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Protein

Mating-type protein ALPHA2

Gene

MATALPHA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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 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 MATALPHA1.1 Publication

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.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi129 – 191Homeobox; TALE-typePROSITE-ProRule annotationAdd BLAST63

GO - Molecular functioni

  • DNA binding, bending Source: SGD
  • sequence-specific DNA binding Source: SGD
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: SGD

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Repressor
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29351-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Mating-type protein ALPHA2
Short name:
MATalpha2 protein
Alternative name(s):
Alpha-2 repressor
Gene namesi
Name:MATALPHA2
Synonyms:ALPHA-2, MAT2A, MATAL2
Ordered Locus Names:YCR039C
ORF Names:YCR39C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

SGDiS000000635 MATALPHA2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4I → T: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication1
Mutagenesisi9L → F: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication1
Mutagenesisi10L → S: Reduces the ability of ALPHA2 to repress transcription, but binds normally to DNA and MCM1. Disrupts interaction with TUP1. 1 Publication1
Mutagenesisi71E → K: Reduces the ability of alpha2 to repress transcription, but binds normally to DNA and MCM1. 1 Publication1
Mutagenesisi114L → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi115V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi116F → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi117N → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi118V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi119V → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi120T → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. 1 Publication1
Mutagenesisi173R → A: Reduces the ability of ALPHA2/MCM1 to repress a-specific genes. Disrupts interaction with SSN6. 1 Publication1
Mutagenesisi181S → 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. 1 Publication1
Mutagenesisi182N → 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. 1 Publication1
Mutagenesisi185R → 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. 1 Publication1
Mutagenesisi192I → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication1
Mutagenesisi196L → A or S: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 2 Publications1
Mutagenesisi199L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication1
Mutagenesisi200L → A: Disrupts the ability of A1/ALPHA2 to repress haploid-specific genes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000491861 – 210Mating-type protein ALPHA2Add BLAST210

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP0CY08
PRIDEiP0CY08

PTM databases

iPTMnetiP0CY08

Expressioni

Developmental stagei

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

Interactioni

Subunit structurei

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/TUP1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MCM1P117462EBI-10443,EBI-10528

Protein-protein interaction databases

BioGridi30922, 7 interactors
31022, 21 interactors
IntActiP0CY08, 3 interactors

Structurei

Secondary structure

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi116 – 120Combined sources5
Beta strandi125 – 129Combined sources5
Helixi138 – 150Combined sources13
Turni151 – 153Combined sources3
Helixi159 – 169Combined sources11
Helixi173 – 188Combined sources16
Helixi194 – 197Combined sources4
Beta strandi200 – 202Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP0CY08
SMRiP0CY08
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CY08

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 102N-terminal domainAdd BLAST102
Regioni103 – 128Flexible linkerAdd BLAST26
Regioni190 – 210C-terminal tailAdd BLAST21

Domaini

The N-terminal domain is required for the interaction with the WD repeats of TUP1 and for dimerization.1 Publication
The homeobox domain binds to DNA and interacts with the TPR repeats of SSN6.1 Publication
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 MCM1.1 Publication
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.1 Publication

Sequence similaritiesi

Belongs to the TALE/M-ATYP homeobox family.Curated

Keywords - Domaini

Homeobox

Phylogenomic databases

HOGENOMiHOG000000902
InParanoidiP0CY08
KOiK09359
OrthoDBiEOG092C2OFZ

Family and domain databases

CDDicd00086 homeodomain, 1 hit
InterProiView protein in InterPro
IPR009057 Homeobox-like_sf
IPR001356 Homeobox_dom
PfamiView protein in Pfam
PF00046 Homeobox, 1 hit
SMARTiView protein in SMART
SM00389 HOX, 1 hit
SUPFAMiSSF46689 SSF46689, 1 hit
PROSITEiView protein in PROSITE
PS50071 HOMEOBOX_2, 1 hit

Sequencei

Sequence statusi: Complete.

P0CY08-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKIPIKDLL NPQITDEFKS SILDINKKLF SICCNLPKLP ESVTTEEEVE
60 70 80 90 100
LRDILGFLSR ANKNRKISDE EKKLLQTTSQ LTTTITVLLK EMRSIENDRS
110 120 130 140 150
NYQLTQKNKS ADGLVFNVVT QDMINKSTKP YRGHRFTKEN VRILESWFAK
160 170 180 190 200
NIENPYLDTK GLENLMKNTS LSRIQIKNWV SNRRRKEKTI TIAPELADLL
210
SGEPLAKKKE
Length:210
Mass (Da):24,282
Last modified:June 28, 2011 - v1
Checksum:i30CD6A486D7D76CE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56G → L in AAA34762 (PubMed:7021055).Curated1
Sequence conflicti150K → KK in AAA34762 (PubMed:7021055).Curated1
Sequence conflicti154N → S in AAT92829 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiS19398 JFBYA2
RefSeqiNP_009866.1, NM_001178708.1
NP_009868.3, NM_001178753.1

Genome annotation databases

EnsemblFungiiCAA42306; CAA42306; CAA42306
YCL067C; YCL067C; YCL067C
YCR039C; YCR039C; YCR039C
GeneIDi850292
850406
KEGGisce:YCL067C
sce:YCR039C

Similar proteinsi

Entry informationi

Entry nameiMTAL2_YEAST
AccessioniPrimary (citable) accession number: P0CY08
Secondary accession number(s): D6VQV2
, P01367, P01368, Q6B2C0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: May 23, 2018
This is version 51 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health