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   13-APR-2016, entry version 29.
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;
OC   Saccharomycetes; 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.,
RA   Nasmyth K.A., Hall B.D.;
RT   "The sequence of the DNAs coding for the mating-type loci of
RT   Saccharomyces cerevisiae.";
RL   Cell 27:15-23(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7021055;
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;
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
RT   type 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;
RA   Ner S.S., Smith M.;
RT   "Role of intron splicing in the function of the MATa1 gene of
RT   Saccharomyces 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
RP   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
RT   bound to DNA.";
RL   Science 270:262-269(1995).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH
RP   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
RT   structure 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
RP   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
RT   crystal structure of a MATa1 homeodomain-maltose binding protein
RT   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
CC       termed the haploid-specific gene (hsg) operator, to repress
CC       transcription of haploid-specific genes and of MATALPHA1.
CC       {ECO:0000269|PubMed:8664541}.
CC   -!- SUBUNIT: Binds DNA with a high specificity as a heterodimer of A1
CC       and ALPHA2. {ECO:0000269|PubMed:12121651,
CC       ECO:0000269|PubMed:7569974, ECO:0000269|PubMed:9838003}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Only present in a-cells and in a/alpha
CC       diploid cells.
CC   -!- MISCELLANEOUS: Was initially thought to be alternatively spliced.
CC   -!- MISCELLANEOUS: This gene is functional with 1, 2 or no introns,
CC       but the functional protein is produced only when both introns are
CC       spliced from the mRNA.
CC   -!- MISCELLANEOUS: There are three genetic loci for mating type genes
CC       in S.cerevisiae. MAT is the expression locus that determines the
CC       mating type of the cell, whereas HML (containing HMLALPHA1 and
CC       HMLALPHA2) and HMR (containing HMRA1 and HMRA2) represent silenced
CC       repositories of mating type information. The mating type is
CC       determined by the MAT locus, which contains either a copy of HML
CC       or of HMR. Diploid cells are usually heterozygous for the MAT
CC       locus.
CC   -!- SIMILARITY: Belongs to the MATA1 family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00108}.
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   ProteinModelPortal; P0CY10; -.
DR   SMR; P0CY10; 77-126.
DR   IntAct; P0CY10; 1.
DR   STRING; 4932.YCR097W; -.
DR   PaxDb; P0CY10; -.
DR   SGD; S000029660; MATA1.
DR   eggNOG; ENOG410J3QJ; Eukaryota.
DR   eggNOG; ENOG410Y2GC; LUCA.
DR   PhylomeDB; P0CY10; -.
DR   EvolutionaryTrace; P0CY10; -.
DR   NextBio; 966093; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.60; -; 1.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   Pfam; PF00046; Homeobox; 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       Mating-type protein A1.
FT                                /FTId=PRO_0000049201.
FT   DNA_BIND     70    126       Homeobox. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00108}.
FT   HELIX        79     91       {ECO:0000244|PDB:1MH3}.
FT   HELIX        97    107       {ECO:0000244|PDB:1MH3}.
FT   HELIX       111    122       {ECO:0000244|PDB:1MH3}.
SQ   SEQUENCE   126 AA;  14803 MW;  B413D0042EB97B3A CRC64;
     MDDICSMAEN INRTLFNILG TEIDEINLNT NNLYNFIMES NLTKVEQHTL HKNISNNRLE
     IYHHIKKEKS PKGKSSISPQ ARAFLEQVFR RKQSLNSKEK EEVAKKCGIT PLQVRVWFIN
     KRMRSK
//