ID A0A340WPS1_LIPVE Unreviewed; 1053 AA.
AC A0A340WPS1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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_007451518.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007451518.1};
RN [1] {ECO:0000313|RefSeq:XP_007451518.1}
RP IDENTIFICATION.
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_007451518.1; XM_007451456.1.
DR AlphaFoldDB; A0A340WPS1; -.
DR STRING; 118797.A0A340WPS1; -.
DR GeneID; 103076969; -.
DR CTD; 23081; -.
DR InParanoid; A0A340WPS1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000265300; Unplaced.
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 CDD; cd15577; PHD_JMJD2C; 1.
DR CDD; cd20465; Tudor_JMJD2C_rpt1; 1.
DR CDD; cd20468; Tudor_JMJD2C_rpt2; 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); 2.
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; IPR011011; Znf_FYVE_PHD.
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; SSF57903; FYVE/PHD zinc finger; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
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 749..862
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 369..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1053 AA; 119329 MW; 426766C1A96EBBDE CRC64;
MEVAKVESPL NPSCKIMTFR PCMEEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQC
YDDIDNLLIP APIQQMVTGQ SGLFTQYNIQ KKAMTVKEFR QLANSGKYCT PRYLDYEDLE
RKYWKNLTFV APIYGADING SIYDEGVDEW NIAHLNTVLD VVEEECGISI EGVNTPYLYF
GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL
RHKMTLISPS VLKKYGIPFD KITQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID
YGKVAKLCTC RKDMVKISMD IFVRKFQPDR YQLWKQGKDI YTIDHTKPTP ESTPEVKAWL
QRRRKVRKAS RSFQCTSSHS KRPKNEEDEE VSAAVDGAEG PTPDPDPDEL KDSEKPEEAL
KLANTEAPSE EEASASKMQL DHNVSDNIRF AGNVCLSTSV AEKIKTEADQ TCATIPPSNP
SDADDSMSSG HVMSKESEPP KLPWPKSPES CSSVAESNSA LTEGEESDVE SHGVGLEPGE
VPEVPSGERN GFKVPSVCEG ETKTAKSWRH PLSKPPARSP MTLVKQQATS DEELPEVPSI
EEEVEETESW AKPLVHLWQT KSPNFVAEQE YNAAMGRMEP HCAICALLMP YYKPDSSNEE
NDSRWETRLD EVVTSGGKTK PLIPEMCFIY REENIEYSPP NAFLEEDGTS LLISCAKCRV
RVHASCYGIP SHEICDGWLC ARCKRNAWTA ECCLCNLRGG ALKETKNNKW AHVMCAVAVP
EVRFTNVPER TQIDVGRIPL QRLKLKCMFC RHRVKKVSGA CIQCSYGRCP ASFHVTCAHA
AGVLMEPDDW PYVVNITCFR HKVNPNVKSK AGEKGIAVGQ TVITKHRNTR YYSCRVIAVT
AQTFYEVVFD DGSFSRDTFP EDIVSRDCVR LGPPAEGEVV QVKWPDGKLY GAKYLGSNVA
HMYQVEFEDG SQIAMKREDI YTLDEELPKR VKARFSTASD MRFEDTFYGT DIIQGEKKRQ
RVLSSRFKNE YVDDPVYRTF LKSSFQKKCQ KRQ
//
