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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}.
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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


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