NO66_CAEEL
ID NO66_CAEEL Reviewed; 748 AA.
AC O01658; G8XYY5;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66;
DE EC=1.14.11.-;
DE EC=1.14.11.27;
DE AltName: Full=Histone lysine demethylase NO66;
DE AltName: Full=Jumanjic domain protein 1;
GN Name=jmjc-1; ORFNames=T28F2.4;
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=20057358; DOI=10.1038/emboj.2009.387;
RA Kirienko N.V., Fay D.S.;
RT "SLR-2 and JMJC-1 regulate an evolutionarily conserved stress-response
RT network.";
RL EMBO J. 29:727-739(2010).
CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase
CC and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-
CC 4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a
CC central role in histone code (By similarity). Mediates response to
CC multiple stress stimuli, including heat shock and osmotic, oxidative,
CC and ethanol stress. {ECO:0000250, ECO:0000269|PubMed:20057358}.
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 -!- 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=O01658-1; Sequence=Displayed;
CC Name=b;
CC IsoId=O01658-2; Sequence=VSP_053839, VSP_053840;
CC -!- DISRUPTION PHENOTYPE: Attenuated response to heat shock stress and
CC reduced survival after heat shock and oxidative stress.
CC {ECO:0000269|PubMed:20057358}.
CC -!- SIMILARITY: Belongs to the ROX family. NO66 subfamily. {ECO:0000305}.
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DR EMBL; FO080999; CCD68363.1; -; Genomic_DNA.
DR EMBL; FO080999; CCD68364.1; -; Genomic_DNA.
DR PIR; T15138; T15138.
DR RefSeq; NP_001021644.1; NM_001026473.4. [O01658-1]
DR RefSeq; NP_001021645.1; NM_001026474.2. [O01658-2]
DR AlphaFoldDB; O01658; -.
DR SMR; O01658; -.
DR BioGRID; 37407; 2.
DR STRING; 6239.T28F2.4a; -.
DR EPD; O01658; -.
DR PaxDb; O01658; -.
DR PeptideAtlas; O01658; -.
DR EnsemblMetazoa; T28F2.4a.1; T28F2.4a.1; WBGene00020902. [O01658-1]
DR EnsemblMetazoa; T28F2.4b.1; T28F2.4b.1; WBGene00020902. [O01658-2]
DR GeneID; 171932; -.
DR KEGG; cel:CELE_T28F2.4; -.
DR UCSC; T28F2.4a; c. elegans. [O01658-1]
DR CTD; 171932; -.
DR WormBase; T28F2.4a; CE28497; WBGene00020902; jmjc-1. [O01658-1]
DR WormBase; T28F2.4b; CE37050; WBGene00020902; jmjc-1. [O01658-2]
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR HOGENOM; CLU_013645_4_0_1; -.
DR InParanoid; O01658; -.
DR OMA; PVFEGWI; -.
DR OrthoDB; 487605at2759; -.
DR PhylomeDB; O01658; -.
DR PRO; PR:O01658; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00020902; Expressed in embryo and 3 other tissues.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISS:UniProtKB.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045471; P:response to ethanol; IMP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR039994; JmjC_protein.
DR PANTHER; PTHR13096; PTHR13096; 1.
DR Pfam; PF08007; Cupin_4; 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; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..748
FT /note="Bifunctional lysine-specific demethylase and
FT histidyl-hydroxylase NO66"
FT /id="PRO_0000390981"
FT DOMAIN 399..543
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 65..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..193
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 442
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 444
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 509
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT VAR_SEQ 121..125
FT /note="HTALV -> RTAAS (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053839"
FT VAR_SEQ 126..748
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053840"
SQ SEQUENCE 748 AA; 86026 MW; A3E1587BAAB5E3AA CRC64;
MGKKKNSNKS AAAAPAVKHN DRWSSIELGE AKSAAVSHYK EPSKEPKFVH PAKLEKVKRI
HDGLNIDRVL SHGPVPKQNG GTKRKHVEVT TQKLENKKPK VEVKKEDEKS KNKKMKNQNK
HTALVQNETS TRSTYFVEEP DNENKVTLIS NGREIAFKKT EVVESDDEQM IGLDSDEELE
DEDETDIDED EMMIDPKDIE RYINFESVED EEDMEDEEIE DEEFEDEEFE DEEEEADEQE
EEEEDVSDEE SVVSEMDADS DDEGFIAGKD REAHVISKDK FTRNAPAVDF DKFPFTDEDS
VVTSSRAFGF MISPCDVQTF FDKFYQSNVL VVRRKQPTYF GNLFSTARLG ELLEKNHLEY
GRNINIAQYK NGVRTTLNGQ GRAYPQIVKQ HLHNMCSVQL VNPQTYDDRI WYLCEVIQEQ
FGCFVGANTY LTPAGSSGFA PHWDEIDAFL LQVEGRKYWR VWAPESAEEE LPLESSDNFT
EDDMKGREPV FEGWIEKGDM IYIPRGYIHQ ARTDSKVHSL HVTVSTGRQW SFANLMEKVV
PEAIGVLTDT RHKLRRGLPT GLFDMGGVID LDYSQEDHFV EKFKMVVDRH MSMLRNLVAD
QLLESSVDSL AKEFMKQALP PRLTEQEKKL SVLGSSTNLL GDDLVDFTAR TKVRLIRRHT
QRLLMESEDA CFISHRINNS RLFEGRPEQI VEYPISGIDA YRVLSNSYPE WRTLYEIFSL
RETKTKSRKE NLAAIQLLFQ IGVLLVKN
