SLLVSNDQFL NEENIFNPET TLRELSTYLT NPKLTAQLNL
     ERDHLIDAIS KYIDPNELVP KGRLLHLLKQ AIKYQQSQDI FNIIDPDDDA SFSSPPHRIN
     LLQDNFSHDL TVTFQEWKTI QDTTDEIWFL TFSPNGKYLA SATSESSRGY FITVYDVEQD
     FKIYKTCVSL SQSVLYLMFS PDSRYLVACP FSEDVTIYDM NATSLPDASA TDSFLLYPST
     RLSPMDSFKL DTTTYPDDTE SSASSSSRPA NANSNQSRVW CCDAFHTAER AGWMVVGSPD
     REAIVHSLTT KESLFSLKGR TCIALGHDEN ISGRKSIDPA KVLYKPTSSN GNWQYVEDDE
     TFPRVHDVKI SYDDKYVLLM THQGVIDVYD FSGFPSKEEL SKQTVDPKNF LIPRIARLDV
     GKNMTCISLP LNTTHQGFHR QQISESQHLV LVSLQDNELQ MWDYKENILI QKYFGQKQQH
     FIIRSCFAYG NKLVMSGSED GKIYIWDRIR GNLVSVLSGH STVMSNSTKP MGKNCNVVAS
     NPADKEMFAS GGDDGKIKIW KISRN
//