PCR1_SCHPO
ID PCR1_SCHPO Reviewed; 171 AA.
AC Q09926;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transcription factor pcr1;
DE AltName: Full=Transcription factor mts2;
GN Name=pcr1; Synonyms=mts2; ORFNames=SPAC21E11.03c;
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], AND FUNCTION.
RX PubMed=8552099; DOI=10.1128/mcb.16.2.704;
RA Watanabe Y., Yamamoto M.;
RT "Schizosaccharomyces pombe pcr1+ encodes a CREB/ATF protein involved in
RT regulation of gene expression for sexual development.";
RL Mol. Cell. Biol. 16:704-711(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kon N., Krawchuk M.D., Warren B.G., Smith G.R., Wahls W.P.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
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).
RN [4]
RP CHARACTERIZATION.
RX PubMed=7958849; DOI=10.1101/gad.8.14.1693;
RA Wahls W.P., Smith G.R.;
RT "A heteromeric protein that binds to a meiotic homologous recombination hot
RT spot: correlation of binding and hot spot activity.";
RL Genes Dev. 8:1693-1702(1994).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=28775286; DOI=10.1038/s41598-017-07647-1;
RA Villahermosa D., Fleck O.;
RT "Elp3 and Dph3 of Schizosaccharomyces pombe mediate cellular stress
RT responses through tRNALysUUU modifications.";
RL Sci. Rep. 7:7225-7225(2017).
CC -!- FUNCTION: Involved in regulation of gene expression for sexual
CC development (PubMed:8552099). Binds and activates CRE sites (cAMP-
CC response elements, also known as M26 meiotic recombination hotspots)
CC (PubMed:8552099, PubMed:7958849). {ECO:0000269|PubMed:7958849,
CC ECO:0000269|PubMed:8552099}.
CC -!- SUBUNIT: Heterodimer of pcr1/mts2 and atf1/mts1.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to cold and thermal stress,
CC simultaneous disruption of dph3 suppresses the growth defect during
CC thermal stress. {ECO:0000269|PubMed:28775286}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; D63667; BAA09818.1; -; Genomic_DNA.
DR EMBL; U87870; AAB46991.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91968.1; -; Genomic_DNA.
DR PIR; S62588; S62588.
DR RefSeq; NP_594500.1; NM_001019929.2.
DR AlphaFoldDB; Q09926; -.
DR SMR; Q09926; -.
DR BioGRID; 278528; 25.
DR STRING; 4896.SPAC21E11.03c.1; -.
DR MaxQB; Q09926; -.
DR PaxDb; Q09926; -.
DR EnsemblFungi; SPAC21E11.03c.1; SPAC21E11.03c.1:pep; SPAC21E11.03c.
DR GeneID; 2542047; -.
DR KEGG; spo:SPAC21E11.03c; -.
DR PomBase; SPAC21E11.03c; pcr1.
DR VEuPathDB; FungiDB:SPAC21E11.03c; -.
DR eggNOG; KOG1414; Eukaryota.
DR HOGENOM; CLU_1571555_0_0_1; -.
DR InParanoid; Q09926; -.
DR OMA; QAQHMAY; -.
DR PhylomeDB; Q09926; -.
DR PRO; PR:Q09926; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990243; C:atf1-pcr1 complex; IDA:PomBase.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0010844; F:recombination hotspot binding; IDA:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0006325; P:chromatin organization; IMP:PomBase.
DR GO; GO:0110034; P:negative regulation of adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:1904765; P:positive regulation of transcription from RNA polymerase II promoter in response to maltose; IMP:PomBase.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:PomBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Meiosis; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..171
FT /note="Transcription factor pcr1"
FT /id="PRO_0000076535"
FT DOMAIN 10..73
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 12..51
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 52..66
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 125..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 171 AA; 19348 MW; 9922FDDDFE150BDE CRC64;
MTAKKKEVDD EKRRRILERN RIAASKFRQK KKEWIKELEQ TANAAFEQSK RLQLLLSQLQ
QEAFRLKSQL LAHQGCQCSV KIRSVLTDFQ TAHNALHSQH MAYRPVQPPP GDNMLESVVS
VSPTQMHPSL QGLPPNQHPQ MPPSSQQPNS DDVQQHMFSA AGLPRSLGGP I
