ID   MATMC_SCHKA             Reviewed;         181 AA.
AC   Q6WRX6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Mating-type M-specific polypeptide Mc;
DE            Short=mat-Mc;
GN   Name=matMc;
OS   Schizosaccharomyces kambucha (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=204045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=14618565; DOI=10.1002/yea.1042;
RA   Singh G., Klar A.J.S.;
RT   "DNA sequence of the mat2,3 region of Schizosaccharomyces kambucha shares
RT   high homology with the corresponding sequence from Sz. pombe.";
RL   Yeast 20:1273-1278(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. Positive
CC       regulator of MFM genes. The HMG box recognizes the DNA sequence 5'-
CC       AACAAAG-3'. Required for conjugation and efficient meiosis (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC   -!- MISCELLANEOUS: There are three genetic loci for mating type genes in
CC       fission yeast, mat1, mat2-P and mat3-M. Cell type is determined by the
CC       alternate allele present in mat1, either P (plus) in a h+ or M (minus)
CC       in a h- cell. Mat2-P and mat3-M serve as donor of information that is
CC       transposed to mat1 during a switch of mating type (By similarity).
CC       {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY271822; AAQ82722.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6WRX6; -.
DR   SMR; Q6WRX6; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN           1..181
FT                   /note="Mating-type M-specific polypeptide Mc"
FT                   /id="PRO_0000048584"
FT   DNA_BIND        103..171
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
SQ   SEQUENCE   181 AA;  21030 MW;  6DEEE06081AEC715 CRC64;
     MDSHQELSAG SPISYDFLDP DWCFKRYLTK DALHSIETGK GAAYFVPDGF TPILIPNSQS
     YLLDGNSAQL PRPQPISFTL DQCKVPGYIL KSLRKDTKST ERTPRPPNAF ILYRKEKHAT
     LLKSNPSINN SQVSKLVGEM WRNESKEVRM RYFKMSEFYK AQHQKMYPGY KYQPRKNKVK
     R