MET30_YEAST
ID MET30_YEAST Reviewed; 640 AA.
AC P39014; D6VVN6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=F-box protein MET30 {ECO:0000305};
DE AltName: Full=E3 ubiquitin ligase complex SCF(Met30) subunit MET30;
DE AltName: Full=Methionine-requiring protein 30;
GN Name=MET30 {ECO:0000303|PubMed:8524217, ECO:0000312|SGD:S000001308};
GN OrderedLocusNames=YIL046W {ECO:0000312|SGD:S000001308};
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 [GENOMIC DNA], FUNCTION, AND INTERACTION WITH MET4.
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=8524217; DOI=10.1128/mcb.15.12.6526;
RA Thomas D., Kuras L., Barbey R., Cherest H., Blaiseau P.L.,
RA Surdin-Kerjan Y.;
RT "Met30p, a yeast transcriptional inhibitor that responds to S-
RT adenosylmethionine, is an essential protein with WD40 repeats.";
RL Mol. Cell. Biol. 15:6526-6534(1995).
RN [2]
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 [3]
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 [4]
RP INTERACTION WITH SKP1/CBF3D AND CDC53.
RX PubMed=9499404; DOI=10.1101/gad.12.5.692;
RA Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L.,
RA Tyers M.;
RT "Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein
RT complexes that regulate cell division and methionine biosynthesis in
RT yeast.";
RL Genes Dev. 12:692-705(1998).
RN [5]
RP FUNCTION, SUBUNIT, AND PATHWAY.
RX PubMed=9716410; DOI=10.1101/gad.12.16.2587;
RA Kaiser P., Sia R.A.L., Bardes E.S.G., Lew D.J., Reed S.I.;
RT "Cdc34 and the F-box protein Met30 are required for degradation of the Cdk-
RT inhibitory kinase Swe1.";
RL Genes Dev. 12:2587-2597(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH MET4 AND
RP SKP1/CBF3D.
RX PubMed=10637232; DOI=10.1093/emboj/19.2.282;
RA Rouillon A., Barbey R., Patton E.E., Tyers M., Thomas D.;
RT "Feedback-regulated degradation of the transcriptional activator Met4 is
RT triggered by the SCF(Met30) complex.";
RL EMBO J. 19:282-294(2000).
RN [7]
RP INDUCTION.
RX PubMed=11027256; DOI=10.1128/mcb.20.21.7845-7852.2000;
RA Smothers D.B., Kozubowski L., Dixon C., Goebl M.G., Mathias N.;
RT "The abundance of Met30p limits SCF(Met30p) complex activity and is
RT regulated by methionine availability.";
RL Mol. Cell. Biol. 20:7845-7852(2000).
RN [8]
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 [9]
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 [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SKP1/CBF3D,
RP HOMOMULTIMERIZATION, AND MUTAGENESIS OF LEU-187 AND GLU-190.
RX PubMed=14660673; DOI=10.1074/jbc.m308875200;
RA Brunson L.E., Dixon C., Kozubowski L., Mathias N.;
RT "The amino-terminal portion of the F-box protein Met30p mediates its
RT nuclear import and assimilation into an SCF complex.";
RL J. Biol. Chem. 279:6674-6682(2004).
RN [11]
RP FUNCTION.
RX PubMed=15689486; DOI=10.1091/mbc.e04-12-1130;
RA Yen J.L., Su N.Y., Kaiser P.;
RT "The yeast ubiquitin ligase SCFMet30 regulates heavy metal response.";
RL Mol. Biol. Cell 16:1872-1882(2005).
RN [12]
RP FUNCTION.
RX PubMed=15870262; DOI=10.1128/mcb.25.10.3875-3885.2005;
RA Su N.Y., Flick K., Kaiser P.;
RT "The F-box protein Met30 is required for multiple steps in the budding
RT yeast cell cycle.";
RL Mol. Cell. Biol. 25:3875-3885(2005).
RN [13]
RP INTERACTION WITH MET4, AND MUTAGENESIS OF LEU-386; ASN-425; GLN-467 AND
RP LEU-530.
RX PubMed=15883825; DOI=10.1007/s00438-005-1137-6;
RA Brunson L.E., Dixon C., LeFebvre A., Sun L., Mathias N.;
RT "Identification of residues in the WD-40 repeat motif of the F-box protein
RT Met30p required for interaction with its substrate Met4p.";
RL Mol. Genet. Genomics 273:361-370(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP 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 [17]
RP FUNCTION, AND PATHWAY.
RX PubMed=33443148; DOI=10.1073/pnas.2005539118;
RA Feng Y., Ariosa A.R., Yang Y., Hu Z., Dengjel J., Klionsky D.J.;
RT "Downregulation of autophagy by Met30-mediated Atg9 ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
CC -!- FUNCTION: Substrate-recognition component of the SCF(Met30) complex, an
CC E3 ubiquitin ligase complex that mediates the ubiquitination and
CC subsequent proteasomal degradation of target proteins (PubMed:9716410,
CC PubMed:10637232, PubMed:14660673). Negatively regulates sulfur amino
CC acids biosynthesis genes expression (PubMed:8524217, PubMed:15689486,
CC PubMed:15870262). Controls cell cycle function (being required for the
CC G1/S transition and M-phase but not the S-phase), sulfur metabolism,
CC and methionine biosynthesis as part of the SCF(Met30) complex
CC (PubMed:8524217, PubMed:15689486, PubMed:15870262). Required for the
CC efficient binding of CDC45 and MCM proteins to origins of replication
CC (PubMed:8524217, PubMed:15689486, PubMed:15870262). Required for
CC efficient expression of G1 cyclins (PubMed:15870262). The SCF(Met30)
CC complex catalyzes ubiquitination and degradation of the Cdk-inhibitory
CC kinase SWE1 (PubMed:9716410). Involved in the S-adenosylmethionine
CC (AdoMet)-mediated inhibition of the transcription function of MET4
CC (PubMed:8524217, PubMed:10637232). The SCF(Met30) complex mediates
CC ubiquitination and subsequent degradation of MET4 and the cellular
CC response to cadmium (PubMed:10637232). The SCF(Met30) complex acts as
CC an inhibitor of autophagy by promoting ubiquitination and degradation
CC of ATG9 in normal conditions (PubMed:33443148).
CC {ECO:0000269|PubMed:10637232, ECO:0000269|PubMed:14660673,
CC ECO:0000269|PubMed:15689486, ECO:0000269|PubMed:15870262,
CC ECO:0000269|PubMed:33443148, ECO:0000269|PubMed:8524217,
CC ECO:0000269|PubMed:9716410}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:33443148, ECO:0000269|PubMed:9716410}.
CC -!- SUBUNIT: Homomultimer (PubMed:14660673). Interacts with CDC53 and
CC SKP1/CBF3D to form the E3 ubiquitin ligase complex SCF(Met30)
CC (PubMed:14660673, PubMed:9499404, PubMed:9716410, PubMed:33443148).
CC Interacts with MET4 (PubMed:10637232, PubMed:15883825, PubMed:8524217).
CC {ECO:0000269|PubMed:10637232, ECO:0000269|PubMed:14660673,
CC ECO:0000269|PubMed:15883825, ECO:0000269|PubMed:33443148,
CC ECO:0000269|PubMed:8524217, ECO:0000269|PubMed:9499404,
CC ECO:0000269|PubMed:9716410}.
CC -!- INTERACTION:
CC P39014; Q12018: CDC53; NbExp=10; IntAct=EBI-11507, EBI-4321;
CC P39014; P39014: MET30; NbExp=2; IntAct=EBI-11507, EBI-11507;
CC P39014; P32389: MET4; NbExp=7; IntAct=EBI-11507, EBI-10757;
CC P39014; P52286: SKP1; NbExp=14; IntAct=EBI-11507, EBI-4090;
CC P39014; Q12020: SRL2; NbExp=3; IntAct=EBI-11507, EBI-38714;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14660673}. Nucleus
CC {ECO:0000269|PubMed:10637232, ECO:0000269|PubMed:14660673}.
CC -!- INDUCTION: Transcriptional activation requires MET4 as well as MET31
CC and MET32. Regulated by intracellular AdoMet levels. L-methionine
CC regulates the abundance of MET30. The amount of MET30 regulates the
CC activity of the E3 ubiquitin ligase complex SCF(Met30).
CC {ECO:0000269|PubMed:10637232, ECO:0000269|PubMed:11027256}.
CC -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
CC {ECO:0000305}.
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DR EMBL; Z46861; CAA86905.1; -; Genomic_DNA.
DR EMBL; L26505; AAA96717.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08502.1; -; Genomic_DNA.
DR PIR; S49932; S49932.
DR RefSeq; NP_012218.1; NM_001179396.1.
DR AlphaFoldDB; P39014; -.
DR SMR; P39014; -.
DR BioGRID; 34944; 485.
DR ComplexPortal; CPX-3249; SCF-Met30 ubiquitin ligase complex.
DR DIP; DIP-1439N; -.
DR IntAct; P39014; 91.
DR MINT; P39014; -.
DR STRING; 4932.YIL046W; -.
DR iPTMnet; P39014; -.
DR MaxQB; P39014; -.
DR PaxDb; P39014; -.
DR PRIDE; P39014; -.
DR EnsemblFungi; YIL046W_mRNA; YIL046W; YIL046W.
DR GeneID; 854765; -.
DR KEGG; sce:YIL046W; -.
DR SGD; S000001308; MET30.
DR VEuPathDB; FungiDB:YIL046W; -.
DR eggNOG; KOG0274; Eukaryota.
DR GeneTree; ENSGT00940000174309; -.
DR HOGENOM; CLU_000288_103_1_1; -.
DR InParanoid; P39014; -.
DR OMA; PTHTACY; -.
DR BioCyc; YEAST:G3O-31317-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P39014; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P39014; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IC:ComplexPortal.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IDA:SGD.
DR GO; GO:0046686; P:response to cadmium ion; IDA:SGD.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IGI:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Cell cycle; Cysteine biosynthesis; Cytoplasm;
KW Methionine biosynthesis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation pathway;
KW WD repeat.
FT CHAIN 1..640
FT /note="F-box protein MET30"
FT /id="PRO_0000051087"
FT DOMAIN 181..227
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 300..328
FT /note="WD 1"
FT REPEAT 340..368
FT /note="WD 2"
FT REPEAT 380..408
FT /note="WD 3"
FT REPEAT 419..449
FT /note="WD 4"
FT REPEAT 461..499
FT /note="WD 5"
FT REPEAT 509..538
FT /note="WD 6"
FT REPEAT 550..578
FT /note="WD 7"
FT REPEAT 607..635
FT /note="WD 8"
FT REGION 1..299
FT /note="Necessary to mediate nuclear localization"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..277
FT /note="Important for mediating homomultimerization"
FT REGION 180..225
FT /note="Interaction with SKP1/CBF3D"
FT REGION 277..640
FT /note="Interaction with MET4"
FT REGION 481..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 187
FT /note="L->D: Strongly reduces nuclear localization;
FT inhibits interaction with SKP1/CBF3D."
FT /evidence="ECO:0000269|PubMed:14660673"
FT MUTAGEN 190
FT /note="E->A: Strongly reduces nuclear localization;
FT inhibits interaction with SKP1/CBF3D."
FT /evidence="ECO:0000269|PubMed:14660673"
FT MUTAGEN 386
FT /note="L->D: Inactivates MET30 and prevents MET4
FT interaction; when associated with A-425 and A-467."
FT /evidence="ECO:0000269|PubMed:15883825"
FT MUTAGEN 425
FT /note="N->A: Inactivates MET30 and prevents MET4
FT interaction; when associated with D-530 or D-386 and A-
FT 467."
FT /evidence="ECO:0000269|PubMed:15883825"
FT MUTAGEN 467
FT /note="Q->A: Inactivates MET30 and prevents MET4
FT interaction; when associated with D-386 and A-425."
FT /evidence="ECO:0000269|PubMed:15883825"
FT MUTAGEN 530
FT /note="L->D: Inactivates MET30 and prevents MET4
FT interaction; when associated with A-425."
FT /evidence="ECO:0000269|PubMed:15883825"
FT CONFLICT 61
FT /note="M -> I (in Ref. 1; AAA96717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 640 AA; 72835 MW; 5135D4BCA2E1EB97 CRC64;
MRRERQRMMS FEDKDKDDLD NSNSNNSSEM TDTAMMPPLK RLLITGSSDD LAQGSSGKKK
MTMATRSPSS SPDLATNDSG TRVQPLPEYN FTKFCYRHNP DIQFSPTHTA CYKQDLKRTQ
EINANIAKLP LQEQSDIHHI ISKYSNSNDK IRKLILDGIL STSCFPQLSY ISSLVTHMIK
IDFISILPQE LSLKILSYLD CQSLCNATRV CRKWQKLADD DRVWYHMCEQ HIDRKCPNCG
WGLPLLHMKR ARIQQNSTGS SSNADIQTQT TRPWKVIYRE RFKVESNWRK GHCRIQEFKG
HMDGVLTLQF NYRLLFTGSY DSTIGIWDLF TGKLIRRLSG HSDGVKTLYF DDRKLITGSL
DKTIRVWNYI TGECISTYRG HSDSVLSVDS YQKVIVSGSA DKTVKVWHVE SRTCYTLRGH
TEWVNCVKLH PKSFSCFSCS DDTTIRMWDI RTNSCLKVFR GHVGQVQKII PLTIKDVENL
ATDNTSDGSS PQDDPTMTDG ADESDTPSNE QETVLDENIP YPTHLLSCGL DNTIKLWDVK
TGKCIRTQFG HVEGVWDIAA DNFRIISGSH DGSIKVWDLQ SGKCMHTFNG RRLQRETQHT
QTQSLGDKVA PIACVCIGDS ECFSGDEFGC VKMYKFDLND
