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Database: UniProt
Entry: H2LQY0_ORYLA
LinkDB: H2LQY0_ORYLA
Original site: H2LQY0_ORYLA 
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
//
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