ID A0A2Y9SV33_PHYMC Unreviewed; 1146 AA.
AC A0A2Y9SV33;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 2.
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_023982526.2};
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_023982526.2};
RN [1] {ECO:0000313|RefSeq:XP_023982526.2}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023982526.2};
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_023982526.2; XM_024126758.2.
DR AlphaFoldDB; A0A2Y9SV33; -.
DR STRING; 9755.ENSPCTP00005009655; -.
DR KEGG; pcad:102986762; -.
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 237..403
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 842..955
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 462..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1146 AA; 129439 MW; 5C248344A35D7ECD CRC64;
MARAPSRRES RLALCARLCR CLPAPRREGE ERRSHRATGA GCACAANSCH PVRNKSPKFP
ESPWAGGHRL PSHLPLLGRV LSPARAPETA PAIMEVAKVE SPLNPSCKIM TFRPCMEEFR
EFNKYLAYME SKGAHRAGLA KVIPPKEWKP RQCYDDIDNL LIPAPIQQMV TGQSGLFTQY
NIQKKAMTVK EFRQLANSGK YCTPRYLDYE DLERKYWKNL TFVAPIYGAD INGSIYDEGV
DEWNIAHLNT VLDVVEEECG ISIEGVNTPY LYFGMWKTTF AWHTEDMDLY SINYLHFGEP
KSWYAIPPEH GKRLERLAQG FFPSSSQGCD AFLRHKMTLI SPSVLKKYGI PFDKITQEAG
EFMITFPYGY HAGFNHGFNC AESTNFATVR WIDYGKVAKL CTCRKDMVKI SMDIFVRKFQ
PDRYQLWKQG KDIYTIDHTK PTPESTPEVK AWLQRRRKVR KASRSFQCTS SHSKRPKNEE
DEEVSAAVDG AEGPTPDPDP DELKDSEKPE EAVKLANTEA PSEEEASASR MQQDHNLSDN
IRFAGNVCLS TSVAEKIKTE ADQTCATIPP SNPSDADDSM SSGHVMSKES EPPKLPWPKS
PESCFSVVES NSGLTEGEES DVESHGVGLE PGEVPEVPSG ERNGFKVPSR IEGETKTAKS
WRHPLSKPPA RSPMTLVKQQ ATSDEELPEV PSIEEEVEET ESWAKPLVHL WQTKSPNFVA
EQEYNAAMGR MEPHCAVCAL LMPYYKPDSS NEENDSRWET KLDEVVTSGG KTKPLIPEMC
FIYSEENIEY SPPNAFLEED GTSLLISCAK CRVRVHASCY GIPSHEICDG WLCARCKRNA
WTAECCLCNL RGGALKETKN NKWAHVMCAV AVPEVRFTNV PERTQIDVGR IPLQRLKLKC
MFCRHRVKKV SGACIQCSYG RCPASFHVTC AHAAGVLMEP DDWPYVVNIT CFRHKVNPNV
KSKAGEKGIA VGQTVITKHR NTRYYSCRVI AVTAQTFYEV VFDDGSFSRD TFPEDIVSRD
CVRLGPPAEG EVVQVKWPDG KLYGAKYLGS NVAHMYQVEF EDGSQIAMKR EDIYTLDEEL
PKRVKARFST ASDMRFEDTF YGTDIIQGEK KRQRVLSSRF KNEYVDDPVY RTFLKSSFQK
KCQKRQ
//
