VID30_YEAST
ID VID30_YEAST Reviewed; 958 AA.
AC P53076; D6VVA7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Vacuolar import and degradation protein 30;
DE AltName: Full=Glucose-induced degradation protein 1;
GN Name=VID30; Synonyms=GID1; OrderedLocusNames=YGL227W;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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=9737955; DOI=10.1074/jbc.273.39.25000;
RA Haemmerle M., Bauer J., Rose M., Szallies A., Thumm M., Duesterhus S.,
RA Mecke D., Entian K.D., Wolf D.H.;
RT "Proteins of newly isolated mutants and the amino-terminal proline are
RT essential for ubiquitin-proteasome-catalyzed catabolite degradation of
RT fructose-1,6-bisphosphatase of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:25000-25005(1998).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-246 AND SER-248, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147; SER-248 AND SER-277, AND
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 FUNCTION, SUBUNIT, INTERACTION WITH GID7 AND GID8, AND MUTAGENESIS OF
RP 710-LEU--ALA-742 AND 754-ASP--LEU-835.
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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION.
RX PubMed=28126757; DOI=10.1126/science.aal3655;
RA Chen S.J., Wu X., Wadas B., Oh J.H., Varshavsky A.;
RT "An N-end rule pathway that recognizes proline and destroys gluconeogenic
RT enzymes.";
RL Science 355:0-0(2017).
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:9737955, PubMed:12686616). Required for proteasome-dependent
CC catabolite degradation of fructose-1,6-bisphosphatase (FBP1)
CC (PubMed:9737955, PubMed:12686616, PubMed:22645139, PubMed:28126757).
CC {ECO:0000269|PubMed:12686616, ECO:0000269|PubMed:22645139,
CC ECO:0000269|PubMed:28126757, ECO:0000269|PubMed:9737955}.
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 complex, VID30/GID1 interacts
CC directly (via LisH domain) with GID8, and (via CTLH domain) with GID7
CC (PubMed:22645139). {ECO:0000269|PubMed:22645139}.
CC -!- INTERACTION:
CC P53076; P25569: GID7; NbExp=6; IntAct=EBI-24173, EBI-21727;
CC P53076; P40208: GID8; NbExp=14; IntAct=EBI-24173, EBI-27276;
CC P53076; Q12508: RMD5; NbExp=8; IntAct=EBI-24173, EBI-38868;
CC P53076; P40547: VID28; NbExp=10; IntAct=EBI-24173, EBI-24957;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72749; CAA96943.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07891.1; -; Genomic_DNA.
DR PIR; S64249; S64249.
DR RefSeq; NP_011287.1; NM_001181093.1.
DR PDB; 6SWY; EM; 3.20 A; 1=1-958.
DR PDB; 7NSB; EM; 3.70 A; a=1-958.
DR PDBsum; 6SWY; -.
DR PDBsum; 7NSB; -.
DR AlphaFoldDB; P53076; -.
DR SMR; P53076; -.
DR BioGRID; 33012; 200.
DR ComplexPortal; CPX-301; GID ubiquitin ligase complex.
DR DIP; DIP-6352N; -.
DR IntAct; P53076; 19.
DR MINT; P53076; -.
DR STRING; 4932.YGL227W; -.
DR iPTMnet; P53076; -.
DR MaxQB; P53076; -.
DR PaxDb; P53076; -.
DR PRIDE; P53076; -.
DR EnsemblFungi; YGL227W_mRNA; YGL227W; YGL227W.
DR GeneID; 852624; -.
DR KEGG; sce:YGL227W; -.
DR SGD; S000003196; VID30.
DR VEuPathDB; FungiDB:YGL227W; -.
DR eggNOG; KOG1477; Eukaryota.
DR GeneTree; ENSGT00940000174485; -.
DR HOGENOM; CLU_308189_0_0_1; -.
DR InParanoid; P53076; -.
DR OMA; INDYLIH; -.
DR BioCyc; YEAST:G3O-30701-MON; -.
DR PRO; PR:P53076; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53076; 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 GO; GO:0006808; P:regulation of nitrogen utilization; IMP:SGD.
DR CDD; cd12885; SPRY_RanBP_like; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR044736; Vid30/RanBPM/SPLA_SPRY.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..958
FT /note="Vacuolar import and degradation protein 30"
FT /id="PRO_0000065829"
FT DOMAIN 390..592
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT DOMAIN 710..742
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 769..826
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT REGION 155..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..742
FT /note="Required for interaction with GID8"
FT /evidence="ECO:0000269|PubMed:22645139"
FT REGION 754..835
FT /note="Required for interaction with GID7"
FT /evidence="ECO:0000269|PubMed:22645139"
FT COMPBIAS 162..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 710..742
FT /note="Missing: Loss of interaction with GID8."
FT /evidence="ECO:0000269|PubMed:22645139"
FT MUTAGEN 754..835
FT /note="Missing: Loss of interaction with GID7."
FT /evidence="ECO:0000269|PubMed:22645139"
FT HELIX 7..16
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 400..410
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 497..503
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 538..544
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 545..548
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 549..554
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 557..564
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 571..577
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 588..591
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 597..612
FT /evidence="ECO:0007829|PDB:6SWY"
FT TURN 705..707
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 709..724
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 728..741
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 752..780
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 915..931
FT /evidence="ECO:0007829|PDB:6SWY"
FT STRAND 936..942
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 945..948
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 951..954
FT /evidence="ECO:0007829|PDB:6SWY"
SQ SEQUENCE 958 AA; 108179 MW; 335ADD152949F8C8 CRC64;
MSEYMDDVDR EFINCLFPSY LLQQPVAYDL WILYLQHRKL FHKLKNTNLI NADENPTGVG
MGRTKLTALT RKEIWSKLMN LGVLGTISFE AVNDDYLIQV YKYFYPDVND FTLRFGVKDS
NKNSVRVMKA SSDMRKNAQE LLEPVLSERE MALNSNTSLE NDRNDDDDDD DDDDDDDDDD
DDDDDESDLE SLEGEVDTDT DDNNEGDGSD NHEEGGEEGS RGADADVSSA QQRAERVADP
WIYQRSRSAI NIETESRNLW DTSDKNSGLQ YYPPDQSPSS SFSSPRVSSG NDKNDNEATN
VLSNSGSKKK NSMIPDIYKI LGYFLPSRWQ AQPNNSLQLS QDGITHLQPN PDYHSYMTYE
RSSASSASTR NRLRTSFENS GKVDFAVTWA NKSLPDNKLT IFYYEIKVLS VTSTESAENS
NIVIGYKLVE NELMEATTKK SVSRSSVAGS SSSLGGSNNM SSNRVPSTSF TMEGTQRRDY
IYEGGVSAMS LNVDGSINKC QKYGFDLNVF GYCGFDGLIT NSTEQSKEYA KPFGRDDVIG
CGINFIDGSI FFTKNGIHLG NAFTDLNDLE FVPYVALRPG NSIKTNFGLN EDFVFDIIGY
QDKWKSLAYE HICRGRQMDV SIEEFDSDES EEDETENGPE ENKSTNVNED LMDIDQEDGA
AGNKDTKKLN DEKDNNLKFL LGEDNRFIDG KLVRPDVNNI NNLSVDDGSL PNTLNVMIND
YLIHEGLVDV AKGFLKDLQK DAVNVNGQHS ESKDVIRHNE RQIMKEERMV KIRQELRYLI
NKGQISKCIN YIDNEIPDLL KNNLELVFEL KLANYLVMIK KSSSKDDDEI ENLILKGQEL
SNEFIYDTKI PQSLRDRFSG QLSNVSALLA YSNPLVEAPK EISGYLSDEY LQERLFQVSN
NTILTFLHKD SECALENVIS NTRAMLSTLL EYNAFGSTNS SDPRYYKAIN FDEDVLNL
