Protein FYV10 (EC 2.3.2.27) (Function required for yeast viability protein 10) (Glucose-induced degradation protein 9) (Probable E3 ubiquitin-protein ligase GID9)

 FYV10_YEAST             Reviewed;         516 AA.
 P40492; D6VVJ0;
 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
 01-FEB-1995, sequence version 1.
 25-MAY-2022, entry version 155.
 RecName: Full=Protein FYV10;
          EC=2.3.2.27 {ECO:0000305|PubMed:22044534};
 AltName: Full=Function required for yeast viability protein 10;
 AltName: Full=Glucose-induced degradation protein 9;
 AltName: Full=Probable E3 ubiquitin-protein ligase GID9 {ECO:0000303|PubMed:22044534};
 Name=FYV10; Synonyms=GID9 {ECO:0000303|PubMed:22044534};
 OrderedLocusNames=YIL097W;
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
 Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
 Saccharomycetales; Saccharomycetaceae; Saccharomyces.
 NCBI_TaxID=559292;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=ATCC 204508 / S288c;
 PubMed=9169870;
 Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
 Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
 Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
 Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
 Walsh S.V., Whitehead S., Barrell B.G.;
 "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
 Nature 387:84-87(1997).
 [2]
 GENOME REANNOTATION.
 STRAIN=ATCC 204508 / S288c;
 PubMed=24374639; DOI=10.1534/g3.113.008995;
 Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
 Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
 Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
 "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
 G3 (Bethesda) 4:389-398(2014).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 STRAIN=ATCC 204508 / S288c;
 PubMed=17322287; DOI=10.1101/gr.6037607;
 Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
 Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
 Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
 Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
 LaBaer J.;
 "Approaching a complete repository of sequence-verified protein-encoding
 clones for Saccharomyces cerevisiae.";
 Genome Res. 17:536-543(2007).
 [4]
 FUNCTION.
 PubMed=12663529; DOI=10.1093/genetics/163.3.875;
 Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M.,
 Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M.,
 Bussey H.;
 "A Saccharomyces cerevisiae genome-wide mutant screen for altered
 sensitivity to K1 killer toxin.";
 Genetics 163:875-894(2003).
 [5]
 FUNCTION.
 PubMed=12686616; DOI=10.1091/mbc.e02-08-0456;
 Regelmann J., Schuele T., Josupeit F.S., Horak J., Rose M., Entian K.-D.,
 Thumm M., Wolf D.H.;
 "Catabolite degradation of fructose-1,6-bisphosphatase in the yeast
 Saccharomyces cerevisiae: a genome-wide screen identifies eight novel GID
 genes and indicates the existence of two degradation pathways.";
 Mol. Biol. Cell 14:1652-1663(2003).
 [6]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
 PubMed=14562095; DOI=10.1038/nature02026;
 Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
 Weissman J.S., O'Shea E.K.;
 "Global analysis of protein localization in budding yeast.";
 Nature 425:686-691(2003).
 [7]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
 PubMed=14562106; DOI=10.1038/nature02046;
 Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
 O'Shea E.K., Weissman J.S.;
 "Global analysis of protein expression in yeast.";
 Nature 425:737-741(2003).
 [8]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=19779198; DOI=10.1126/science.1172867;
 Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
 "Global analysis of Cdk1 substrate phosphorylation sites provides insights
 into evolution.";
 Science 325:1682-1686(2009).
 [9]
 FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH RMD5, PATHWAY, AND
 MUTAGENESIS OF CYS-434.
 PubMed=22044534; DOI=10.1016/j.febslet.2011.10.038;
 Braun B., Pfirrmann T., Menssen R., Hofmann K., Scheel H., Wolf D.H.;
 "Gid9, a second RING finger protein contributes to the ubiquitin ligase
 activity of the Gid complex required for catabolite degradation.";
 FEBS Lett. 585:3856-3861(2011).
 [10]
 SUBUNIT, AND INTERACTION WITH VID28; GID8 AND RMD5.
 PubMed=22645139; DOI=10.1074/jbc.m112.363762;
 Menssen R., Schweiggert J., Schreiner J., Kusevic D., Reuther J., Braun B.,
 Wolf D.H.;
 "Exploring the topology of the Gid complex, the E3 ubiquitin ligase
 involved in catabolite-induced degradation of gluconeogenic enzymes.";
 J. Biol. Chem. 287:25602-25614(2012).
 -!- FUNCTION: Required for the adaptation to the presence of glucose in the
     growth medium; mediates the degradation of enzymes involved in
     gluconeogenesis when cells are shifted to glucose-containing medium
     (PubMed:12686616, PubMed:22044534). Required for proteasome-dependent
     catabolite degradation of fructose-1,6-bisphosphatase (FBP1)
     (PubMed:12686616, PubMed:22044534). May catalyze ubiquitination of
     target proteins in complex with RMD5 (Probable). Required for survival
     upon exposure to K1 killer toxin (PubMed:12663529).
     {ECO:0000269|PubMed:12663529, ECO:0000269|PubMed:12686616,
     ECO:0000269|PubMed:22044534, ECO:0000305}.
 -!- CATALYTIC ACTIVITY:
     Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
       [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
       cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
       EC=2.3.2.27; Evidence={ECO:0000305|PubMed:22044534};
 -!- PATHWAY: Protein modification; protein ubiquitination.
     {ECO:0000269|PubMed:22044534}.
 -!- SUBUNIT: Identified in the GID complex. In the absence of glucose, the
     complex contains VID30/GID1, the E3 ubiquitin-ligase RMD5/GID2,
     VID28/GID5, GID7, GID8, and FYV10/GID9. When cells are shifted to
     glucose-containing medium, VID24/GID4 is induced and becomes part of
     the complex (PubMed:22645139). Interacts with RMD5/GID2; the
     interaction is direct (PubMed:22044534). Within the GID complex,
     interacts directly with VID28/GID5, GID8 and RMD5/GID2
     (PubMed:22645139). {ECO:0000269|PubMed:22044534,
     ECO:0000269|PubMed:22645139}.
 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
     {ECO:0000269|PubMed:14562095}.
 -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
     {ECO:0000269|PubMed:14562106}.
 -!- SIMILARITY: Belongs to the FYV10 family. {ECO:0000305}.
 -!- CAUTION: It is not certain that this protein has E3 ubiquitin-protein
     ligase activity by itself. Lacks a detectable RING-type zinc finger
     domain; the sequence in this region is highly divergent and lacks most
     of the expected Cys residues. Still, Cys-434 in this highly divergent
     region is required for ubiquitination of FBP1, suggesting a direct role
     in catalyzing ubiquitination. {ECO:0000305|PubMed:22044534}.
 ---------------------------------------------------------------------------
 Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
 Distributed under the Creative Commons Attribution (CC BY 4.0) License
 ---------------------------------------------------------------------------
 EMBL; Z38125; CAA86284.1; -; Genomic_DNA.
 EMBL; AY692905; AAT92924.1; -; Genomic_DNA.
 EMBL; BK006942; DAA08456.1; -; Genomic_DNA.
 PIR; S48476; S48476.
 RefSeq; NP_012169.1; NM_001179445.1.
 PDB; 6SWY; EM; 3.20 A; 9=1-431.
 PDB; 7NS4; EM; 3.90 A; i=1-516.
 PDBsum; 6SWY; -.
 PDBsum; 7NS4; -.
 AlphaFoldDB; P40492; -.
 SMR; P40492; -.
 BioGRID; 34894; 271.
 ComplexPortal; CPX-301; GID ubiquitin ligase complex.
 DIP; DIP-4148N; -.
 IntAct; P40492; 6.
 MINT; P40492; -.
 STRING; 4932.YIL097W; -.
 MaxQB; P40492; -.
 PaxDb; P40492; -.
 PRIDE; P40492; -.
 EnsemblFungi; YIL097W_mRNA; YIL097W; YIL097W.
 GeneID; 854710; -.
 KEGG; sce:YIL097W; -.
 SGD; S000001359; FYV10.
 VEuPathDB; FungiDB:YIL097W; -.
 eggNOG; KOG0396; Eukaryota.
 GeneTree; ENSGT00940000153203; -.
 HOGENOM; CLU_027445_2_0_1; -.
 InParanoid; P40492; -.
 OMA; DVKYDEW; -.
 UniPathway; UPA00143; -.
 PRO; PR:P40492; -.
 Proteomes; UP000002311; Chromosome IX.
 RNAct; P40492; protein.
 GO; GO:0005737; C:cytoplasm; HDA:SGD.
 GO; GO:0034657; C:GID complex; IDA:SGD.
 GO; GO:0005634; C:nucleus; HDA:SGD.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
 GO; GO:0043066; P:negative regulation of apoptotic process; IMP:SGD.
 GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:SGD.
 GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
 InterPro; IPR024964; CTLH/CRA.
 InterPro; IPR006595; CTLH_C.
 InterPro; IPR027714; Fyv10/MAEA.
 InterPro; IPR045098; Fyv10_fam.
 InterPro; IPR044063; ZF_RING_GID.
 PANTHER; PTHR12170; PTHR12170; 1.
 PANTHER; PTHR12170:SF2; PTHR12170:SF2; 1.
 Pfam; PF10607; CLTH; 1.
 SMART; SM00668; CTLH; 1.
 PROSITE; PS50897; CTLH; 1.
 PROSITE; PS51867; ZF_RING_GID; 1.
 1: Evidence at protein level;
 3D-structure; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
 Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
 CHAIN           1..516
                 /note="Protein FYV10"
                 /id="PRO_0000202970"
 DOMAIN          187..245
                 /note="CTLH"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
 ZN_FING         434..501
                 /note="RING-Gid-type"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
 SITE            434
                 /note="Essential for ubiquitin ligase activity"
                 /evidence="ECO:0000269|PubMed:22044534"
 MUTAGEN         434
                 /note="C->S: Abolishes FBP1 ubiquitination and
                 degradation."
                 /evidence="ECO:0000269|PubMed:22044534"
 HELIX           225..239
                 /evidence="ECO:0007829|PDB:6SWY"
 HELIX           243..253
                 /evidence="ECO:0007829|PDB:6SWY"
 HELIX           256..258
                 /evidence="ECO:0007829|PDB:6SWY"
 HELIX           262..278
                 /evidence="ECO:0007829|PDB:6SWY"
 HELIX           304..312
                 /evidence="ECO:0007829|PDB:6SWY"
 HELIX           346..349
                 /evidence="ECO:0007829|PDB:6SWY"
 HELIX           353..370
                 /evidence="ECO:0007829|PDB:6SWY"
 SEQUENCE   516 AA;  59894 MW;  2EACCF8C6C314D56 CRC64;
 MAEKSIFNEP DVDFHLKLNQ QLFHIPYELL SKRIKHTQAV INKETKSLHE HTAALNQIFE
 HNDVEHDELA LAKITEMIRK VDHIERFLNT QIKSYCQILN RIKKRLEFFH ELKDIKSQNS
 GTSHNGNNEG TRTKLIQWYQ SYTNILIGDY LTRNNPIKYN SETKDHWNSG VVFLKQSQLD
 DLIDYDVLLE ANRISTSLLH ERNLLPLISW INENKKTLTK KSSILEFQAR LQEYIELLKV
 DNYTDAIVCF QRFLLPFVKS NFTDLKLASG LLIFIKYCND QKPTSSTSSG FDTEEIKSQS
 LPMKKDRIFQ HFFHKSLPRI TSKPAVNTTD YDKSSLINLQ SGDFERYLNL LDDQRWSVLN
 DLFLSDFYSM YGISQNDPLL IYLSLGISSL KTRDCLHPSD DENGNQETET ATTAEKEVED
 LQLFTLHSLK RKNCPVCSET FKPITQALPF AHHIQSQLFE NPILLPNGNV YDSKKLKKLA
 KTLKKQNLIS LNPGQIMDPV DMKIFCESDS IKMYPT

Related products :