ID   JHD1_SCHPO              Reviewed;         948 AA.
AC   O94603;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JUN-2009, entry version 52.
DE   RecName: Full=Putative JmjC domain-containing histone demethylation protein 1;
DE            EC=1.14.11.27;
DE   AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
DE   AltName: Full=Heterochromatin-destabilizing protein epe1;
GN   Name=jhd1; Synonyms=epe1; ORFNames=SPCC622.16c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-307.
RX   MEDLINE=22658528; PubMed=12773576;
RX   DOI=10.1128/MCB.23.12.4356-4370.2003;
RA   Ayoub N., Noma K., Isaac S., Kahan T., Grewal S.I.S., Cohen A.;
RT   "A novel jmjC domain protein modulates heterochromatization in fission
RT   yeast.";
RL   Mol. Cell. Biol. 23:4356-4370(2003).
RN   [3]
RP   POSSIBLE FUNCTION AS A DEMETHYLASE.
RX   PubMed=15809658; DOI=10.1038/sj.embor.7400379;
RA   Trewick S.C., McLaughlin P.J., Allshire R.C.;
RT   "Methylation: lost in hydroxylation?";
RL   EMBO Rep. 6:315-320(2005).
RN   [4]
RP   LACK OF DEMETHYLASE ACTIVITY IN VITRO.
RX   PubMed=16362057; DOI=10.1038/nature04433;
RA   Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H.,
RA   Tempst P., Zhang Y.;
RT   "Histone demethylation by a family of JmjC domain-containing
RT   proteins.";
RL   Nature 439:811-816(2006).
CC   -!- FUNCTION: May have histone demethylase that specifically
CC       demethylates 'Lys-36' of histone H3, thereby playing a central
CC       role in histone code (By similarity). Represses transcriptional
CC       silencing by negatively affecting heterochromatin stability.
CC   -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2-
CC       oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate +
CC       formaldehyde + CO(2).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate
CC       + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The JmjC domain mediates the demethylation activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- CAUTION: In contrast to other JHDM1 histone demethylases, it lacks
CC       the iron catalytic His in position 370 which is replaced by a Tyr
CC       residue and has no histone demethylase activity in vitro. It
CC       therefore may not be functional in vivo.
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DR   EMBL; CU329672; CAA21872.1; -; Genomic_DNA.
DR   PIR; T41496; T41496.
DR   RefSeq; NP_588188.1; -.
DR   GeneID; 2539481; -.
DR   KEGG; spo:SPCC622.16c; -.
DR   NMPDR; fig|4896.1.peg.526; -.
DR   GeneDB_Spombe; SPCC622.16c; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-000127-MON; -.
DR   BRENDA; 1.14.11.27; 653.
DR   ArrayExpress; O94603; -.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:GeneDB_SPombe.
DR   GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:GeneDB_SPombe.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:GeneDB_SPombe.
DR   GO; GO:0030702; P:chromatin silencing at centromere; IMP:GeneDB_SPombe.
DR   GO; GO:0030466; P:chromatin silencing at silent mating-type c...; IMP:GeneDB_SPombe.
DR   GO; GO:0007059; P:chromosome segregation; IMP:GeneDB_SPombe.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0031454; P:regulation of extent of heterochromatin for...; IMP:GeneDB_SPombe.
DR   GO; GO:0006357; P:regulation of transcription from RNA polyme...; IMP:GeneDB_SPombe.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   Pfam; PF02373; JmjC; 1.
DR   SMART; SM00558; JmjC; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Complete proteome; Dioxygenase; Iron;
KW   Metal-binding; Nucleus; Oxidoreductase; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    948       Putative JmjC domain-containing histone
FT                                demethylation protein 1.
FT                                /FTId=PRO_0000086985.
FT   DOMAIN      243    402       JmjC.
FT   METAL       297    297       Iron; catalytic (By similarity).
FT   METAL       299    299       Iron; catalytic (By similarity).
FT   BINDING     294    294       Substrate (By similarity).
FT   BINDING     314    314       Substrate (By similarity).
FT   MUTAGEN     307    307       Y->A: Loss of function.
SQ   SEQUENCE   948 AA;  108653 MW;  5CACC9C1F39751C4 CRC64;
     MDSWLEYDDI INQDIDIPSN DLSGSGTLCV GVHSSLLENS LNSIDSFISS KEEISWCGNQ
     STPIATKSHL SCINPQYVNP FDTSPVSVDT EFQDTYLLDA PSFAQPHFSE RQSVDKTRSR
     CLSRNRRRKR HPNLHKNHQR LLGMSFPQDG FRRMPAESVN FSYFRDTGFN EPTIFPSSDT
     QNTRQLNLSK IATLIGYDCP LALVDVVTQK QIPNKMDMES WVKYMSLEPS KRGRIYDVLS
     LEVSTTKLAY YVRKPNIVRD LDLVNTVWPP GSFALGEYPH VDTYCLMSAE NSYTEFHIEF
     GGSSAYYNIL DGCKIFYLIP GTSKNWEAYT AWLTSSNDSD KKFLPNMVDV CYCVEVHSQQ
     TILVPSGWIY AVVTPCDTIS IAGNFLTFLH IYPQLSIYNL ELQLGIEKEY QYPYFESIMW
     YTAIHFYLAF PDNSSRDGID DIIAEYETGR LFDINAFTEQ ELDGFEELLN YLYIRAQILR
     DCDIIIDIYN EPVKISKNNG YNSAYTMVPP DLDEICVDFV QKFGAWITYH HRRSAKHPSC
     NCFSHLQTKL IDSGPKPANN SYQHQSNFIG VVISTNHNII KKCQESQIQT GKNNCSFQLV
     KKRIKSTKKA PSWRSIIKAF KKRENTRCNF LSSLHATTFR EDIVVRPKIK SFVLEQLIFQ
     ALFSFAINWT PSFFLNHSNF ENIALSKETF NFGGEANCEN TDTTLFTTWG DQGFRPSDSI
     CYNDFNLLET ANSDAEASIH ELELQPLNAV NEREVDISQT DMTPSTALDT RVDTRVDSLP
     EFSNLILSPS SNDDSFQLDD LLSPSSSNLK QQIQKVVPQN SLEFSVGEKE KKAAEYSLLH
     TFSYKRLSME NEKPDTTKVP LKYNIQHEEM KAYRRKNDLE YIDQHFASSK SGISNGRNNN
     KEVNLTKAEN VGIKKRRIMK NENNIYDFED HSPVREKWGH RLRSRGAS
//