ID H2LQY0_ORYLA Unreviewed; 1068 AA.
AC H2LQY0;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase {ECO:0000256|ARBA:ARBA00012900};
DE EC=1.14.11.66 {ECO:0000256|ARBA:ARBA00012900};
GN Name=LOC101173928 {ECO:0000313|Ensembl:ENSORLP00000008475.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000008475.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000008475.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008475.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000008475.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008475.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000256|ARBA:ARBA00000040};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00009711}.
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DR AlphaFoldDB; H2LQY0; -.
DR STRING; 8090.ENSORLP00000008475; -.
DR Ensembl; ENSORLT00000008476.2; ENSORLP00000008475.2; ENSORLG00000006749.2.
DR eggNOG; KOG0958; Eukaryota.
DR GeneTree; ENSGT00940000159248; -.
DR HOGENOM; CLU_001442_0_1_1; -.
DR InParanoid; H2LQY0; -.
DR TreeFam; TF106449; -.
DR Proteomes; UP000001038; Chromosome 4.
DR Bgee; ENSORLG00000006749; Expressed in ovary and 14 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IBA:GO_Central.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 3.10.330.70; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694:SF7; [HISTONE H3]-TRIMETHYL-L-LYSINE(9) DEMETHYLASE; 1.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 102..144
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 230..396
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 719..838
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 120490 MW; 1C90B3AABD348D13 CRC64;
MATDMPMDMM SPPDPLPAQP PPPAFGAVLA QDHVPVQQPA GAQTPDTTKT SKDNVQPPLA
QSADPAIPPE PVSMSETPTP PLLAPTQQPQ PAFTAKNPSC KIMTFRPTME EFKDFAKYIV
YMESQGAHRA GLAKVIPPEG WKPRKSYDTI EDMVIPAPIM QVVTGQSGLF TQYNIQKKSM
SVGEFRKLAN SKKYCTPRHK DFDDLERKYW KNLTFVSPIY GADVGGSIYD EDIQEWNIGH
LNTLLDMVEQ ECGIVIEGVN TPYLYFGMWK TTFAWHTEDM DLYSINYLHF GQPKSWYTVP
PEHGKRLERL AQGFFPGSSQ GCDAFLRHKM TLISPSILKK YSIPFDRITQ NEGEFMITFP
YGYHAGFNHG FNCAESTNFA TLRWVDYGKN ATLCSCRKDM VKISMDVFVR RLQPDRYELW
KQGKDMTVLD HLKPTELDSP ELERWRQHRV TFRMNLLRRA MQKMKMLRRL KLEEVKVLAE
EGISLNAAEY QRQVEEREAQ RKKEREERLA REALMTLEAM EREEQEAAAK AAETPAADND
VDKKKHKKQK RTSNALSGFE EVFEEFAKST MKNSANMIND FPTSFSKMKM PTEVKKSRRH
PLSKPPTRTP PSVVKQDPAS EKGIPLYVTD MKKQEHLWQN HSPNFLAEKA FNAAVAALQP
HCAVCSLFCP YAANAPFPRH GSWTRPLVPE MCFSVGAGNP EPPPTNHHIR EDGTSLLLRC
TSCEMQVHAS CYGVKPDSVS SSWRWVHVIC AIAVAEARFI NAIDREPVDV SAVPETRKNL
RCVFCHSKSS NQNRGACIQC TYENCATSFH VTCAQIAGVL MKPADWPYVV SVICQKHKKN
QRKISNGNGP FLGQTVIGRN RDSWYYHCTI IGMATQTFYE VNFDDGSYCD NVYPENIVSH
DCLHNGPPEA GELITVATPE GQILRASFVK QHSHKLYQVE FGNQSQLMLK HSEVFQLDHE
LPKRVKARLV SVPFFSGNQM DAETPMDTSS PLAAALSESF LGSDPTLTPQ STPFQATLNS
DPLLSAQSPP HPQHHMSEGY TPSSGYVSYM ETLLHSHFPQ DDGSSSLY
//