MATA1_YEASX
ID MATA1_YEASX Reviewed; 126 AA.
AC P0CY10; D6VR98; P01366; P09091; Q06724;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Mating-type protein A1;
DE Short=MATa1 protein;
GN Name=MATA1; Synonyms=MAT1A;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7034964; DOI=10.1016/0092-8674(81)90356-1;
RA Astell C.R., Ahlstrom-Jonasson L., Smith M., Tatchell K., Nasmyth K.A.,
RA Hall B.D.;
RT "The sequence of the DNAs coding for the mating-type loci of Saccharomyces
RT cerevisiae.";
RL Cell 27:15-23(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7021055; DOI=10.1101/sqb.1981.045.01.113;
RA Nasmyth K.A., Tatchell K., Hall B.D., Astell C., Smith M.;
RT "Physical analysis of mating-type loci in Saccharomyces cerevisiae.";
RL Cold Spring Harb. Symp. Quant. Biol. 45:961-981(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION OF INTRONS.
RX PubMed=6329735; DOI=10.1002/j.1460-2075.1984.tb01927.x;
RA Miller A.M.;
RT "The yeast MATa1 gene contains two introns.";
RL EMBO J. 3:1061-1065(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=6256656; DOI=10.1038/289244a0;
RA Nasmyth K.A., Tatchell K., Hall B.D., Astell C.R., Smith M.;
RT "A position effect in the control of transcription at yeast mating type
RT loci.";
RL Nature 289:244-250(1981).
RN [5]
RP SIMILARITY TO HOMEOBOX PROTEINS.
RX PubMed=6429549; DOI=10.1038/310070a0;
RA Shepherd J.C.W., McGinnis W., Carrasco A.E., De Robertis E.M.,
RA Gehring W.J.;
RT "Fly and frog homoeo domains show homologies with yeast mating type
RT regulatory proteins.";
RL Nature 310:70-71(1984).
RN [6]
RP ROLE OF INTRON SPLICING IN THE FUNCTION OF MATA1.
RX PubMed=2574822; DOI=10.1128/mcb.9.11.4613-4620.1989;
RA Ner S.S., Smith M.;
RT "Role of intron splicing in the function of the MATa1 gene of Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 9:4613-4620(1989).
RN [7]
RP FUNCTION IN MATING-TYPE REGULATION.
RX PubMed=8664541; DOI=10.1016/0959-437x(95)80022-0;
RA Johnson A.D.;
RT "Molecular mechanisms of cell-type determination in budding yeast.";
RL Curr. Opin. Genet. Dev. 5:552-558(1995).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH ALPHA2.
RX PubMed=7569974; DOI=10.1126/science.270.5234.262;
RA Li T., Stark M.R., Johnson A.D., Wolberger C.;
RT "Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound
RT to DNA.";
RL Science 270:262-269(1995).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH ALPHA2.
RX PubMed=9838003; DOI=10.1093/nar/26.24.5707;
RA Li T., Jin Y., Vershon A.K., Wolberger C.;
RT "Crystal structure of the MATa1/MATalpha2 homeodomain heterodimer in
RT complex with DNA containing an A-tract.";
RL Nucleic Acids Res. 26:5707-5718(1998).
RN [10]
RP STRUCTURE BY NMR OF HOMEOBOX.
RX PubMed=10955992; DOI=10.1021/bi000677z;
RA Anderson J.S., Forman M.D., Modleski S., Dahlquist F.W., Baxter S.M.;
RT "Cooperative ordering in homeodomain-DNA recognition: solution structure
RT and dynamics of the MATa1 homeodomain.";
RL Biochemistry 39:10045-10054(2000).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH ALPHA2.
RX PubMed=12121651; DOI=10.1016/s0969-2126(02)00790-6;
RA Ke A., Mathias J.R., Vershon A.K., Wolberger C.;
RT "Structural and thermodynamic characterization of the DNA binding
RT properties of a triple alanine mutant of MATalpha2.";
RL Structure 10:961-971(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOMEOBOX.
RX PubMed=12538894; DOI=10.1110/ps.0219103;
RA Ke A., Wolberger C.;
RT "Insights into binding cooperativity of MATa1/MATalpha2 from the crystal
RT structure of a MATa1 homeodomain-maltose binding protein chimera.";
RL Protein Sci. 12:306-312(2003).
CC -!- FUNCTION: Mating type proteins are sequence specific DNA-binding
CC proteins that act as master switches in yeast differentiation by
CC controlling gene expression in a cell type-specific fashion.
CC Transcriptional corepressor that, in a/alpha diploid cells, binds
CC cooperatively with the ALPHA2 protein to a 21-bp DNA sequence termed
CC the haploid-specific gene (hsg) operator, to repress transcription of
CC haploid-specific genes and of MATALPHA1. {ECO:0000269|PubMed:8664541}.
CC -!- SUBUNIT: Binds DNA with a high specificity as a heterodimer of A1 and
CC ALPHA2. {ECO:0000269|PubMed:12121651, ECO:0000269|PubMed:7569974,
CC ECO:0000269|PubMed:9838003}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Only present in a-cells and in a/alpha diploid
CC cells.
CC -!- MISCELLANEOUS: Was initially thought to be alternatively spliced.
CC -!- MISCELLANEOUS: This gene is functional with 1, 2 or no introns, but the
CC functional protein is produced only when both introns are spliced from
CC the mRNA.
CC -!- MISCELLANEOUS: There are three genetic loci for mating type genes in
CC S.cerevisiae. MAT is the expression locus that determines the mating
CC type of the cell, whereas HML (containing HMLALPHA1 and HMLALPHA2) and
CC HMR (containing HMRA1 and HMRA2) represent silenced repositories of
CC mating type information. The mating type is determined by the MAT
CC locus, which contains either a copy of HML or of HMR. Diploid cells are
CC usually heterozygous for the MAT locus.
CC -!- SIMILARITY: Belongs to the MATA1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA24622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=Ref.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; V01313; CAA24622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V01312; CAA24619.1; -; Genomic_DNA.
DR PIR; A90983; JEBY1.
DR PDB; 1AKH; X-ray; 2.50 A; A=66-126.
DR PDB; 1F43; NMR; -; A=66-126.
DR PDB; 1LE8; X-ray; 2.30 A; A=74-126.
DR PDB; 1MH3; X-ray; 2.10 A; A=77-126.
DR PDB; 1MH4; X-ray; 2.30 A; A=77-126.
DR PDB; 1YRN; X-ray; 2.50 A; A=66-126.
DR PDBsum; 1AKH; -.
DR PDBsum; 1F43; -.
DR PDBsum; 1LE8; -.
DR PDBsum; 1MH3; -.
DR PDBsum; 1MH4; -.
DR PDBsum; 1YRN; -.
DR AlphaFoldDB; P0CY10; -.
DR BMRB; P0CY10; -.
DR SMR; P0CY10; -.
DR IntAct; P0CY10; 1.
DR MINT; P0CY10; -.
DR SGD; S000029660; MATA1.
DR VEuPathDB; FungiDB:YCR097W; -.
DR PhylomeDB; P0CY10; -.
DR EvolutionaryTrace; P0CY10; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR Pfam; PF00046; Homeodomain; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Homeobox; Nucleus; Transcription;
KW Transcription regulation.
FT CHAIN 1..126
FT /note="Mating-type protein A1"
FT /id="PRO_0000049201"
FT DNA_BIND 70..126
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1LE8"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:1LE8"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:1LE8"
SQ SEQUENCE 126 AA; 14803 MW; B413D0042EB97B3A CRC64;
MDDICSMAEN INRTLFNILG TEIDEINLNT NNLYNFIMES NLTKVEQHTL HKNISNNRLE
IYHHIKKEKS PKGKSSISPQ ARAFLEQVFR RKQSLNSKEK EEVAKKCGIT PLQVRVWFIN
KRMRSK
