PMAP1_SCHPO
ID PMAP1_SCHPO Reviewed; 398 AA.
AC P78926; Q10291;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Pheromone receptor transcription activator;
DE AltName: Full=Protein map1;
GN Name=map1; ORFNames=SPAC11E3.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8668157; DOI=10.1128/mcb.16.7.3420;
RA Yabana N., Yamamoto M.;
RT "Schizosaccharomyces pombe map1+ encodes a MADS-box-family protein required
RT for cell-type-specific gene expression.";
RL Mol. Cell. Biol. 16:3420-3428(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9003326; DOI=10.1007/pl00008604;
RA Nielsen O., Friis T., Kjaerulff S.;
RT "The Schizosaccharomyces pombe map1 gene encodes an SRF/MCM1-related
RT protein required for P-cell specific gene expression.";
RL Mol. Gen. Genet. 253:387-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: In response to mating-pheromone signaling or nitrogen
CC starvation, it interacts with mat1-Pc. This activates the expression of
CC one of two mating-type-specific genes sxa2 or map3, which leads to
CC inactivation of the P-factor. May also interact with mat1-Mc.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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; D78483; BAA11385.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11185.1; -; Genomic_DNA.
DR EMBL; L77973; AAA99295.1; ALT_SEQ; Genomic_DNA.
DR PIR; T43225; T43225.
DR PIR; T43415; T43415.
DR RefSeq; NP_594931.1; NM_001020362.2.
DR AlphaFoldDB; P78926; -.
DR SMR; P78926; -.
DR BioGRID; 278259; 1.
DR STRING; 4896.SPAC11E3.06.1; -.
DR iPTMnet; P78926; -.
DR MaxQB; P78926; -.
DR PaxDb; P78926; -.
DR PRIDE; P78926; -.
DR EnsemblFungi; SPAC11E3.06.1; SPAC11E3.06.1:pep; SPAC11E3.06.
DR GeneID; 2541765; -.
DR KEGG; spo:SPAC11E3.06; -.
DR PomBase; SPAC11E3.06; map1.
DR VEuPathDB; FungiDB:SPAC11E3.06; -.
DR eggNOG; KOG0015; Eukaryota.
DR HOGENOM; CLU_692908_0_0_1; -.
DR InParanoid; P78926; -.
DR PRO; PR:P78926; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISM:PomBase.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IMP:PomBase.
DR GO; GO:0007532; P:regulation of mating-type specific transcription, DNA-templated; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR CDD; cd00266; MADS_SRF_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033897; MADS_SRF-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 4: Predicted;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..398
FT /note="Pheromone receptor transcription activator"
FT /id="PRO_0000199442"
FT DOMAIN 20..74
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 44423 MW; 95D509ADDCE1B3EC CRC64;
MMDERKLSNF QIDGEKAYTG SSQGNSYLED RQKRQNTFTK RKAGIFKKAN ELALLTGSEV
MVLVVSETGL VHTFSTPKLE NVVKSPEGQK LITESLINAT TDQNESQASQ AKQSSAQLSD
SESGYPLDHE EMRISEENGP SHIENLNFFS DIDNFSKTSA EEIASKLFSS VSPTHETLQF
DHGLQNLEGF QANEHPEMFA DHSIDFYNSN NVDIPALSML TSQTSSSSTL NLPPEPASRE
VKIFPKQGKR IFSPSTGIDY ETTGQHSVNS PPSTYKHRRS LNKSFATRSE PQTPRKNKIR
DSLQSSPLNF PPRDRPPLIP ISRIAVPSTI ETEERQYRGN QKIINFYAKI FEPNSGLGTS
SEGASSSFPD VDPNLAQNGV PYYSLPDIDH NQFDHLRR
