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Protein

Mating-type protein A1

Gene

MATA1

Organism
Saccharomyces cerevisiae (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that, in a/alpha diploid cells, binds cooperatively with the ALPHA2 protein to a 21-bp DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi70 – 12657HomeoboxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Mating-type protein A1
Short name:
MATa1 protein
Gene namesi
Name:MATA1
Synonyms:MAT1A
OrganismiSaccharomyces cerevisiae (Baker's yeast)
Taxonomic identifieri4932 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Organism-specific databases

SGDiS000029660. MATA1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 126126Mating-type protein A1PRO_0000049201Add
BLAST

Proteomic databases

PaxDbiP0CY10.

Expressioni

Developmental stagei

Only present in a-cells and in a/alpha diploid cells.

Interactioni

Subunit structurei

Binds DNA with a high specificity as a heterodimer of A1 and ALPHA2.3 Publications

Protein-protein interaction databases

STRINGi4932.YCR097W.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi79 – 9113Combined sources
Helixi97 – 10711Combined sources
Helixi111 – 12212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKHX-ray2.50A66-126[»]
1F43NMR-A66-126[»]
1LE8X-ray2.30A74-126[»]
1MH3X-ray2.10A77-126[»]
1MH4X-ray2.30A77-126[»]
1YRNX-ray2.50A66-126[»]
ProteinModelPortaliP0CY10.
SMRiP0CY10. Positions 77-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CY10.

Family & Domainsi

Sequence similaritiesi

Belongs to the MATA1 family.Curated
Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Homeobox

Phylogenomic databases

eggNOGiENOG410J3QJ. Eukaryota.
ENOG410Y2GC. LUCA.
PhylomeDBiP0CY10.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
[Graphical view]
PfamiPF00046. Homeobox. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CY10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDICSMAEN INRTLFNILG TEIDEINLNT NNLYNFIMES NLTKVEQHTL
60 70 80 90 100
HKNISNNRLE IYHHIKKEKS PKGKSSISPQ ARAFLEQVFR RKQSLNSKEK
110 120
EEVAKKCGIT PLQVRVWFIN KRMRSK
Length:126
Mass (Da):14,803
Last modified:June 28, 2011 - v1
Checksum:iB413D0042EB97B3A
GO

Sequence cautioni

The sequence CAA24622.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence described in PubMed:7021055 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01313 Genomic DNA. Translation: CAA24622.1. Sequence problems.
V01312 Genomic DNA. Translation: CAA24619.1.
PIRiA90983. JEBY1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01313 Genomic DNA. Translation: CAA24622.1. Sequence problems.
V01312 Genomic DNA. Translation: CAA24619.1.
PIRiA90983. JEBY1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKHX-ray2.50A66-126[»]
1F43NMR-A66-126[»]
1LE8X-ray2.30A74-126[»]
1MH3X-ray2.10A77-126[»]
1MH4X-ray2.30A77-126[»]
1YRNX-ray2.50A66-126[»]
ProteinModelPortaliP0CY10.
SMRiP0CY10. Positions 77-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4932.YCR097W.

Proteomic databases

PaxDbiP0CY10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

SGDiS000029660. MATA1.

Phylogenomic databases

eggNOGiENOG410J3QJ. Eukaryota.
ENOG410Y2GC. LUCA.
PhylomeDBiP0CY10.

Miscellaneous databases

EvolutionaryTraceiP0CY10.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
[Graphical view]
PfamiPF00046. Homeobox. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The sequence of the DNAs coding for the mating-type loci of Saccharomyces cerevisiae."
    Astell C.R., Ahlstrom-Jonasson L., Smith M., Tatchell K., Nasmyth K.A., Hall B.D.
    Cell 27:15-23(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Physical analysis of mating-type loci in Saccharomyces cerevisiae."
    Nasmyth K.A., Tatchell K., Hall B.D., Astell C., Smith M.
    Cold Spring Harb. Symp. Quant. Biol. 45:961-981(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The yeast MATa1 gene contains two introns."
    Miller A.M.
    EMBO J. 3:1061-1065(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION OF INTRONS.
  4. "A position effect in the control of transcription at yeast mating type loci."
    Nasmyth K.A., Tatchell K., Hall B.D., Astell C.R., Smith M.
    Nature 289:244-250(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
  5. "Fly and frog homoeo domains show homologies with yeast mating type regulatory proteins."
    Shepherd J.C.W., McGinnis W., Carrasco A.E., De Robertis E.M., Gehring W.J.
    Nature 310:70-71(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO HOMEOBOX PROTEINS.
  6. "Role of intron splicing in the function of the MATa1 gene of Saccharomyces cerevisiae."
    Ner S.S., Smith M.
    Mol. Cell. Biol. 9:4613-4620(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE OF INTRON SPLICING IN THE FUNCTION OF MATA1.
  7. "Molecular mechanisms of cell-type determination in budding yeast."
    Johnson A.D.
    Curr. Opin. Genet. Dev. 5:552-558(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MATING-TYPE REGULATION.
  8. "Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA."
    Li T., Stark M.R., Johnson A.D., Wolberger C.
    Science 270:262-269(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH ALPHA2.
  9. "Crystal structure of the MATa1/MATalpha2 homeodomain heterodimer in complex with DNA containing an A-tract."
    Li T., Jin Y., Vershon A.K., Wolberger C.
    Nucleic Acids Res. 26:5707-5718(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH ALPHA2.
  10. "Cooperative ordering in homeodomain-DNA recognition: solution structure and dynamics of the MATa1 homeodomain."
    Anderson J.S., Forman M.D., Modleski S., Dahlquist F.W., Baxter S.M.
    Biochemistry 39:10045-10054(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF HOMEOBOX.
  11. "Structural and thermodynamic characterization of the DNA binding properties of a triple alanine mutant of MATalpha2."
    Ke A., Mathias J.R., Vershon A.K., Wolberger C.
    Structure 10:961-971(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH ALPHA2.
  12. "Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera."
    Ke A., Wolberger C.
    Protein Sci. 12:306-312(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOMEOBOX.

Entry informationi

Entry nameiMATA1_YEASX
AccessioniPrimary (citable) accession number: P0CY10
Secondary accession number(s): D6VR98
, P01366, P09091, Q06724
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: June 8, 2016
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Was initially thought to be alternatively spliced.
This gene is functional with 1, 2 or no introns, but the functional protein is produced only when both introns are spliced from the mRNA.
There are three genetic loci for mating type genes in S.cerevisiae. MAT is the expression locus that determines the mating type of the cell, whereas HML (containing HMLALPHA1 and HMLALPHA2) and HMR (containing HMRA1 and HMRA2) represent silenced repositories of mating type information. The mating type is determined by the MAT locus, which contains either a copy of HML or of HMR. Diploid cells are usually heterozygous for the MAT locus.

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.