PST3_SCHPO
ID PST3_SCHPO Reviewed; 1154 AA.
AC O74755;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Paired amphipathic helix protein pst3;
DE AltName: Full=SIN3 homolog 3;
GN Name=pst3; ORFNames=SPBC1734.16c;
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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810}.
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DR EMBL; CU329671; CAA21310.1; -; Genomic_DNA.
DR PIR; T39663; T39663.
DR RefSeq; NP_595433.1; NM_001021341.2.
DR AlphaFoldDB; O74755; -.
DR SMR; O74755; -.
DR BioGRID; 276343; 10.
DR STRING; 4896.SPBC1734.16c.1; -.
DR iPTMnet; O74755; -.
DR MaxQB; O74755; -.
DR PaxDb; O74755; -.
DR PRIDE; O74755; -.
DR EnsemblFungi; SPBC1734.16c.1; SPBC1734.16c.1:pep; SPBC1734.16c.
DR GeneID; 2539793; -.
DR KEGG; spo:SPBC1734.16c; -.
DR PomBase; SPBC1734.16c; pst3.
DR VEuPathDB; FungiDB:SPBC1734.16c; -.
DR eggNOG; KOG4204; Eukaryota.
DR HOGENOM; CLU_001360_2_0_1; -.
DR InParanoid; O74755; -.
DR OMA; NYAIAYM; -.
DR PhylomeDB; O74755; -.
DR PRO; PR:O74755; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:1990483; C:Clr6 histone deacetylase complex I''; IPI:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0033698; C:Rpd3L complex; IDA:PomBase.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IDA:PomBase.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:PomBase.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:PomBase.
DR Gene3D; 1.20.1160.11; -; 3.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR Pfam; PF02671; PAH; 2.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 2.
DR PROSITE; PS51477; PAH; 3.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat.
FT CHAIN 1..1154
FT /note="Paired amphipathic helix protein pst3"
FT /id="PRO_0000121543"
FT DOMAIN 111..181
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 252..322
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 403..472
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 132881 MW; 29896703342DF40E CRC64;
MDVMNVPVDS ERDNPGDKVE TQSDKNHLPK ASPSQSQSPV NTSLHNGDGK DNGVATEPVE
NKQILSERSV TRDDYEKGKT IVSSLALSSI SGKDGSISSQ NAEGLSSSSN RPLDVNDALS
YLELVKYYFS ERREIYNRFL EIMRDFKSQA LDTLGVINRV SELFNGYPQL IEGFNTFLPS
GYKIEVQLDS SNTSVVRVGT PMHPLPQQGV QSTLPVAPSN EDQRTMESTS PTDSQPQPSA
PNLVSSTENE KPRVDFNYAI AYMNKVKARY PPNSDTYMEF LGVLRTYQKA QKSIFEVRAR
VAEIFKDSPD LLEEFKLFLP DNVDSTEPST PNVQKSPNRL PPVGNFSLPP SAPVREKRNR
PAHSAQISRS ISKTSRMYRQ TAEEPLNSYS LHVYPQKITA PTSPYAATQE ELLAFTTIRQ
HLPDTLAFHK FLELLHLYRE KLLDKTELLN SFSKLVRNDN LTLWFSEFIR WSDNPILVKN
EPVDERVYLP ETFECISLTY RKLPDSWKQD KCSGRDDLDN SVLNDDYISV APKPSHVKNI
MHHENQYLQA LQLVEDERYD YDRVLNTTES AIKILANFCE PTIHEHLETA LQELERSKRI
IKNALIIVYG KEHANLALDT LFKKLPTAAP VLLKRIKTKD QEWRRSKREW SKIWRQIEKK
NAQAAFDDRY CRIEGRDRRG LSYSRILRDI DDIYQRQKHR IDGAKLGFQF TQVLCDSLIF
LNILRLSDAQ LTNSSFYSYA DKGRISAVLK ALLSQFFGIP LPREALETNL ASENIESVKK
HRDGLSKIFI RPESADNSNN TNVSFQTDET QTEDETMSDI HPDDVENHSK SKFLGEESKN
IIGYNFFGNA TMYVLFRLIC VCYSRLEHIK LFVESSTIYA SSTGGYENIL NICEKYLKGS
CSRLEFRKYL QKFNNETCYM ICSIERLLKV IFYRIHEILL DPKLGQLLLL FESDGANSVT
TPREQMVYRN HVESILAPES KIFNMRWYPL EKRLCIQQLL PADLTMHDFE NPAKAFMYYV
DSYAISHITE GVDLMQVKMP FLRRSLQRIS QQGYLAGRGS GRLHSLFNEH FCKSNLQLFF
STDTYVIFFE PNTENVYINS YNLWVDQSSQ SKKQNRTTNW RRWLESDEGW RKSKANTDIK
FFSETTLDQC IEAM
