ID I3M7L2_ICTTR Unreviewed; 1050 AA.
AC I3M7L2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 72.
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:ENSSTOP00000005614.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000005614.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000005614.3}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AGTP01051289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01051298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005328029.1; XM_005327972.2.
DR AlphaFoldDB; I3M7L2; -.
DR STRING; 43179.ENSSTOP00000005614; -.
DR Ensembl; ENSSTOT00000006279.3; ENSSTOP00000005614.3; ENSSTOG00000006263.3.
DR GeneID; 101957049; -.
DR CTD; 23081; -.
DR eggNOG; KOG0958; Eukaryota.
DR GeneTree; ENSGT00940000154930; -.
DR HOGENOM; CLU_001442_0_0_1; -.
DR InParanoid; I3M7L2; -.
DR OrthoDB; 48111at2759; -.
DR TreeFam; TF106449; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
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:0001825; P:blastocyst formation; 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 GO; GO:2000736; P:regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
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 746..859
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 370..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1050 AA; 119572 MW; 50EA8B6C14942905 CRC64;
MEVVEADSPL 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 RSFQCTRSHS KRPKAEEDEE VPADVDEAED PNHDIGIEDL KVREKPEAAA
KLGNTEAPSE DRVQMDQHFS DNINVSGNSC SSTPVMEKIK TECAKAGATI IPALPKEAND
SIPLYTGHEE VEESDPPKLP WPKSPESTSS VTESYGVFTE GEESDMEGLR SGLEPGEIPA
VLSEERNGFK VPSIMEAETK TAKSWRHPLS KPPARSPMTL VKQQATSDEE LPEVPSVEEE
VEETESWAKP LIHLWQTKSP NFVAEQEYNA AAAKMEPHCA ICTLLMPYYK PDSSNEENDS
RWEIKLDEVV ASGGKTKPLI PEMCFIYSEE NIEYSPPNAF LEEDGTSLLI SCAKCCVRVH
ASCYGVPSHE ICAGWLCARC KRNAWTAECC LCNLRGGALK QTKNNKWAHV MCAVAVPEVR
FTNVPERTQI DVGRIPLQRL KLKCIFCRHR VKKVSGACIQ CSYGRCPASF HVTCAHAAGV
LMEPDDWPYV VNITCFRHKV NPNVKSKAFE KAISVGQTVI TKHRNTRYYS CRVMAVTSQT
FYEVMFDDGS FSRDTFPEDI VSRDCLKLGP PAEGEVVQVK WPDGKLYGAK YLGSNVAYMY
QVEFEDGSQI AMKREDIYTL DEELPKRVKA RYSTASDMRF EDTFYGTDII QGERKRQRVL
SSRFKNEYVD DPVYRTFLKS SFQKKCQKRQ
//
