MATB_NEUCS
ID MATB_NEUCS Reviewed; 382 AA.
AC P36981;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Mating-type protein a-1;
DE Short=Mt a-1;
GN Name=mta-1;
OS Neurospora crassa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=5141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF ARG-258.
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=2142304; DOI=10.1073/pnas.87.13.4917;
RA Staben C., Yanofsky C.;
RT "Neurospora crassa a mating-type region.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:4917-4921(1990).
RN [2]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=8088517; DOI=10.1093/genetics/137.3.715;
RA Philley M.L., Staben C.;
RT "Functional analyses of the Neurospora crassa MT a-1 mating type
RT polypeptide.";
RL Genetics 137:715-722(1994).
RN [3]
RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION.
RC STRAIN=74-ORS-6a / FGSC 4200;
RX PubMed=12139624; DOI=10.1046/j.1365-2958.2002.03052.x;
RA Bobrowicz P., Pawlak R., Correa A., Bell-Pedersen D., Ebbole D.J.;
RT "The Neurospora crassa pheromone precursor genes are regulated by the
RT mating type locus and the circadian clock.";
RL Mol. Microbiol. 45:795-804(2002).
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 activator that induces the transcription of a-specific
CC genes like mating factor mfa-1. Required for mating as an a-cell,
CC blocking of heterokaryon formation (vegetative incompatibility) and for
CC perithecium induction. {ECO:0000269|PubMed:12139624,
CC ECO:0000269|PubMed:8088517}.
CC -!- SUBUNIT: Binds in vitro to DNA containing a specific core sequence 5'-
CC CTTTG-3'.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
CC -!- DEVELOPMENTAL STAGE: Only present in a-cells and in a/A diploid cells.
CC {ECO:0000269|PubMed:8088517}.
CC -!- CAUTION: Do not confuse Mt a-1 with MT A-1; these are two different
CC proteins. {ECO:0000305}.
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DR EMBL; M54787; AAA33598.2; -; Genomic_DNA.
DR PIR; T10163; T10163.
DR AlphaFoldDB; P36981; -.
DR SMR; P36981; -.
DR PRIDE; P36981; -.
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 1: Evidence at protein level;
KW DNA-binding; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..382
FT /note="Mating-type protein a-1"
FT /id="PRO_0000048588"
FT DNA_BIND 116..184
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT MUTAGEN 258
FT /note="R->S: In a-1m33; abolishes vegetative
FT incompatibility."
FT /evidence="ECO:0000269|PubMed:2142304"
SQ SEQUENCE 382 AA; 43467 MW; 1113D40B34DFF01C CRC64;
MDGNSTHPAP NLKTTMAWSR ISNQLGHWND RKVIAIPLSD FLNTHPDIQS GIIAEFKKAT
GEEGMFARDP ESLGIMLLGP VKLFKPDSVV VDGNLFWDPK GIHASAPKEQ QKKAKIPRPP
NAYILYRKDH HREIREQNPG LHNNEISVIV GNMWRDEQPH IREKYFNMSN EIKTRLLLEN
PDYRYNPRRS QDIRRRVSPY LKIKLLNYDV NGNLLWGTVN AEDAALIRTH FHGVVRVEEM
DDGCRIVCRP VAGSRKLRAA VVDTWMPRYT VDTTPVTEDD DAQAFNFNDP LGGAYFPLNE
HLWITVNQNP PFNAPPPNPN PHLDFVHPDG MEAVVHNVQN MIAQVQEANE AAALTLPPPP
PLRLLSLRLW LMIPLTQLSF PL