RDP1L_SCHPO
ID RDP1L_SCHPO Reviewed; 478 AA.
AC O13862;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Transcriptional activator protein rdp1;
DE AltName: Full=Rhp51-DRE-binding protein 1;
GN Name=rdp1; ORFNames=SPAC1B1.01;
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=11073995; DOI=10.1128/mcb.20.23.8958-8968.2000;
RA Shim Y.S., Jang Y.K., Lim M.S., Lee J.S., Seong R.H., Hong S.H., Park S.D.;
RT "Rdp1, a novel zinc finger protein, regulates the DNA damage response of
RT rhp51(+) from Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 20:8958-8968(2000).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Acts as a DNA damage-response activator of rhp51. Binds to
CC part of the DNA damage-responsive element (DRE), (5'-NG[GT]T[GA]-3').
CC {ECO:0000269|PubMed:11073995}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAB11080.1; -; Genomic_DNA.
DR PIR; T38014; T38014.
DR RefSeq; NP_594231.1; NM_001019654.2.
DR AlphaFoldDB; O13862; -.
DR BioGRID; 278996; 7.
DR STRING; 4896.SPAC1B1.01.1; -.
DR iPTMnet; O13862; -.
DR MaxQB; O13862; -.
DR PaxDb; O13862; -.
DR PRIDE; O13862; -.
DR EnsemblFungi; SPAC1B1.01.1; SPAC1B1.01.1:pep; SPAC1B1.01.
DR GeneID; 2542539; -.
DR KEGG; spo:SPAC1B1.01; -.
DR PomBase; SPAC1B1.01; -.
DR VEuPathDB; FungiDB:SPAC1B1.01; -.
DR HOGENOM; CLU_045169_0_0_1; -.
DR OMA; PVNFASH; -.
DR PRO; PR:O13862; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; NAS: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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:PomBase.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..478
FT /note="Transcriptional activator protein rdp1"
FT /id="PRO_0000046815"
FT ZN_FING 139..162
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 478 AA; 51766 MW; B79441407760B15B CRC64;
MSEHSPEASS TYAQVTSNDE LSSNKIYMNA DQNNSRKKEM DGSLQNNGGR LQNVNPLGGN
ESMSAVATSA ASSLPTAENG VSLNAASPTI HSNTPTVVSH PVMSGSELKG EESHNSPGTL
NGTSVANASK QPNMPNATFR CDKCDMMFVK QSGLTNHKRT YHQVETVVII GHRRYVWRRN
ENGRFQCVCG RQNWRRPVNF ASHAKQCPSF LAMDPNNIPP EINKVSPHDD LRPLSDSRRR
ARRPHPSDTI PPGASMARSD PSQVPESNPS AAAAVAAAAV AAAANLTNGV NPPEVPRNLN
SSLVDAAESL ANVSQQQHHR HPFARQPDYS AHSIPRTAAP YAPSMNMFAQ NGPNTSLLPT
AMPSDVSISS SLQQQPIHPS YDSRFSKAPQ GTDALAALGY GTPSSAATLC PLYRDTPAAI
VSEKLHLRLA NLRIAYCEDC REFISLNAAL DHRRSHHQQN ITGDLVHVYS DFLDFQNC
