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F-box protein MET30 (E3 ubiquitin ligase complex SCF(Met30) subunit MET30) (Methionine-requiring protein 30)

 MET30_YEAST             Reviewed;         640 AA.
P39014; D6VVN6;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
18-JUL-2018, entry version 182.
RecName: Full=F-box protein MET30;
AltName: Full=E3 ubiquitin ligase complex SCF(Met30) subunit MET30;
AltName: Full=Methionine-requiring protein 30;
Name=MET30; OrderedLocusNames=YIL046W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH
MET4.
STRAIN=ATCC 26786 / X2180-1A;
PubMed=8524217; DOI=10.1128/MCB.15.12.6526;
Thomas D., Kuras L., Barbey R., Cherest H., Blaiseau P.L.,
Surdin-Kerjan Y.;
"Met30p, a yeast transcriptional inhibitor that responds to S-
adenosylmethionine, is an essential protein with WD40 repeats.";
Mol. Cell. Biol. 15:6526-6534(1995).
[2]
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).
[3]
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).
[4]
INTERACTION WITH SKP1/CBF3D AND CDC53.
PubMed=9499404; DOI=10.1101/gad.12.5.692;
Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L.,
Tyers M.;
"Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein
complexes that regulate cell division and methionine biosynthesis in
yeast.";
Genes Dev. 12:692-705(1998).
[5]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH MET4
AND SKP1/CBF3D.
PubMed=10637232; DOI=10.1093/emboj/19.2.282;
Rouillon A., Barbey R., Patton E.E., Tyers M., Thomas D.;
"Feedback-regulated degradation of the transcriptional activator Met4
is triggered by the SCF(Met30) complex.";
EMBO J. 19:282-294(2000).
[6]
INDUCTION.
PubMed=11027256; DOI=10.1128/MCB.20.21.7845-7852.2000;
Smothers D.B., Kozubowski L., Dixon C., Goebl M.G., Mathias N.;
"The abundance of Met30p limits SCF(Met30p) complex activity and is
regulated by methionine availability.";
Mol. Cell. Biol. 20:7845-7852(2000).
[7]
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).
[8]
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).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SKP1/CBF3D,
HOMOMULTIMERIZATION, AND MUTAGENESIS OF LEU-187 AND GLU-190.
PubMed=14660673; DOI=10.1074/jbc.M308875200;
Brunson L.E., Dixon C., Kozubowski L., Mathias N.;
"The amino-terminal portion of the F-box protein Met30p mediates its
nuclear import and assimilation into an SCF complex.";
J. Biol. Chem. 279:6674-6682(2004).
[10]
FUNCTION.
PubMed=15689486; DOI=10.1091/mbc.E04-12-1130;
Yen J.L., Su N.Y., Kaiser P.;
"The yeast ubiquitin ligase SCFMet30 regulates heavy metal response.";
Mol. Biol. Cell 16:1872-1882(2005).
[11]
FUNCTION.
PubMed=15870262; DOI=10.1128/MCB.25.10.3875-3885.2005;
Su N.Y., Flick K., Kaiser P.;
"The F-box protein Met30 is required for multiple steps in the budding
yeast cell cycle.";
Mol. Cell. Biol. 25:3875-3885(2005).
[12]
INTERACTION WITH MET4, AND MUTAGENESIS OF LEU-386; ASN-425; GLN-467
AND LEU-530.
PubMed=15883825; DOI=10.1007/s00438-005-1137-6;
Brunson L.E., Dixon C., LeFebvre A., Sun L., Mathias N.;
"Identification of residues in the WD-40 repeat motif of the F-box
protein Met30p required for interaction with its substrate Met4p.";
Mol. Genet. Genomics 273:361-370(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND 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).
-!- FUNCTION: Negatively regulates sulfur amino acids biosynthesis
genes expression. Controls cell cycle function (being required for
the G1/S transition and M-phase but not the S-phase), sulfur
metabolism, and methionine biosynthesis as part of the E3
ubiquitin ligase complex SCF(Met30). Required for the efficient
binding of CDC45 and MCM proteins to origins of replication.
Involved in the S-adenosylmethionine (AdoMet)-mediated inhibition
of the transcription function of MET4. In the context of the E3
ubiquitin ligase complex SCF(Met30), involved in the degradation
of MET4 and the cellular response to cadmium. Required for
efficient expression of G1 cyclins. {ECO:0000269|PubMed:10637232,
ECO:0000269|PubMed:14660673, ECO:0000269|PubMed:15689486,
ECO:0000269|PubMed:15870262, ECO:0000269|PubMed:8524217}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Homomultimer. Interacts with MET4. Interacts with CDC53
and SKP1/CBF3D to form the E3 ubiquitin ligase complex SCF(Met30).
{ECO:0000269|PubMed:10637232, ECO:0000269|PubMed:14660673,
ECO:0000269|PubMed:15883825, ECO:0000269|PubMed:8524217,
ECO:0000269|PubMed:9499404}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-11507, EBI-11507;
Q12018:CDC53; NbExp=10; IntAct=EBI-11507, EBI-4321;
P32389:MET4; NbExp=7; IntAct=EBI-11507, EBI-10757;
P52286:SKP1; NbExp=14; IntAct=EBI-11507, EBI-4090;
Q12020:SRL2; NbExp=3; IntAct=EBI-11507, EBI-38714;
A0A0C4DGF1:ZBTB32 (xeno); NbExp=3; IntAct=EBI-11507, EBI-10188476;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- INDUCTION: Transcriptional activation requires MET4 as well as
MET31 and MET32. Regulated by intracellular AdoMet levels. L-
methionine regulates the abundance of MET30. The amount of MET30
regulates the activity of the E3 ubiquitin ligase complex
SCF(Met30). {ECO:0000269|PubMed:10637232,
ECO:0000269|PubMed:11027256}.
-!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the WD repeat MET30/SCONB/SCON-2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z46861; CAA86905.1; -; Genomic_DNA.
EMBL; L26505; AAA96717.1; -; Genomic_DNA.
EMBL; BK006942; DAA08502.1; -; Genomic_DNA.
PIR; S49932; S49932.
RefSeq; NP_012218.1; NM_001179396.1.
ProteinModelPortal; P39014; -.
BioGrid; 34944; 480.
ComplexPortal; CPX-3249; SCF-Met30 ubiquitin ligase complex.
DIP; DIP-1439N; -.
IntAct; P39014; 98.
MINT; P39014; -.
STRING; 4932.YIL046W; -.
iPTMnet; P39014; -.
MaxQB; P39014; -.
PaxDb; P39014; -.
PRIDE; P39014; -.
EnsemblFungi; YIL046W; YIL046W; YIL046W.
GeneID; 854765; -.
KEGG; sce:YIL046W; -.
EuPathDB; FungiDB:YIL046W; -.
SGD; S000001308; MET30.
GeneTree; ENSGT00760000119106; -.
HOGENOM; HOG000166480; -.
InParanoid; P39014; -.
KO; K10259; -.
OMA; TQCCFPQ; -.
OrthoDB; EOG092C10HM; -.
BioCyc; YEAST:G3O-31317-MONOMER; -.
Reactome; R-SCE-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-SCE-8951664; Neddylation.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:P39014; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006270; P:DNA replication initiation; IMP:SGD.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:SGD.
GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0000209; P:protein polyubiquitination; IMP:SGD.
GO; GO:0016567; P:protein ubiquitination; IGI:SGD.
GO; GO:0030174; P:regulation of DNA-dependent DNA replication initiation; IMP:SGD.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
GO; GO:0046685; P:response to arsenic-containing substance; IDA:SGD.
GO; GO:0046686; P:response to cadmium ion; IDA:SGD.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IGI:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 3.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Amino-acid biosynthesis; Cell cycle; Complete proteome;
Cysteine biosynthesis; Cytoplasm; Methionine biosynthesis; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation; Ubl conjugation pathway; WD repeat.
CHAIN 1 640 F-box protein MET30.
/FTId=PRO_0000051087.
DOMAIN 181 227 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 300 328 WD 1.
REPEAT 340 368 WD 2.
REPEAT 380 408 WD 3.
REPEAT 419 449 WD 4.
REPEAT 461 499 WD 5.
REPEAT 509 538 WD 6.
REPEAT 550 578 WD 7.
REPEAT 607 635 WD 8.
REGION 1 299 Necessary to mediate nuclear
localization.
REGION 180 277 Important for mediating
homomultimerization.
REGION 180 225 Interaction with SKP1/CBF3D.
REGION 277 640 Interaction with MET4.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 187 187 L->D: Strongly reduces nuclear
localization; inhibits interaction with
SKP1/CBF3D.
{ECO:0000269|PubMed:14660673}.
MUTAGEN 190 190 E->A: Strongly reduces nuclear
localization; inhibits interaction with
SKP1/CBF3D.
{ECO:0000269|PubMed:14660673}.
MUTAGEN 386 386 L->D: Inactivates MET30 and prevents MET4
interaction; when associated with A-425
and A-467. {ECO:0000269|PubMed:15883825}.
MUTAGEN 425 425 N->A: Inactivates MET30 and prevents MET4
interaction; when associated with D-530
or D-386 and A-467.
{ECO:0000269|PubMed:15883825}.
MUTAGEN 467 467 Q->A: Inactivates MET30 and prevents MET4
interaction; when associated with D-386
and A-425. {ECO:0000269|PubMed:15883825}.
MUTAGEN 530 530 L->D: Inactivates MET30 and prevents MET4
interaction; when associated with A-425.
{ECO:0000269|PubMed:15883825}.
CONFLICT 61 61 M -> I (in Ref. 1; AAA96717).
{ECO:0000305}.
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


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