MIG1_KLULA
ID MIG1_KLULA Reviewed; 474 AA.
AC P50898;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Regulatory protein MIG1;
GN Name=MIG1; OrderedLocusNames=KLLA0E10989g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=7672126; DOI=10.1016/0014-5793(95)00909-s;
RA Cassart J.-P., Georis I., Oestling J., Ronne H., Vandenhaute J.;
RT "The MIG1 repressor from Kluyveromyces lactis: cloning, sequencing and
RT functional analysis in Saccharomyces cerevisiae.";
RL FEBS Lett. 371:191-194(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Involved in glucose repression of glucose metabolism genes.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the creA/MIG C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; Z50017; CAA90320.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99533.1; -; Genomic_DNA.
DR PIR; S66480; S66480.
DR RefSeq; XP_454446.1; XM_454446.1.
DR AlphaFoldDB; P50898; -.
DR SMR; P50898; -.
DR STRING; 28985.XP_454446.1; -.
DR EnsemblFungi; CAG99533; CAG99533; KLLA0_E11023g.
DR GeneID; 2894281; -.
DR KEGG; kla:KLLA0_E11023g; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_576273_0_0_1; -.
DR InParanoid; P50898; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
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 3: Inferred from homology;
KW Carbohydrate metabolism; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..474
FT /note="Regulatory protein MIG1"
FT /id="PRO_0000046879"
FT ZN_FING 26..48
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 54..78
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 52908 MW; 4A5F3EA3603B17C3 CRC64;
MTEAIIEKKN HKKSINDHDK DGPRPYVCPI CQRGFHRLEH QTRHIRTHTG ERPHACDFPG
CSKRFSRSDE LTRHRRIHDS DKPKGKRGRK KKSETIAREK ELELQRQKQR NANDSAAVDS
AGGTSANVIE PNHKLLKSTN SIKQDGSTFT EPLKSLRSKP MFDLGSDESD ECGIYSVPPI
RSQNNSGNID LLLNAAKFES DKASSSFKFI DKLPLTSSSS SPSLSFTSHS INNSSSGLLL
PRPASRAKLS ALSSLQRMTP LSQNSESYNH SQQNLVHLHH PAPNRPLTEF VDNEYISNGL
PRTRSWTNLS EQQSPSGFSS SALNSRFSSS NSLNQLIDQH SRNSSTVSIS TLLKQETVIS
QDEDMSTEDA YGRPLKKSKA IMPIMRPSST MPPSSGSATE GEFYDELHSR LRSMDQLPVR
NSKDEKDYYF QSHFSSLLCT PTHSPPPEGL LPSLNQNKPV QLPSLRSLDL LPPK
