STE12_KLULA
ID STE12_KLULA Reviewed; 666 AA.
AC Q08400; Q6CMW7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Protein STE12;
GN Name=STE12; OrderedLocusNames=KLLA0E17193g;
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].
RX PubMed=8339934; DOI=10.1101/gad.7.8.1584;
RA Yuan Y.-L.O., Stroke I., Fields S.;
RT "Coupling of cell identity to signal response in yeast: interaction between
RT the alpha-1 and STE12 proteins.";
RL Genes Dev. 7:1584-1597(1993).
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: Binds to the DNA sequence mediating pheromone induction
CC (called the pheromone response element = PRE) which is found in the
CC upstream control region of several a-, alpha- and haploid-specific
CC genes. Involved in the mating process (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylated by the STE7 and STE11 kinases. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the STE12 transcription factor family.
CC {ECO:0000305}.
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DR EMBL; L21156; AAA35270.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99809.1; -; Genomic_DNA.
DR PIR; A47650; A47650.
DR RefSeq; XP_454722.1; XM_454722.1.
DR AlphaFoldDB; Q08400; -.
DR SMR; Q08400; -.
DR DIP; DIP-234N; -.
DR STRING; 28985.XP_454722.1; -.
DR EnsemblFungi; CAG99809; CAG99809; KLLA0_E17139g.
DR GeneID; 2894276; -.
DR KEGG; kla:KLLA0_E17139g; -.
DR eggNOG; ENOG502QTVR; Eukaryota.
DR HOGENOM; CLU_019798_0_0_1; -.
DR InParanoid; Q08400; -.
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:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR InterPro; IPR003120; Ste12.
DR Pfam; PF02200; STE; 1.
DR SMART; SM00424; STE; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Nucleus; Pheromone response; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..666
FT /note="Protein STE12"
FT /id="PRO_0000072261"
FT DNA_BIND 51..161
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..636
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="T -> A (in Ref. 1; AAA35270)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="A -> R (in Ref. 1; AAA35270)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="G -> R (in Ref. 1; AAA35270)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 75759 MW; 96A95137E020E9F2 CRC64;
MTGSIVKTED ISSISGRGDT SQSPEEVEES LRLIEDLKFF LATAPANWQE NQVIRRYYLS
NDEGFVSCVF WNNLYYITGT DIVRCCAYRM QKFGREIVER KKFEEGIFSD LRNLKCGIDA
TLEKPKSDLL AFLYKNMCLK TQKKQKVFFW FSVPHDRLFA DALERDLKRS STGSQPTTRA
VSEPALSFRW EANSDVSLYD QITNHVDSQR TDSRPSTVGA QDVTQKQNNR VTDTPVSASK
DVEPFESNVV EDEVQIVDNN KMCYGLPHSE SNNYVPQQLI VPQSDLERNE LTNEFDELNA
DLKPSDILTS NQEDDDFPLD YFPVEIEYSQ TSMDSSLHMA SQGAKHPSQM MFYEDMDGMM
LGPKYPISAG IYEDPFFREE MAASNASKYM MPPPMSATRA HFMTNGEYYS KSREGKKHGK
SGRQHGPDDG RRDYDNENVG SSPSENQNPN EELDATENNQ DADDNRSPDI YPPTDAMAND
EYIPAYNRRM QMSESLVHPY TGMMLNPYMF CNMLAVDPSL NMGVNPVVDP FYGQNHSMDV
AHDVYSPQEV VYPSNYRSTP KAAYFNMRSP YGRNFPPPSA MNPYYTPYHR RQPSSATRRY
FSKANLINRK SKSPPRKNVV SKPSHKAPKK VNRTRHATSM HVGLGGKDSG NTSSESRDDS
TKEDSN
