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MIG2_YEAST
ID   MIG2_YEAST              Reviewed;         382 AA.
AC   P53035; D6VTU6; O11853; O11854;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Regulatory protein MIG2;
GN   Name=MIG2; Synonyms=MLZ1; OrderedLocusNames=YGL209W;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8756637; DOI=10.1128/mcb.16.9.4790;
RA   Lutfiyya L.L., Johnston M.;
RT   "Two zinc-finger-containing repressors are responsible for glucose
RT   repression of SUC2 expression.";
RL   Mol. Cell. Biol. 16:4790-4797(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8813766;
RX   DOI=10.1002/(sici)1097-0061(19960630)12:8<799::aid-yea965>3.0.co;2-u;
RA   Kail M., Juettner E., Vaux D.;
RT   "Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces
RT   cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and
RT   containing three novel transcribed open reading frames.";
RL   Yeast 12:799-807(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9153757;
RX   DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0;
RA   Feuermann M., Simeonava L., Souciet J.-L., Potier S.;
RT   "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII
RT   reveals 11 open reading frames: two correspond to new genes.";
RL   Yeast 13:475-477(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [5]
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   [6]
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).
CC   -!- FUNCTION: Involved in glucose repression of the SUC2 gene.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
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DR   EMBL; U54564; AAB37570.1; -; Genomic_DNA.
DR   EMBL; U33754; AAC49496.1; -; Genomic_DNA.
DR   EMBL; Z72731; CAA96923.2; -; Genomic_DNA.
DR   EMBL; Z72731; CAA96924.1; -; Genomic_DNA.
DR   EMBL; Z72730; CAA96921.1; -; Genomic_DNA.
DR   EMBL; Z72732; CAA96925.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA07907.1; -; Genomic_DNA.
DR   PIR; S71669; S71669.
DR   RefSeq; NP_011306.1; NM_001181074.1.
DR   AlphaFoldDB; P53035; -.
DR   SMR; P53035; -.
DR   BioGRID; 33047; 109.
DR   IntAct; P53035; 7.
DR   STRING; 4932.YGL209W; -.
DR   MaxQB; P53035; -.
DR   PaxDb; P53035; -.
DR   PRIDE; P53035; -.
DR   EnsemblFungi; YGL209W_mRNA; YGL209W; YGL209W.
DR   GeneID; 852663; -.
DR   KEGG; sce:YGL209W; -.
DR   SGD; S000003177; MIG2.
DR   VEuPathDB; FungiDB:YGL209W; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000169836; -.
DR   HOGENOM; CLU_039422_0_0_1; -.
DR   InParanoid; P53035; -.
DR   OMA; HQPIPQV; -.
DR   BioCyc; YEAST:G3O-30686-MON; -.
DR   PRO; PR:P53035; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53035; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
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:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000433; P:carbon catabolite repression of transcription from RNA polymerase II promoter by glucose; IDA:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IGI:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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   Carbohydrate metabolism; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..382
FT                   /note="Regulatory protein MIG2"
FT                   /id="PRO_0000046882"
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          252..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   382 AA;  42048 MW;  BE25CBC21FB962C6 CRC64;
     MPKKQTNFPV DNENRPFRCD TCHRGFHRLE HKKRHLRTHT GEKPHHCAFP GCGKSFSRSD
     ELKRHMRTHT GQSQRRLKKA SVQKQEFLTV SGIPTIASGV MIHQPIPQVL PANMAINVQA
     VNGGNIIHAP NAVHPMVIPI MAQPAPIHAS AASFQPATSP MPISTYTPVP SQSFTSFQSS
     IGSIQSNSDV SSIFSNMNVR VNTPRSVPNS PNDGYLHQQH IPQQYQHQTA SPSVAKQQKT
     FAHSLASALS TLQKRTPVSA PSTTIESPSS PSDSSHTSAS SSAISLPFSN APSQLAVAKE
     LESVYLDSNR YTTKTRRERA KFEIPEEQEE DTNNSSSGSN EEEHESLDHE SSKSRKKLSG
     VKLPPVRNLL KQIDVFNGPK RV
 
 
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