ID   HIF2_SCHPO              Reviewed;         564 AA.
AC   O74845;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Set3 complex subunit hif2;
GN   Name=hif2; ORFNames=SPCC1235.09;
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   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).
RN   [3]
RP   IDENTIFICATION IN THE SET3 COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA   Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA   Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT   "Chromatin Central: towards the comparative proteome by accurate mapping of
RT   the yeast proteomic environment.";
RL   Genome Biol. 9:R167.1-R167.22(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP   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: Component of the set3 histone deacetylase complex which is
CC       involved in chromatin remodeling and transcription regulation, such as
CC       repression of the sporulation gene program.
CC   -!- SUBUNIT: Component of the set3 histone deacetylase complex.
CC       {ECO:0000269|PubMed:19040720}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
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DR   EMBL; CU329672; CAA21113.1; -; Genomic_DNA.
DR   PIR; T40883; T40883.
DR   RefSeq; NP_587735.1; NM_001022730.2.
DR   AlphaFoldDB; O74845; -.
DR   SMR; O74845; -.
DR   BioGRID; 275286; 105.
DR   STRING; 4896.SPCC1235.09.1; -.
DR   iPTMnet; O74845; -.
DR   MaxQB; O74845; -.
DR   PaxDb; O74845; -.
DR   PRIDE; O74845; -.
DR   EnsemblFungi; SPCC1235.09.1; SPCC1235.09.1:pep; SPCC1235.09.
DR   GeneID; 2538701; -.
DR   KEGG; spo:SPCC1235.09; -.
DR   PomBase; SPCC1235.09; hif2.
DR   VEuPathDB; FungiDB:SPCC1235.09; -.
DR   eggNOG; KOG0273; Eukaryota.
DR   HOGENOM; CLU_007609_1_1_1; -.
DR   InParanoid; O74845; -.
DR   OMA; EMSTIAW; -.
DR   PhylomeDB; O74845; -.
DR   PRO; PR:O74845; -.
DR   Proteomes; UP000002485; Chromosome III.
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:0070210; C:Rpd3L-Expanded complex; IDA:PomBase.
DR   GO; GO:0034967; C:Set3 complex; IDA:PomBase.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR045183; Ebi-like.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR22846; PTHR22846; 1.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   WD repeat.
FT   CHAIN           1..564
FT                   /note="Set3 complex subunit hif2"
FT                   /id="PRO_0000303899"
FT   DOMAIN          2..34
FT                   /note="LisH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT   REPEAT          262..302
FT                   /note="WD 1"
FT   REPEAT          303..342
FT                   /note="WD 2"
FT   REPEAT          344..382
FT                   /note="WD 3"
FT   REPEAT          386..425
FT                   /note="WD 4"
FT   REPEAT          430..470
FT                   /note="WD 5"
FT   REPEAT          473..512
FT                   /note="WD 6"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   564 AA;  62758 MW;  11C836D2C295B389 CRC64;
     MDTNQVNYII WRYLKECGYS HTKFAFERET GIQNLDKQWG STCQVGALVE ILQKGLQYVE
     LEKHYVDNHS SNEEASKTSI DGESLVNENP CKLPFYLTVP HICETTLTKA DSTNGFCEHN
     NSNDHQLKIL QDKGSGSPSS PVMPFKDKIE KRDIDITMAD ESNVEKDPAR PIAVYNSSPV
     TEITEIKQVT FTGGEDIKSD FFKVIPTKHP VTCADWRPLL QENYHVYEFS IGMTNATLAS
     VSICEEQNDF KAKTDYCLQS SFDNQDITGV AWNNSGSFLA YAFFSGVIEI YDSHGSQILS
     FHNNKGPVLS LKWSGTDTYL AAGSADGTIT LFDQLKQTQY SIDTLASSVL DIEWISFDEF
     VTSDVEGSLR VYKVDGKAPV STVSHAHDNS IVALRYNLRI SLLLTASSDT TVKLWSRGDA
     GAFECLHVFS FSSPVNCIDW NLREGTPILA VASNSIVSMY NAISLQQLAV FMRHTAPVSA
     LSFSHNGRYL ATGDTSGGVC IWSCKTAKLF KELGSDNSEL IAVTNVLPEE QVNFLRWSFD
     DKDLLIGKQK KEIICCCDFL HDSL