ID A0A455BM06_PHYMC Unreviewed; 1179 AA.
AC A0A455BM06;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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_028349777.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028349777.1};
RN [1] {ECO:0000313|RefSeq:XP_028349777.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028349777.1};
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_028349777.1; XM_028493976.1.
DR AlphaFoldDB; A0A455BM06; -.
DR InParanoid; A0A455BM06; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000248484; Chromosome 9.
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:UP000248484};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 109..151
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 270..436
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 875..988
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 495..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1179 AA; 133220 MW; 0181E0C3A3F46D4D CRC64;
MARAPSRRES RLALCARLCR CLPAPRREGE ERRSHRATGA GCACAANSCH PVRNKSPKFP
ESPWAGGHRL PSHLPLLGRV LSPARAPETA PAIMEVAKVE SPLNPSCKIM TFRPCMEEFR
EFNKYLAYME SKGAHRAGLA KVIPPKEWKP RQCYDDIDNL LIPAPIQQMV TGQSGLFTQY
NIQKKAMTVK EFRQLANSGK YCTPRYLDYE DLERKYWKNL TFVAPIYGAD INGSIYDEQK
KLSFNIMATL ALPRRNCCRH IICPLMGRIS IGVDEWNIAH LNTVLDVVEE ECGISIEGVN
TPYLYFGMWK TTFAWHTEDM DLYSINYLHF GEPKSWYAIP PEHGKRLERL AQGFFPSSSQ
GCDAFLRHKM TLISPSVLKK YGIPFDKITQ EAGEFMITFP YGYHAGFNHG FNCAESTNFA
TVRWIDYGKV AKLCTCRKDM VKISMDIFVR KFQPDRYQLW KQGKDIYTID HTKPTPESTP
EVKAWLQRRR KVRKASRSFQ CTSSHSKRPK NEEDEEVSAA VDGAEGPTPD PDPDELKDSE
KPEEAVKLAN TEAPSEEEAS ASRMQQDHNL SDNIRFAGNV CLSTSVAEKI KTEADQTCAT
IPPSNPSDAD DSMSSGHVMS KESEPPKLPW PKSPESCFSV VESNSGLTEG EESDVESHGV
GLEPGEVPEV PSGERNGFKV PSRIEGETKT AKSWRHPLSK PPARSPMTLV KQQATSDEEL
PEVPSIEEEV EETESWAKPL VHLWQTKSPN FVAEQEYNAA MGRMEPHCAV CALLMPYYKP
DSSNEENDSR WETKLDEVVT SGGKTKPLIP EMCFIYSEEN IEYSPPNAFL EEDGTSLLIS
CAKCRVRVHA SCYGIPSHEI CDGWLCARCK RNAWTAECCL CNLRGGALKE TKNNKWAHVM
CAVAVPEVRF TNVPERTQID VGRIPLQRLK LKCMFCRHRV KKVSGACIQC SYGRCPASFH
VTCAHAAGVL MEPDDWPYVV NITCFRHKVN PNVKSKAGEK GIAVGQTVIT KHRNTRYYSC
RVIAVTAQTF YEVVFDDGSF SRDTFPEDIV SRDCVRLGPP AEGEVVQVKW PDGKLYGAKY
LGSNVAHMYQ VEFEDGSQIA MKREDIYTLD EELPKRVKAR FSTASDMRFE DTFYGTDIIQ
GEKKRQRVLS SRFKNEYVDD PVYRTFLKSS FQKKCQKRQ
//
