JHD1_SCHPO
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 03-AUG-2022, entry version 136.
DE RecName: Full=Putative JmjC domain-containing histone demethylation protein 1;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:P40034};
DE AltName: Full=Heterochromatin-destabilizing protein epe1;
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
GN Name=jhd1; Synonyms=epe1; ORFNames=SPCC622.16c;
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).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-307.
RX PubMed=12773576; 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 proteins.";
RL Nature 439:811-816(2006).
CC -!- FUNCTION: May be a histone demethylase that specifically demethylates
CC 'Lys-36' of histone H3, thereby playing a central role in histone code
CC (By similarity). Represses transcriptional silencing by negatively
CC affecting heterochromatin stability. {ECO:0000250|UniProtKB:P40034,
CC ECO:0000269|PubMed:12773576}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000250|UniProtKB:P40034};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- INTERACTION:
CC O94603; Q10990: cdt2; NbExp=2; IntAct=EBI-3505187, EBI-3505190;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773576}.
CC -!- DOMAIN: The JmjC domain mediates the demethylation activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
CC -!- CAUTION: In contrast to other JHDM1 histone demethylases, it lacks the
CC iron catalytic His in position 370 which is replaced by a Tyr residue
CC and has no histone demethylase activity in vitro (PubMed:16362057). It
CC therefore may not be functional in vivo. {ECO:0000305|PubMed:16362057}.
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DR EMBL; CU329672; CAA21872.1; -; Genomic_DNA.
DR PIR; T41496; T41496.
DR RefSeq; NP_588188.1; NM_001023178.2.
DR AlphaFoldDB; O94603; -.
DR SMR; O94603; -.
DR BioGRID; 276044; 327.
DR IntAct; O94603; 2.
DR STRING; 4896.SPCC622.16c.1; -.
DR iPTMnet; O94603; -.
DR PaxDb; O94603; -.
DR PRIDE; O94603; -.
DR EnsemblFungi; SPCC622.16c.1; SPCC622.16c.1:pep; SPCC622.16c.
DR GeneID; 2539481; -.
DR KEGG; spo:SPCC622.16c; -.
DR PomBase; SPCC622.16c; -.
DR VEuPathDB; FungiDB:SPCC622.16c; -.
DR eggNOG; KOG1633; Eukaryota.
DR HOGENOM; CLU_013397_0_0_1; -.
DR InParanoid; O94603; -.
DR Reactome; R-SPO-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-SPO-3214842; HDMs demethylate histones.
DR PRO; PR:O94603; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:1990342; C:heterochromatin island; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:PomBase.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..948
FT /note="Putative JmjC domain-containing histone
FT demethylation protein 1"
FT /id="PRO_0000086985"
FT DOMAIN 243..402
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 299
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 307
FT /note="Y->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:12773576"
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
