ID A0A9L0K3L6_EQUAS Unreviewed; 1052 AA. AC A0A9L0K3L6; DT 13-SEP-2023, integrated into UniProtKB/TrEMBL. DT 13-SEP-2023, sequence version 1. DT 02-SEP-2026, entry version 15. 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=KDM4C {ECO:0000313|Ensembl:ENSEASP00005055940.1}; OS Equus asinus (Donkey) (Equus africanus asinus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9793 {ECO:0000313|Ensembl:ENSEASP00005055940.1, ECO:0000313|Proteomes:UP000694387}; RN [1] {ECO:0000313|Ensembl:ENSEASP00005055940.1, ECO:0000313|Proteomes:UP000694387} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=33293529; RA Wang, C., Li, H., Guo, Y., Huang, J., Sun, Y., Min, J., Wang, J., Fang, X., RA Zhao, Z., Wang, S., Zhang, Y., Liu, Q., Jiang, Q., Wang, X., Guo, Y., Yang, RA C., Wang, Y., Tian, F., Zhuang, G., Fan, Y., Gao, Q., Li, Y., Ju, Z., Li, RA J., Li, R., Hou, M., Yang, G., Liu, G., Liu, W., Guo, J., Pan, S., Fan, G., RA Zhang, W., Zhang, R., Yu, J., Zhang, X., Yin, Q., Ji, C., Jin, Y., Yue, G., RA Liu, M., Xu, J., Liu, S., Jordana, J., Noce, A., Amills, M., Wu, D.D., Li, RA S., Zhou, X. and Zhong, J.; RT "Donkey genomes provide new insights into domestication and selection for RT coat color."; RL Nat. Commun. 11:6014-6014(2020). RN [2] {ECO:0000313|Ensembl:ENSEASP00005055940.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 2 2- CC oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(9)-[histone H3] + 2 CC formaldehyde + 2 succinate + 2 CO2; 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:ARBA00049349}; 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 ECO:0000256|PROSITE-ProRule:PRU00537}. CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family. CC {ECO:0000256|ARBA:ARBA00009711}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A9L0K3L6; -. DR Ensembl; ENSEAST00005044332.1; ENSEASP00005055940.1; ENSEASG00005010714.2. DR GeneTree; ENSGT00940000154930; -. DR Proteomes; UP000694387; Chromosome 23. DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:TreeGrafter. DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC. DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter. DR CDD; cd15715; ePHD_JMJD2C; 1. DR CDD; cd15577; PHD_JMJD2C; 1. DR CDD; cd20465; Tudor_JMJD2C_rpt1; 1. DR CDD; cd20468; Tudor_JMJD2C_rpt2; 1. DR FunFam; 2.60.120.650:FF:000048; Lysine-specific demethylase 4A; 1. DR FunFam; 3.30.40.10:FF:000029; lysine-specific demethylase 4C isoform X1; 1. DR FunFam; 3.10.330.70:FF:000001; Putative lysine-specific demethylase 4a; 1. 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; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1. DR PANTHER; PTHR10694:SF104; LYSINE-SPECIFIC DEMETHYLASE 4C; 1. DR Pfam; PF02373; JmjC; 1. DR Pfam; PF02375; JmjN; 1. DR Pfam; PF13831; PHD_2; 1. DR Pfam; PF18104; Tudor_2; 2. DR Pfam; PF13832; zf-HC5HC2H_2; 1. DR SMART; SM00558; JmjC; 1. DR SMART; SM00545; JmjN; 1. DR SMART; SM00249; PHD; 2. 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 Dioxygenase {ECO:0000256|ARBA:ARBA00022964}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00538}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00538}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE- KW ProRule:PRU00537}; Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000694387}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|PROSITE- KW ProRule:PRU00537}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, KW ECO:0000256|PROSITE-ProRule:PRU00537}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 16..58 FT /note="JmjN" FT /evidence="ECO:0000259|PROSITE:PS51183" FT DOMAIN 144..310 FT /note="JmjC" FT /evidence="ECO:0000259|PROSITE:PS51184" FT DOMAIN 748..861 FT /note="PHD-type" FT /evidence="ECO:0000259|PROSITE:PS51805" FT REGION 367..388 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 418..582 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 371..380 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 435..460 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 479..491 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 508..520 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 190 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00538" FT BINDING 192 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00538" FT BINDING 278 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00538" SQ SEQUENCE 1052 AA; 118804 MW; C242CB09CC1C18AA CRC64; MEEAEVESPL NPSCKIMTFR PSMEEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQC YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR QLANSGKYCT PRYLDYEDLE RKYWKNLTFV APIYGADING SIYDEGVDEW NIARLNTVLD VVEEECGISI EGVNTPYLYF GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL RHKMTLISPS VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID YGKVAKLCTC RKDMVKISMD IFVRKFQPDR YQLWKQGKDI YTIDHTKPTP ESTPEVKAWL QRRRKVRKAS KSFQGTSSQS KRPKNEEDGE VLAAVGAEGP TSDPHPDDLK ASEKPEAAAK LGNTQAPSEE EASASRMQLD QNSSENIRLS GNSCSSTSIM EETKTENDQA CATIPPSNPS EADNSASSGH VTSEELDPPK LPWPKSPESC SSMAESNSVL TEGEESDVES RGSGLEPGEV PAVPSGERNG FKVPTRIEGE TKTAKSWRHP LSKPPARSPM TLVKQQATSD EELLEVPSIE EEVEETESWA KPLVHLWQTK SPNFAAEQEY NAAVARMEPH CAICALLMPY YKPDSSNEEN DSRWETKLDE VVTSGGKTKP LIPEMCFIYS EENIEYSPPN AFLEEDGTSL LISCAKCCVR VHASCYGIPS HEICDGWLCA RCKRNAWSAE CCLCNLRGGA LKETKNNKWA HVMCAVAVPE VRFTNVPERT QIDVGRIPLQ RLKLKCIFCR HRVKKVSGAC IQCSYGRCPA SFHVTCAHAA GVLMEPDDWP YVVNITCFRH KVNPNVKSKA GEKGISVGQT VITKHRNTRY YSCRVMAVTS QTFYEVVFDD GSFSRDTFPE DIVSRDCVKL GPPAEGEVVQ VKWPDGKLYG AKYLGSNVAH MYQVEFEDGS QIAMKREDIY TLDEELPKRV KARFSTASDM RFEDTFYGAD IIQGEKKRQR VLSSRFKNEY VDDPVYRTFL KSSFQKKCQK RQ //