FYV10_YEAST
ID FYV10_YEAST Reviewed; 516 AA.
AC P40492; D6VVJ0;
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=Protein FYV10;
DE EC=2.3.2.27 {ECO:0000305|PubMed:22044534};
DE AltName: Full=Function required for yeast viability protein 10;
DE AltName: Full=Glucose-induced degradation protein 9;
DE AltName: Full=Probable E3 ubiquitin-protein ligase GID9 {ECO:0000303|PubMed:22044534};
GN Name=FYV10; Synonyms=GID9 {ECO:0000303|PubMed:22044534};
GN OrderedLocusNames=YIL097W;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=12663529; DOI=10.1093/genetics/163.3.875;
RA Page N., Gerard-Vincent M., Menard P., Beaulieu M., Azuma M.,
RA Dijkgraaf G.J.P., Li H., Marcoux J., Nguyen T., Dowse T., Sdicu A.-M.,
RA Bussey H.;
RT "A Saccharomyces cerevisiae genome-wide mutant screen for altered
RT sensitivity to K1 killer toxin.";
RL Genetics 163:875-894(2003).
RN [5]
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 [6]
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 [7]
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 [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 FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH RMD5, PATHWAY, AND
RP MUTAGENESIS OF CYS-434.
RX PubMed=22044534; DOI=10.1016/j.febslet.2011.10.038;
RA Braun B., Pfirrmann T., Menssen R., Hofmann K., Scheel H., Wolf D.H.;
RT "Gid9, a second RING finger protein contributes to the ubiquitin ligase
RT activity of the Gid complex required for catabolite degradation.";
RL FEBS Lett. 585:3856-3861(2011).
RN [10]
RP SUBUNIT, AND INTERACTION WITH VID28; GID8 AND RMD5.
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, PubMed:22044534). Required for proteasome-dependent
CC catabolite degradation of fructose-1,6-bisphosphatase (FBP1)
CC (PubMed:12686616, PubMed:22044534). May catalyze ubiquitination of
CC target proteins in complex with RMD5 (Probable). Required for survival
CC upon exposure to K1 killer toxin (PubMed:12663529).
CC {ECO:0000269|PubMed:12663529, ECO:0000269|PubMed:12686616,
CC ECO:0000269|PubMed:22044534, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305|PubMed:22044534};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:22044534}.
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). Interacts with RMD5/GID2; the
CC interaction is direct (PubMed:22044534). Within the GID complex,
CC interacts directly with VID28/GID5, GID8 and RMD5/GID2
CC (PubMed:22645139). {ECO:0000269|PubMed:22044534,
CC ECO:0000269|PubMed:22645139}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 784 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FYV10 family. {ECO:0000305}.
CC -!- CAUTION: It is not certain that this protein has E3 ubiquitin-protein
CC ligase activity by itself. Lacks a detectable RING-type zinc finger
CC domain; the sequence in this region is highly divergent and lacks most
CC of the expected Cys residues. Still, Cys-434 in this highly divergent
CC region is required for ubiquitination of FBP1, suggesting a direct role
CC in catalyzing ubiquitination. {ECO:0000305|PubMed:22044534}.
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DR EMBL; Z38125; CAA86284.1; -; Genomic_DNA.
DR EMBL; AY692905; AAT92924.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08456.1; -; Genomic_DNA.
DR PIR; S48476; S48476.
DR RefSeq; NP_012169.1; NM_001179445.1.
DR PDB; 6SWY; EM; 3.20 A; 9=1-431.
DR PDB; 7NS4; EM; 3.90 A; i=1-516.
DR PDBsum; 6SWY; -.
DR PDBsum; 7NS4; -.
DR AlphaFoldDB; P40492; -.
DR SMR; P40492; -.
DR BioGRID; 34894; 271.
DR ComplexPortal; CPX-301; GID ubiquitin ligase complex.
DR DIP; DIP-4148N; -.
DR IntAct; P40492; 6.
DR MINT; P40492; -.
DR STRING; 4932.YIL097W; -.
DR MaxQB; P40492; -.
DR PaxDb; P40492; -.
DR PRIDE; P40492; -.
DR EnsemblFungi; YIL097W_mRNA; YIL097W; YIL097W.
DR GeneID; 854710; -.
DR KEGG; sce:YIL097W; -.
DR SGD; S000001359; FYV10.
DR VEuPathDB; FungiDB:YIL097W; -.
DR eggNOG; KOG0396; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_027445_2_0_1; -.
DR InParanoid; P40492; -.
DR OMA; DVKYDEW; -.
DR BioCyc; YEAST:G3O-31356-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P40492; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40492; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP: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 InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR027714; Fyv10/MAEA.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR PANTHER; PTHR12170:SF2; PTHR12170:SF2; 1.
DR Pfam; PF10607; CLTH; 1.
DR SMART; SM00668; CTLH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..516
FT /note="Protein FYV10"
FT /id="PRO_0000202970"
FT DOMAIN 187..245
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 434..501
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT SITE 434
FT /note="Essential for ubiquitin ligase activity"
FT /evidence="ECO:0000269|PubMed:22044534"
FT MUTAGEN 434
FT /note="C->S: Abolishes FBP1 ubiquitination and
FT degradation."
FT /evidence="ECO:0000269|PubMed:22044534"
FT HELIX 225..239
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 262..278
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:6SWY"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:6SWY"
SQ 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
