MIG3_YEAST
ID MIG3_YEAST Reviewed; 394 AA.
AC P39943; D3DLS7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transcription corepressor MIG3;
DE AltName: Full=Multicopy inhibitor of growth protein 3;
GN Name=MIG3; OrderedLocusNames=YER028C;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 INDUCTION.
RX PubMed=12161108; DOI=10.1016/s0143-4160(02)00110-0;
RA Lombardia L.J., Becerra M., Rodriguez-Belmonte E., Hauser N.C.,
RA Cerdan M.E.;
RT "Genome-wide analysis of yeast transcription upon calcium shortage.";
RL Cell Calcium 32:83-91(2002).
RN [4]
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 [5]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=14993292; DOI=10.1128/mcb.24.6.2560-2572.2004;
RA Dubacq C., Chevalier A., Mann C.;
RT "The protein kinase Snf1 is required for tolerance to the ribonucleotide
RT reductase inhibitor hydroxyurea.";
RL Mol. Cell. Biol. 24:2560-2572(2004).
CC -!- FUNCTION: DNA-binding transcriptional repressor involved in response to
CC toxic agents such as ribonucleotide reductase inhibitor, hydroxyurea
CC (HU). {ECO:0000269|PubMed:14993292}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Down-regulated at low calcium levels.
CC {ECO:0000269|PubMed:12161108}.
CC -!- PTM: Phosphorylated during genotoxic stress. DNA damage induces
CC phosphorylation by SNF1 or the MEC1 pathway and leads to its
CC inactivation, which allows induction of damage response genes.
CC {ECO:0000269|PubMed:14993292}.
CC -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U18778; AAB64561.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07681.1; -; Genomic_DNA.
DR PIR; S50486; S50486.
DR RefSeq; NP_010945.1; NM_001178919.1.
DR AlphaFoldDB; P39943; -.
DR BioGRID; 36763; 37.
DR DIP; DIP-2545N; -.
DR IntAct; P39943; 4.
DR MINT; P39943; -.
DR STRING; 4932.YER028C; -.
DR MaxQB; P39943; -.
DR PaxDb; P39943; -.
DR PRIDE; P39943; -.
DR EnsemblFungi; YER028C_mRNA; YER028C; YER028C.
DR GeneID; 856750; -.
DR KEGG; sce:YER028C; -.
DR SGD; S000000830; MIG3.
DR VEuPathDB; FungiDB:YER028C; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_058878_0_0_1; -.
DR InParanoid; P39943; -.
DR OMA; NTGDMEI; -.
DR BioCyc; YEAST:G3O-30209-MON; -.
DR PRO; PR:P39943; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39943; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR GO; GO:0034644; P:cellular response to UV; IGI:SGD.
DR GO; GO:0010768; P:negative regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; IMP:SGD.
DR GO; GO:0000430; P:regulation of transcription from RNA polymerase II promoter by glucose; IMP:SGD.
DR GO; GO:0045471; P:response to ethanol; IMP:SGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..394
FT /note="Transcription corepressor MIG3"
FT /id="PRO_0000046886"
FT ZN_FING 17..39
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 45..69
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 43119 MW; 5218D1A0F117BEBB CRC64;
MNYLRDRFPP DNDQRPFRCE ICSRGFHRLE HKKRHGRTHT GEKPHKCTVQ GCPKSFSRSD
ELKRHLRTHT KGVQRRRIKS KGSRKTVVNT ATAAPTTFNE NTGVSLTGIG QSKVPPILIS
VAQNCDDVNI RNTGNNNGIV ETQAPAILVP VINIPNDPHP IPSSLSTTSI TSIASVYPST
SPFQYLKSGF PEDPASTPYV HSSGSSLALG ELSSNSSIFS KSRRNLAAMS GPDSLSSSKN
QSSASLLSQT SHPSKSFSRP PTDLSPLRRI MPSVNTGDME ISRTVSVSSS SSSLTSVTYD
DTAAKDMGMG IFFDRPPVTQ KACRSNHKYK VNAVSRGRQH ERAQFHISGD DEDSNVHRQE
SRASNTSPNV SLPPIKSILR QIDNFNSAPS YFSK
