TUP11_SCHPO
ID TUP11_SCHPO Reviewed; 614 AA.
AC Q09715; Q9USG3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Transcriptional repressor tup11;
GN Name=tup11; ORFNames=SPAC18B11.10;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 71-101, AND SUBCELLULAR
RP LOCATION.
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 [3]
RP CHARACTERIZATION.
RX PubMed=10567571; DOI=10.1128/mcb.19.12.8461;
RA Mukai Y., Matsuo E., Roth S.Y., Harashima S.;
RT "Conservation of histone binding and transcriptional repressor functions in
RT a Schizosaccharomyces pombe Tup1p homolog.";
RL Mol. Cell. Biol. 19:8461-8468(1999).
RN [4]
RP INTERACTION WITH FEP1, AND MUTAGENESIS OF TYR-362 AND LEU-542.
RX PubMed=14668334; DOI=10.1074/jbc.m312787200;
RA Znaidi S., Pelletier B., Mukai Y., Labbe S.;
RT "The Schizosaccharomyces pombe corepressor Tup11 interacts with the iron-
RT responsive transcription factor Fep1.";
RL J. Biol. Chem. 279:9462-9474(2004).
RN [5]
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: Transcriptional repressor.
CC -!- SUBUNIT: Interacts with fep1. Binds to histones H3 and H4.
CC {ECO:0000269|PubMed:14668334}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the WD repeat TUP1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA90594.1; -; Genomic_DNA.
DR EMBL; AB027768; BAA87072.1; -; Genomic_DNA.
DR PIR; S58306; S58306.
DR RefSeq; NP_592873.1; NM_001018273.2.
DR AlphaFoldDB; Q09715; -.
DR SMR; Q09715; -.
DR BioGRID; 278766; 32.
DR STRING; 4896.SPAC18B11.10.1; -.
DR iPTMnet; Q09715; -.
DR MaxQB; Q09715; -.
DR PaxDb; Q09715; -.
DR PRIDE; Q09715; -.
DR EnsemblFungi; SPAC18B11.10.1; SPAC18B11.10.1:pep; SPAC18B11.10.
DR GeneID; 2542299; -.
DR KEGG; spo:SPAC18B11.10; -.
DR PomBase; SPAC18B11.10; tup11.
DR VEuPathDB; FungiDB:SPAC18B11.10; -.
DR eggNOG; KOG0266; Eukaryota.
DR HOGENOM; CLU_000288_57_23_1; -.
DR InParanoid; Q09715; -.
DR OMA; SHNGRFI; -.
DR PhylomeDB; Q09715; -.
DR PRO; PR:Q09715; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0017053; C:transcription repressor complex; EXP:PomBase.
DR GO; GO:0042393; F:histone binding; IDA:PomBase.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:PomBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:PomBase.
DR GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IMP:PomBase.
DR GO; GO:0034396; P:negative regulation of transcription from RNA polymerase II promoter in response to iron; IMP:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013890; Tscrpt_rep_Tup1_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08581; Tup_N; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..614
FT /note="Transcriptional repressor tup11"
FT /id="PRO_0000051310"
FT REPEAT 311..340
FT /note="WD 1"
FT REPEAT 358..388
FT /note="WD 2"
FT REPEAT 400..430
FT /note="WD 3"
FT REPEAT 441..471
FT /note="WD 4"
FT REPEAT 482..512
FT /note="WD 5"
FT REPEAT 536..566
FT /note="WD 6"
FT REPEAT 578..608
FT /note="WD 7"
FT REGION 93..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 362
FT /note="Y->C: No interaction with fep1."
FT /evidence="ECO:0000269|PubMed:14668334"
FT MUTAGEN 542
FT /note="L->S: No interaction with fep1."
FT /evidence="ECO:0000269|PubMed:14668334"
SQ SEQUENCE 614 AA; 67331 MW; B02289556DE2C1B1 CRC64;
MASVEDATKV QEMLDALKAE YNALAHHSFA SKARGNDYES SMIQSQIQEI EAFRKTVDDM
YEKQKSIRET YEKDINKLKR ELEELGVEAN TASYRNRGER SELAASNNQV THIDQEHPSQ
TKSTSQPPSN HLPAFQQIPP IHQSAYPQNN VAEVLMPPIP PSVEASSGQN FNQGIASQNP
AISTSNLPST TPLYIPPVNY GANQVSQQPN PQLPGVSNYY NPSATSKPAV NVQPPRIPTK
ATPSAEPSMT ASANAGSISQ AGPDGEYQGR EQIAPVSDTE AARKTTSQSW YVTYNPACKR
VFNINLVHTL EHPSVVCCVK FSNNGKYLAT GCNQAANVFD VQTGKKLFTL HEESPDPSRD
LYVRTIAFSP DGKYLVTGTE DRQIKLWDLS TQKVRYVFSG HEQDIYSLDF SHNGRFIVSG
SGDRTARLWD VETGQCILKL EIENGVTAIA ISPNDQFIAV GSLDQIIRVW SVSGTLVERL
EGHKESVYSI AFSPDSSILL SGSLDKTIKV WELQATRSVG LSAIKPEGIC KATYTGHTDF
VLSVAVSPDS RWGLSGSKDR SMQFWDLQTG QSYLTCQGHK NSVISVCFSP DGRQFASGSG
DLRARIWSID PASP
