PRR1_SCHPO
ID PRR1_SCHPO Reviewed; 539 AA.
AC O14283; Q9UTX5;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Transcription factor prr1;
DE AltName: Full=Pombe response regulator 1;
GN Name=prr1; ORFNames=SPAC8C9.14;
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 [MRNA], AND FUNCTION.
RX PubMed=10348908; DOI=10.1093/oxfordjournals.jbchem.a022387;
RA Ohmiya R., Kato C., Yamada H., Aiba H., Mizuno T.;
RT "A fission yeast gene (prr1(+)) that encodes a response regulator
RT implicated in oxidative stress response.";
RL J. Biochem. 125:1061-1066(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 224-413.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221 AND SER-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in oxidative stress. Transcription factor that acts
CC upon trr1 and ctt1. {ECO:0000269|PubMed:10348908}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HSF family.
CC {ECO:0000305}.
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DR EMBL; AB041768; BAB16722.1; -; mRNA.
DR EMBL; CU329670; CAB16301.1; -; Genomic_DNA.
DR EMBL; AB027943; BAA87247.1; -; Genomic_DNA.
DR PIR; T39150; T39150.
DR RefSeq; NP_594284.1; NM_001019707.2.
DR AlphaFoldDB; O14283; -.
DR SMR; O14283; -.
DR BioGRID; 278250; 13.
DR STRING; 4896.SPAC8C9.14.1; -.
DR iPTMnet; O14283; -.
DR MaxQB; O14283; -.
DR PaxDb; O14283; -.
DR PRIDE; O14283; -.
DR EnsemblFungi; SPAC8C9.14.1; SPAC8C9.14.1:pep; SPAC8C9.14.
DR GeneID; 2541756; -.
DR KEGG; spo:SPAC8C9.14; -.
DR PomBase; SPAC8C9.14; prr1.
DR VEuPathDB; FungiDB:SPAC8C9.14; -.
DR eggNOG; KOG0519; Eukaryota.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_008776_3_1_1; -.
DR InParanoid; O14283; -.
DR OMA; NWQSPGQ; -.
DR PhylomeDB; O14283; -.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SPO-3371511; HSF1 activation.
DR Reactome; R-SPO-3371568; Attenuation phase.
DR Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR PRO; PR:O14283; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:1900237; P:positive regulation of induction of conjugation with cellular fusion; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR014402; Sig_transdc_resp-reg_Skn7.
DR InterPro; IPR027718; TF_Skn7.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR PANTHER; PTHR10015:SF361; PTHR10015:SF361; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PIRSF; PIRSF002595; RR_SKN7; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Sensory transduction; Transcription; Transcription regulation.
FT CHAIN 1..539
FT /note="Transcription factor prr1"
FT /id="PRO_0000124594"
FT DOMAIN 369..483
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 7..111
FT /evidence="ECO:0000250"
FT REGION 251..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 221
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 418
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 539 AA; 60046 MW; F3B4945C595B2871 CRC64;
MPSSNGSSDF VRKLFNMLEE PEYRHILRWS DSGDSFIVLD TNEFTKTILP RHFKHSNFAS
FVRQLNKYDF HKVRHEEGAP SIYGEGAWEF RHDDFQLHHK DLLDNIKRKA PSKRNLANEN
TAPVIENLKQ QVDSILDFQK LLDRNLSGLA TSYQTILLKM FELKRGIESR DLLMSSIISY
LCDLEGSTQR QANPGAMFVP SHPLQELLNA YQALAKGQVA TTSPQQIPNQ IQQASAATTA
SSKMTVDTNL GTAQPSLYNT PSSDYELANQ EKPADSMASA ASLNTPLSSN DHSLNPHAHG
SYPMYEKFQP IQHPNPGSFT THLDSNASMA KSFSQISNDS LAKASSVATS MSQMGAAVPT
TGLWKRQPRI LLVEDDELSR RMTIKFLTSF DCQVDVAVDG IGAVNKANAG GFDLILMDFI
LPNLDGLSVT CLIRQYDHNT PILAITSNIS MNDAVTYFNH GVTDLLVKPF TKLTLLQLLK
KQLLNLLQAD NSINMSDVPS TKEAKDDKAP VTFYLENDAP MYPQQMLQDP IQADLQHPH
