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P0CY08 (MTAL2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mating-type protein ALPHA2

Short name=MATalpha2 protein
Alternative name(s):
Alpha-2 repressor
Gene names
Name:MATALPHA2
Synonyms:ALPHA-2, MAT2A, MATAL2
Ordered Locus Names:YCR039C
ORF Names:YCR39C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 binds cooperatively with MCM1 to a 31-basepair DNA sequence termed the a-specific gene (asg) operator, to repress the transcription of a-cell-specific genes. Additionally, in a/alpha diploid cells, binds cooperatively with the A1 protein to a 21-basepair DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1. Ref.13

Subunit structure

Binds DNA with a high specificity as a heterotetramer consisting of an ALPHA2 dimer and an MCM1 dimer. Also binds DNA with a high specificity as a heterodimer of A1 and ALPHA2 in a/alpha diploid cells. Interacts with the general transcription repressor complex SSN6/TUP1. Ref.8 Ref.12 Ref.14 Ref.15 Ref.16

Subcellular location

Nucleus.

Developmental stage

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

Domain

The N-terminal domain is required for the interaction with the WD repeats of TUP1 and for dimerization. Ref.7 Ref.8

The homeobox domain binds to DNA and interacts with the TPR repeats of SSN6. Ref.7 Ref.8

The unstructured, flexible linker domain contains eight residues (Leu-114 to Gln-121), which, in the presence of MCM1, adopt a beta-fold and mediate the cooperative interaction to MCM1. Ref.7 Ref.8

The C-terminal tail domain is disordered in the monomer, even when bound to DNA. In the ternary complex with A1 and DNA, 16 residues (Ile-190 to Leu-205) of the C-terminal tail undergo a conformational change, becoming ordered and contacting the A1 homeodomain. Ref.7 Ref.8

Miscellaneous

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.

Sequence similarities

Belongs to the TALE/M-ATYP homeobox family.

Contains 1 homeobox DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 210210Mating-type protein ALPHA2
PRO_0000049186

Regions

DNA binding129 – 19163Homeobox; TALE-type Ref.6
Region1 – 102102N-terminal domain
Region103 – 12826Flexible linker
Region190 – 21021C-terminal tail

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10

Experimental info

Mutagenesis41I → T: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. Ref.12
Mutagenesis91L → F: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. Ref.12
Mutagenesis101L → S: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. Disrupts interaction with TUP1. Ref.12
Mutagenesis711E → K: Reduces the ability of alpha2 to repress transcription, but binds normally to DNA and MCM1. Ref.12
Mutagenesis1141L → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
Mutagenesis1151V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
Mutagenesis1161F → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
Mutagenesis1171N → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
Mutagenesis1181V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
Mutagenesis1191V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
Mutagenesis1201T → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes.
Mutagenesis1731R → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. Disrupts interaction with SSN6. Ref.16
Mutagenesis1811S → A in ALPHA2-3A; defective in binding DNA alone or in complex with MCM1, but binds DNA normally in complex with A1; when associated with A-182 and A-185. Ref.23
Mutagenesis1821N → A in ALPHA2-3A; defective in binding DNA alone or in complex with MCM1, but binds DNA normally in complex with A1; when associated with A-181 and A-185. Ref.23
Mutagenesis1851R → A in ALPHA2-3A; defective in binding DNA alone or in complex with MCM1, but binds DNA normally in complex with A1; when associated with A-181 and A-182. Ref.23
Mutagenesis1921I → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. Ref.19
Mutagenesis1961L → A or S: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. Ref.9 Ref.19
Mutagenesis1991L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. Ref.19
Mutagenesis2001L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. Ref.19
Sequence conflict561G → L in AAA34762. Ref.1
Sequence conflict1501K → KK in AAA34762. Ref.1
Sequence conflict1541N → S in AAT92829. Ref.5

Secondary structure

................ 210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CY08 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 30CD6A486D7D76CE

FASTA21024,282
        10         20         30         40         50         60 
MNKIPIKDLL NPQITDEFKS SILDINKKLF SICCNLPKLP ESVTTEEEVE LRDILGFLSR 

        70         80         90        100        110        120 
ANKNRKISDE EKKLLQTTSQ LTTTITVLLK EMRSIENDRS NYQLTQKNKS ADGLVFNVVT 

       130        140        150        160        170        180 
QDMINKSTKP YRGHRFTKEN VRILESWFAK NIENPYLDTK GLENLMKNTS LSRIQIKNWV 

       190        200        210 
SNRRRKEKTI TIAPELADLL SGEPLAKKKE 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"The MAT locus revisited within a 9.8 kb fragment of chromosome III containing BUD5 and two new open reading frames."
Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C., Soustelle C.
Yeast 7:881-888(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]"A repressor (MAT alpha 2 Product) and its operator control expression of a set of cell type specific genes in yeast."
Johnson A.D., Herskowitz I.
Cell 42:237-247(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING SPECIFICITY.
[7]"Homeo domain of the yeast repressor alpha 2 is a sequence-specific DNA-binding domain but is not sufficient for repression."
Hall M.N., Johnson A.D.
Science 237:1007-1012(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS BY DOMAIN DELETION.
[8]"Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free."
Sauer R.T., Smith D.L., Johnson A.D.
Genes Dev. 2:807-816(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS, DIMERIZATION.
[9]"a/Alpha-specific repression by MAT alpha 2."
Strathern J., Shafer B., Hicks J., McGill C.
Genetics 120:75-81(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-196.
[10]"N-terminal acetylation of cellular proteins creates specific degradation signals."
Hwang C.S., Shemorry A., Varshavsky A.
Science 327:973-977(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-7, ACETYLATION AT MET-1.
[11]"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.
[12]"The WD repeats of Tup1 interact with the homeo domain protein alpha 2."
Komachi K., Redd M.J., Johnson A.D.
Genes Dev. 8:2857-2867(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TUP1, MUTAGENESIS OF ILE-4; LEU-9; LEU-10 AND GLU-71.
[13]"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.
[14]"The tetratricopeptide repeats of Ssn6 interact with the homeo domain of alpha 2."
Smith R.L., Redd M.J., Johnson A.D.
Genes Dev. 9:2903-2910(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSN6.
[15]"The yeast alpha2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes."
Mead J., Zhong H., Acton T.B., Vershon A.K.
Mol. Cell. Biol. 16:2135-2143(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCM1, MUTAGENESIS OF 114-LEU--THR-120.
[16]"A sequence resembling a peroxisomal targeting sequence directs the interaction between the tetratricopeptide repeats of Ssn6 and the homeodomain of alpha 2."
Smith R.L., Johnson A.D.
Proc. Natl. Acad. Sci. U.S.A. 97:3901-3906(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSN6, MUTAGENESIS OF ARG-173.
[17]"Crystal structure of a MAT alpha 2 homeodomain-operator complex suggests a general model for homeodomain-DNA interactions."
Wolberger C., Vershon A.K., Liu B., Johnson A.D., Pabo C.O.
Cell 67:517-528(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF HOMEOBOX.
[18]"Secondary structure of the homeo domain of yeast alpha 2 repressor determined by NMR spectroscopy."
Phillips C.L., Vershon A.K., Johnson A.D., Dahlquist F.W.
Genes Dev. 5:764-772(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF HOMEOBOX.
[19]"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 A1, MUTAGENESIS OF ILE-192; LEU-196; LEU-199 AND LEU-200.
[20]"Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex."
Tan S., Richmond T.J.
Nature 391:660-666(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF HOMEOBOX IN COMPLEX WITH MCM1.
[21]"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 A1.
[22]"A Hoogsteen base pair embedded in undistorted B-DNA."
Aishima J., Gitti R.K., Noah J.E., Gan H.H., Schlick T., Wolberger C.
Nucleic Acids Res. 30:5244-5252(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF HOMEOBOX.
[23]"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 A1, MUTAGENESIS OF SER-181; ASN-182 AND ARG-185.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00060 Genomic DNA. Translation: AAA34762.1.
X63853 Genomic DNA. Translation: CAA45335.1.
X59720 Genomic DNA. Translation: CAA42306.1.
AY692810 Genomic DNA. Translation: AAT92829.1.
BK006937 Genomic DNA. Translation: DAA07518.1.
PIRJFBYA2. S19398.
RefSeqNP_009866.1. NM_001178708.1.
NP_009868.3. NM_001178753.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AKHX-ray2.50B128-210[»]
1APLX-ray2.70C/D128-210[»]
1K61X-ray2.10A/B/C/D132-191[»]
1LE8X-ray2.30B128-210[»]
1MNMX-ray2.25C/D103-189[»]
1YRNX-ray2.50B128-210[»]
ProteinModelPortalP0CY08.
SMRP0CY08. Positions 128-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30922. 7 interactions.
31022. 10 interactions.
MINTMINT-2735547.

Proteomic databases

MaxQBP0CY08.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL067C; YCL067C; YCL067C.
YCR039C; YCR039C; YCR039C.
GeneID850292.
850406.
KEGGsce:YCL067C.
sce:YCR039C.

Organism-specific databases

CYGDYCR039c.
SGDS000000635. MATALPHA2.

Phylogenomic databases

HOGENOMHOG000000902.
KOK09359.
OrthoDBEOG7W41QS.

Enzyme and pathway databases

BioCycYEAST:G3O-29351-MONOMER.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
[Graphical view]
PfamPF00046. Homeobox. 1 hit.
[Graphical view]
SMARTSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS50071. HOMEOBOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0CY08.
NextBio965658.

Entry information

Entry nameMTAL2_YEAST
AccessionPrimary (citable) accession number: P0CY08
Secondary accession number(s): D6VQV2 expand/collapse secondary AC list , P01367, P01368, Q6B2C0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references