JHD1_CAEEL
ID JHD1_CAEEL Reviewed; 1076 AA.
AC Q95Q98; Q95Q99;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=JmjC domain-containing histone demethylation protein 1;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:P40034};
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1;
GN Name=jhdm-1; ORFNames=T26A5.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21834846; DOI=10.1111/j.1474-9726.2011.00738.x;
RA Maures T.J., Greer E.L., Hauswirth A.G., Brunet A.;
RT "The H3K27 demethylase UTX-1 regulates C. elegans lifespan in a germline-
RT independent, insulin-dependent manner.";
RL Aging Cell 10:980-990(2011).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-36'
CC of histone H3, thereby playing a central role in histone code (By
CC similarity). Has a role in regulating lifespan.
CC {ECO:0000250|UniProtKB:P40034, ECO:0000269|PubMed:21834846}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q95Q98-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q95Q98-2; Sequence=VSP_017481, VSP_017482;
CC -!- DOMAIN: The JmjC domain mediates the demethylation activity.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown introduced at L1 and
CC young adult stages increases lifespan by 12% and 15% respectively.
CC {ECO:0000269|PubMed:21834846}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; FO080366; CCD63210.1; -; Genomic_DNA.
DR EMBL; FO080366; CCD63211.1; -; Genomic_DNA.
DR RefSeq; NP_498418.3; NM_066017.6.
DR RefSeq; NP_498419.3; NM_066018.9.
DR AlphaFoldDB; Q95Q98; -.
DR SMR; Q95Q98; -.
DR BioGRID; 41137; 2.
DR STRING; 6239.T26A5.5a; -.
DR iPTMnet; Q95Q98; -.
DR EPD; Q95Q98; -.
DR PaxDb; Q95Q98; -.
DR PeptideAtlas; Q95Q98; -.
DR PRIDE; Q95Q98; -.
DR EnsemblMetazoa; T26A5.5a.1; T26A5.5a.1; WBGene00020821.
DR EnsemblMetazoa; T26A5.5b.1; T26A5.5b.1; WBGene00020821.
DR GeneID; 175919; -.
DR KEGG; cel:CELE_T26A5.5; -.
DR UCSC; T26A5.5b; c. elegans. [Q95Q98-1]
DR CTD; 175919; -.
DR WormBase; T26A5.5a; CE50209; WBGene00020821; jhdm-1.
DR WormBase; T26A5.5b; CE50262; WBGene00020821; jhdm-1.
DR eggNOG; KOG1633; Eukaryota.
DR GeneTree; ENSGT00940000167551; -.
DR HOGENOM; CLU_286864_0_0_1; -.
DR InParanoid; Q95Q98; -.
DR OrthoDB; 353641at2759; -.
DR Reactome; R-CEL-3214842; HDMs demethylate histones.
DR PRO; PR:Q95Q98; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00020821; Expressed in embryo and 4 other tissues.
DR ExpressionAtlas; Q95Q98; baseline and differential.
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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF13621; Cupin_8; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Chromatin regulator; Dioxygenase; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1076
FT /note="JmjC domain-containing histone demethylation protein
FT 1"
FT /id="PRO_0000226789"
FT DOMAIN 93..265
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 597..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..635
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..838
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..992
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT VAR_SEQ 504..505
FT /note="TG -> PN (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_017481"
FT VAR_SEQ 506..1076
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_017482"
SQ SEQUENCE 1076 AA; 123434 MW; C050485361154151 CRC64;
MDPEALNLEF YDKNGLDNPI HFRCDPKRIG MTLPSPDFSV DDVLELVGGN RMIEVVQVQN
QGSVKMSLQE FINFYKTPQE KREVLYNVLS LEFSQTPLED LVKSPELVRQ IDWVGNQWPD
ALRQRWISFN GRDKKFYNPH HTFPKVQNYC LMSVANCYTD FHIDFSGTSV WYHVLKGRKV
FWLIPPTETN FFIYQEFIKT VNDNAFFGKS VEKCHVAILE PGDTMLIPSG WIHAVYTPDD
SLVFGGNFLH SQSCKTQLRV YQVENKLNIT RKFRLPYNEE LIFYVIADYV KQWTGREYVR
PLRIEDAKYD YVGDKWKTAG GHHKKIEYSD YETGVELTND MIKGDEESTK DEVKVIAMHA
ENSLFGYPMV SKATFSADTG LEEEADEDEV KYQETKEEMD ARRDAEIDEL ANSNSLIFYK
NRTHDFVRNK CVPDHKLPIG HEPPIYFNDD EISRISPRLL DELETLGTYI RRKARVEVAE
GICQPASLIN TFQTVLKKRR SELTGKKFEF NQIMPRRYTR STMETGEYDF QPTQEVPQES
ARRSTRFKVD NFPDELLESE VTDKPIILPQ QPSSGPLEYL PAPKDEIKED INGFEEEFEE
EYEGIGQRDD QEEEEYDAEE PEDQEEEEED EYQAEEYTPT PVTRRSSSRR SGAKNDESEE
VSVKKDKKEK MEKVEKDEKR RNSKSKKDKI SKEKKKKERE RIELESQLDA ELRAAHGGGS
SKSKKKKPEK PAFVGGLPTS SIQIDPVVSN PYNYDPRMEM MKLGTGQLKS AYRKTKNNVE
LHIEKNLYKI EPKRGSEEGS QSREQSMEPE HSTPVFTTFD DINEANNDHY DGQKPPTKRA
KYEAISVDTY ETPSSSRNKE HKEYRPSPNA APTPSPSHHQ KPKLSSPAMV SSTNEYQLRK
HMSSERRSSD AGSAMKKGVY MPAMSRQDKM IAEGASAPSS RHSSISSERR PSFIPDFNSS
RNSSIDTPYT PTTVTPSRSS WLPNTSSINR HSIEDDSPID VVNDSLSPIN IASSPTYPTA
ITPPPVTLSD LKKDMSNGRK SHSQHHDDGH KHKIPSKEAI AELKLLVGKL KAINDS
