ID   A0A2D0QGV3_ICTPU        Unreviewed;      1278 AA.
AC   A0A2D0QGV3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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|RefSeq:XP_017316656.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017316656.1};
RN   [1] {ECO:0000313|RefSeq:XP_017316656.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017316656.1};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_017316655.1; XM_017461166.1.
DR   RefSeq; XP_017316656.1; XM_017461167.3.
DR   AlphaFoldDB; A0A2D0QGV3; -.
DR   STRING; 7998.ENSIPUP00000002111; -.
DR   GeneID; 108260706; -.
DR   KEGG; ipu:108260706; -.
DR   CTD; 23081; -.
DR   OrthoDB; 48111at2759; -.
DR   Proteomes; UP000221080; Chromosome 29.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
SQ   SEQUENCE   1278 AA;  142591 MW;  70F8B4E9D43D5D3F CRC64;
     MAGVGANASA NPACKIMTFH PTMEEFRDFN KYLVYMESQG AHRAGLAKVI PPKGWKPRRT
     YDDIDDLVIL APIQQMVAGQ SGLFTQYNIQ KKPLSVQEFR RLANSDKYCT PRYLNYEDLE
     RKYWKNVTFV PPIYGADVSG TLYDEDVEEW NIGHLNSILD VIEEDCGVSI QGVNTPYLYF
     GMWKTSFSWH TEDMDLYSIN YLHFGEPKFW YAIPPEHGKR LERLATGFFP NSFKSCEAFL
     RHKMTLISPS VLKKYSIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFASLRWID
     YGKVATQCTC SKDMVKISMD PFVRRFQPDR YPAWTQGKDA CSIDHTRTTP GSTPELQAWL
     QRRRKTRTNK KVSYPCTRSK RLKTVQQPVV VENATARTSD QEEDVKEEED AKPHNASRLS
     GPATLCQQMC FVKVTRVKSN LLAQSSKRVP PPNPQDTARE ALGTDEPPNS ADEASGTDDT
     PDSEETPERF CVAKSSSSKS PNRSCCQEEE EEEEENRSAV NPSSTTVTME TCGFAERSGA
     PSSDMPLLTP EVTEDPEGRK SPNLSSEMPF LTLAVQSGDD DMLPNPNGPE DSTPPQNAMG
     ETGVCCSKAP YSDWCSNPFR EDVGQSLGSD PDANEELLEK SDGDGSASVH TSHHPKASTE
     LSSESPSTSY GQNPLDEADF TSSALPNLFG ESSTVWKSLS YQNPDVSELA VPYAVWAEPR
     CQQVKCPDPS DFPEKSLTFT DLEPSVAHHS GAELLDSPGR PPRSDSSSES GEENSSVSET
     EYEDSGIEPG EIRIYTMPTA KRKTTKSWRH PLRKPTARAV PSAVKQQANS DDEPMEECIA
     EEELQEADVW ARPLVHLWHG RKSHFPSERE YNSAAAKTAP NCAVCTLFMP YYQPEETKDE
     SRPEVTMAVR EAAARSRPLI PEICFAYREG SCPPNTLLEE DGSSPLVACK HCCVQVHASC
     YGVAAHEVTP DWTCDRCSCG DLTAECCLCN LRGGALKRTT DDRWAHVMCA VGLPEAKFTD
     VVKRSPVDVS GVPAQRYKLK CIYCHKRMKK LAGACIQCSC GRCPTSFHVT CAHAAGVTME
     PDDWPYVVFI ICHRHQSRSS SAKSKVSQTE LALGQTVIAK HKNLRYYSSR VASVTAQTFY
     EVMFDDGSFS NDTFPEDIVS RDCGQLGPPE VSEVVQVKWP DGLFYGAKYL GSNTTYMYQV
     EFEDGSQVLA KREDIYTLDE DLPKKVKGRL STASSMRFED AFFTTQGERK RQRTPNSRFQ
     NDYVADPNPR TSSCSKTN
//