ID A0A4X2K5N0_VOMUR Unreviewed; 1074 AA.
AC A0A4X2K5N0;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:ENSVURP00010007283.1};
OS Vombatus ursinus (Common wombat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Vombatidae; Vombatus.
OX NCBI_TaxID=29139 {ECO:0000313|Ensembl:ENSVURP00010007283.1, ECO:0000313|Proteomes:UP000314987};
RN [1] {ECO:0000313|Proteomes:UP000314987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yazar S.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSVURP00010007283.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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; A0A4X2K5N0; -.
DR STRING; 29139.ENSVURP00010007283; -.
DR Ensembl; ENSVURT00010008234.1; ENSVURP00010007283.1; ENSVURG00010005641.1.
DR GeneTree; ENSGT00940000154930; -.
DR OMA; VAKMEPH; -.
DR Proteomes; UP000314987; Unassembled WGS sequence.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0062072; F:H3K9me3 modified histone binding; IEA:Ensembl.
DR GO; GO:0051864; F:histone H3K36 demethylase activity; IEA:Ensembl.
DR GO; GO:0140684; F:histone H3K9me2/H3K9me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IEA:Ensembl.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd15715; ePHD_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:UP000314987};
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 770..883
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 367..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1074 AA; 122304 MW; 5FC488FA2596AC2B CRC64;
MEAAEVDSPP NLSCKIMTFR PSMDEFREFN KYLAYMESKG AHRAGLAKVI PPKEWKPRQR
YDDIDNLVIP APIQQMVTGQ SGLFTQYNIQ KKPMTVKEFR QLANSDKYCT PRYLDYEDLE
RKYWKNLTFV APIYGADING SIYDEGVDEW NIAHLNTILD VVGEECGISI EGVNTPYLYF
GMWKTTFAWH TEDMDLYSIN YLHFGEPKSW YAIPPEHGKR LERLAQGFFP SSSQGCDAFL
RHKMTLISPS VLKKYGIPFD KVTQEAGEFM ITFPYGYHAG FNHGFNCAES TNFATVRWID
YGKMAKLCTC RKDMVKISMD IFVKKFQPDR YHLWKQGKDI YTIDHTLPTP ETTPEVKLWL
QRRKIKKPSR SLQHTRSRSK KLKTPEDERI SAMVVGAEIV ATEAATDDFK VNEKPAEKKE
LVNTGMPSGE ENTIKRMQVD QNLLDNIKVS GSSDLSTSFH PDSVKQEIKP EDDKVGSTIA
ASDSVESSAS MPLSFECIKE DNLKSEREHE QTVSRPKSCE SVSSEAESLE KEESSSISTE
EDDSDLESSE SGLEPGEIPA VTKGERNGLK IPSFCSQRGE SETKTSKSWR HPLSKPPARS
PMTLVKQQAA SDEELPEVPL VEEEVQETES WAKPLVYLWQ TKAPNFVAEQ EYNAAVAKLE
PYCAICTLLM PYYKPDNSNE ENYCRWETKS SEVTSALEKT KPLIPEMCFI YSEENTEHSP
SNAFIEEDGT SLLISCAKCC VQVHASCYGV PSQDIRDGWL CSRCKRSAWT AECCLCNLRG
GALKQTKNKK WAHVMCAVAI PEVRFVNVTE RTPIDISRIP LQRLKLKCIF CRQRVKKVSG
ACIQCSYGRC PASFHVTCAH ATGVLMEPDD WPYVVNITCF RHKINQNVRS KACEKAITVG
QTVISKHRNT RYYSCRVIEV TSQTFYEVVF DDGSFSRDTF PEDIVSRDCL KLGPPAEGEV
VQVKWPDGKL YGAKYLGTNV AHMYQVEFED GSQIAMKRED IYTLDEELPK RVKARFSTAS
DMRFEDTFYG ADIIQGEKKR QRMLSSRFKN EYVDDPVYRT FLKSSFQKKC QKGL
//
