GID7_YEAST
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 03-AUG-2022, entry version 180.
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 SMR; P25569; -.
DR BioGRID; 30944; 114.
DR ComplexPortal; CPX-301; GID ubiquitin ligase complex.
DR DIP; DIP-4496N; -.
DR IntAct; P25569; 22.
DR MINT; P25569; -.
DR STRING; 4932.YCL039W; -.
DR iPTMnet; P25569; -.
DR MaxQB; P25569; -.
DR PaxDb; P25569; -.
DR PRIDE; P25569; -.
DR TopDownProteomics; P25569; -.
DR EnsemblFungi; YCL039W_mRNA; YCL039W; YCL039W.
DR GeneID; 850318; -.
DR KEGG; sce:YCL039W; -.
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 BioCyc; YEAST:G3O-29298-MON; -.
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; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 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
