ID A0A3Q7T8S2_VULVU Unreviewed; 1187 AA.
AC A0A3Q7T8S2;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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_025857152.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025857152.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025857152.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025857152.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025857152.1};
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_025857152.1; XM_026001367.1.
DR AlphaFoldDB; A0A3Q7T8S2; -.
DR STRING; 9627.ENSVVUP00000028122; -.
DR Proteomes; UP000286640; 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); 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 150..192
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 278..444
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 883..996
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 29..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 133902 MW; B7AEB43197F82EC3 CRC64;
MHHSEPRLTE ARKTNPEARR CCASLSGVGV HVTSSAGPGG HVTARAPSRG ESRPALCARL
RRCLPTPRRE GEERRSHRAS GPLRVRGEQL SPSAEQVFQI PQISPGRRLP SSSSSSSSGP
CPRPHPRARH CLAIMEVAEV ESPLNPSCKI MTFRPSMEEF REFNKYLAFM ESKGAHRAGL
AKVIPPREWK PRQCYDDIDN LLIPAPIQQM VTGQSGLFTQ YNIQKKAMTV KEFRQLANSG
KYCTPRYLDY EDLERKYWKN LTFVAPIYGA DINGSIYDED VDEWNIARLN TVLDVVEEEC
GISIEGVNTP YLYFGMWKTT FAWHTEDMDL YSINYLHFGE PKSWYAIPPE HGKRLERLAQ
GFFPSSSQGC DAFLRHKMTL ISPSVLKKYG IPFDKITQEA GEFMITFPYG YHAGFNHGFN
CAESTNFATV RWIDYGKVAK LCTCRKDMVK ISMDIFVRKF QPDRYQLWKQ GKDIYTIDHT
KPTPESTPEV KAWLQRRRKV RKASRSFQCT GSHSKRLKNE EDEEVSPAVE GAQSLSPDTD
PDDPKVSEKP EKAVRMGNTE APSEEEASPS RKQPDQNSSD NIKLPGNNCL STSITEEIET
KDNQACGIIL PSHPSEAGDS LSSGHVTSKE PDPPKLPWPK SPESCSSVAE TNSVLTEGEE
SDVESRRSGL ELGEIPAISS GERNGLELPG RIEGETKTAK SWRHPLSKPP ARSPLTLVKQ
QAISDEELPE VPSIEEEVEE TESWAKPLVH LWQTKSPNFV AEQEYNATMA KMEPHCAICA
LLMPYYKPDS SNEENDSRWE TKLDEVVTPG GKTKPLIPEM CFIYSEENIE YSPPNAFLEE
DGTSLLISCA KCCVRVHASC YGIPSHEICD GWLCARCKRN AWTAECCLCN LRGGALKETK
NNKWAHVMCA VAVPEVRFTN VPERTQIDVG RIPLQRLKLK CIFCRHRVKK VSGACIQCSY
GRCPASFHVT CAHAAGVLME PDDWPYVVNI TCFRHKVNPN VKSKAGEKGI SVGQTVITKH
RNTRYYSCRV IAVTSQTFYE VVFDDGSFSR DTFPEDIVSR DCVKLGPPTE GEVVQVKWPD
GKLYGAKYLG SNVAHMYQVE FEDGSQIAMK REDIYTLDEE LPKRVKARFS TASDMRFEDT
FYGADIIQGE KKRQRMLSSR FKNEYVDDPV YRTFLKSSFQ KKCQKRQ
//
