VID28_YEAST
ID VID28_YEAST Reviewed; 921 AA.
AC P40547; D6VVR2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Vacuolar import and degradation protein 28;
DE AltName: Full=Glucose-induced degradation protein 5;
GN Name=VID28; Synonyms=GID5 {ECO:0000303|PubMed:12686616};
GN OrderedLocusNames=YIL017C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP 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 [6]
RP SUBUNIT, AND INTERACTION WITH VID24/GID4; RMD5 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 {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
CC directly with RMD5/GID2 and FYV10/GID9, and recruits VID24/GID4 to the
CC complex when cells are shifted to glucose-containing medium
CC (PubMed:22645139). {ECO:0000269|PubMed:22645139}.
CC -!- INTERACTION:
CC P40547; P53076: VID30; NbExp=10; IntAct=EBI-24957, EBI-24173;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
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DR EMBL; Z46881; CAA86975.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08528.1; -; Genomic_DNA.
DR PIR; S49965; S49965.
DR RefSeq; NP_012247.3; NM_001179367.3.
DR PDB; 6SWY; EM; 3.20 A; 5=1-921.
DR PDB; 7NS3; EM; 3.50 A; 5=1-921.
DR PDBsum; 6SWY; -.
DR PDBsum; 7NS3; -.
DR AlphaFoldDB; P40547; -.
DR SMR; P40547; -.
DR BioGRID; 34971; 175.
DR ComplexPortal; CPX-301; GID ubiquitin ligase complex.
DR DIP; DIP-6335N; -.
DR IntAct; P40547; 6.
DR MINT; P40547; -.
DR STRING; 4932.YIL017C; -.
DR iPTMnet; P40547; -.
DR MaxQB; P40547; -.
DR PaxDb; P40547; -.
DR PRIDE; P40547; -.
DR EnsemblFungi; YIL017C_mRNA; YIL017C; YIL017C.
DR GeneID; 854795; -.
DR KEGG; sce:YIL017C; -.
DR SGD; S000001279; VID28.
DR VEuPathDB; FungiDB:YIL017C; -.
DR eggNOG; KOG1293; Eukaryota.
DR GeneTree; ENSGT00390000003033; -.
DR HOGENOM; CLU_316687_0_0_1; -.
DR InParanoid; P40547; -.
DR OMA; LRHLMYN; -.
DR BioCyc; YEAST:G3O-31293-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P40547; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40547; 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:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0030437; P:ascospore formation; HMP:SGD.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; HMP:SGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038739; ARMC8/Vid28.
DR PANTHER; PTHR15651; PTHR15651; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..921
FT /note="Vacuolar import and degradation protein 28"
FT /id="PRO_0000065828"
FT REGION 822..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..855
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 21..26
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 89..95
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 137..141
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 145..159
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 183..204
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 300..316
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 349..363
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 379..391
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 398..415
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 431..460
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 474..487
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 501..520
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 530..546
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 554..559
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 562..570
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 586..591
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 599..611
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 617..626
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 629..633
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 634..637
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 641..655
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 660..667
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 691..701
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 707..724
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 728..736
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 738..748
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 758..760
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 762..776
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 874..885
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 888..894
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 895..897
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 901..917
FT /evidence="ECO:0007829|PDB:6SWY"
SQ SEQUENCE 921 AA; 105491 MW; DDFA550E22E846A0 CRC64;
MTVAYSLENL KKISNSLVGD QLAKVDYFLA PKCQIFQCLL SIEQSDGVEL KNAKLDLLYT
LLHLEPQQRD IVGTYYFDIV SAIYKSMSLA SSFTKNNSST NYKYIKLLNL CAGVYPNCGF
PDLQYLQNGF IQLVNHKFLR SKCKIDEVVT IIELLKLFLL VDEKNCSDFN KSKFMEEERE
VTETSHYQDF KMAESLEHII VKISSKYLDQ ISLKYIVRLK VSRPASPSSV KNDPFDNKGV
DCTRAIPKKI NISNMYDSSL LSLALLLYLR YHYMIPGDRK LRNDATFKMF VLGLLKSNDV
NIRCVALKFL LQPYFTEDKK WEDTRTLEKI LPYLVKSFNY DPLPWWFDPF DMLDSLIVLY
NEITPMNNPV LTTLAHTNVI FCILSRFAQC LSLPQHNEAT LKTTTKFIKI CASFAASDEK
YRLLLLNDTL LLNHLEYGLE SHITLIQDFI SLKDEIKETT TESHSMCLPP IYDHDFVAAW
LLLLKSFSRS VSALRTTLKR NKIAQLLLQI LSKTYTLTKE CYFAGQDFMK PEIMIMGITL
GSICNFVVEF SNLQSFMLRN GIIDIIEKML TDPLFNSKKA WDDNEDERRI ALQGIPVHEV
KANSLWVLRH LMYNCQNEEK FQLLAKIPMN LILDFINDPC WAVQAQCFQL LRNLTCNSRK
IVNILLEKFK DVEYKIDPQT GNKISIGSTY LFEFLAKKMR LLNPLDTQQK KAMEGILYII
VNLAAVNENK KQLVIEQDEI LNIMSEILVE TTTDSSSNGN DSNLKLACLW VLNNLLWNSS
VSHYTQYAIE NGLEPGHSPS DSENPQSTVT IGYNESVAGG YSRGKYYDEP DGDDSSSNAN
DDEDDDNDEG DDEGDEFVRT PAAKGSTSNV QVTRATVERC RKLVEVGLYD LVRKNITDES
LSVREKARTL LYHMDLLLKV K
