ID A0A3Q7RFI7_VULVU Unreviewed; 1516 AA.
AC A0A3Q7RFI7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase {ECO:0000256|ARBA:ARBA00012902};
DE EC=1.14.11.67 {ECO:0000256|ARBA:ARBA00012902};
GN Name=LOC112911964 {ECO:0000313|RefSeq:XP_025844457.1};
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_025844457.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025844457.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025844457.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025844457.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000256|ARBA:ARBA00000604};
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 JARID1 histone demethylase family.
CC {ECO:0000256|ARBA:ARBA00006801}.
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DR RefSeq; XP_025844457.1; XM_025988672.1.
DR KEGG; vvp:112911964; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16875; ARID_KDM5C_5D; 1.
DR CDD; cd15604; PHD1_KDM5C_5D; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 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; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF141; LYSINE-SPECIFIC DEMETHYLASE 5D; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 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:UP000286640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 14..55
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 79..169
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 324..374
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 468..635
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 185..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1516 AA; 172497 MW; EF34D09898EA5202 CRC64;
MESGSDDFLP PPECPVFEPT WAEFRDPLDY IAKIRPIAEK SGICKIRPPA DWQPPFAVEV
DNFRFTPRIQ RLNELEAQTR VKLNYLDQIA KFWEIQGSSL KIPNVERRIL DLYSLSKIVM
EEGGYEAICK DRRWARVAQR LNYPAGKNIG SLLRSHYERI IYPYEMFQSG ANLVQCNTYP
FDNEEKDKEY KPHGIPLRQS VQPSTFSSYS RRAKRLQPDP EPTEEDIEKN PELKKLQIYG
AGPKMMGLGL MAKDKTLRKK DLFLTALDKE GVLCPRAVLM KEEPREDERV MSSLPREDLS
HSVEPCTKMT MQLRTHSSAQ FIDLYVCRIC SRGDEDDKLL LCDGCDDTYH IFCLIPPLPE
IPRGVWRCPK CIMAECKRPP EAFGFEQATQ EYTLQSFGEM ADSFKADYFS MPVHMVPTEL
VEKEFWRLVS SIEEDVTVEY GADIHSKEFG SGFPVSSSQG ILSPEEEEYA TSGWNLNVMP
VLDQSVLCHI NADISGMKVP WLYVGMVFSA FCWHIEDHWS YSINYLHCRG EPKTWYGVPS
LAAEQLEEVM KRLTPELFDS QPDLLHQLVT LMNPNTLMSH GVPVVRTNQC AGEFVITFPR
AYHSGFNQGY NFAEAVNFCT ADWLPAGRQC IEHYRRLRRY CVFSHEELIC KMAAFPEKLD
LNLAVAVHKE MFIMVQEERR LRKALLEKYM WVEHPQGITE AEREAFELLP DDERQCIKCK
TTCFLSALAC YDCPDGLVCL SHINDLCKCS SSRQYLRYRY TLDELPAMLH KLKIRAESFD
TWANKVRVAL EVEDGRKRSF EELRALESEA RERRFPNSEL LQRLRNCIHE AEACVSQVLG
LVSGQEARIQ TSPLTLTELR VLLEQMGSLP CAMHQIEDVK EVLEQVEAYQ IEAREAMASL
CPSVGLMRSL LEKGQQLGVD VPEAHQLQQQ VEQARWLDDV KKALAPSAQR GSLVIMQGLL
VTGTKIASSP CVDKARAELQ ELLTIAERWE EKAHFCLEAR QKHPPATLEA IIREAENIPV
HLPNIQALKD ALAKAQAWIA DVDEIQNGDH YPCLDDLECL VAVGRDLPVS LEELRQLELQ
VLTAHSWREK ASRMFLKKNS CYTLLEVLCP CAHAGSDSSK RRRWIEKELH LYRSCTDTEL
LGLSAQDLRD PGSVIVAFKE GEQKEKEGIL QLRRTNSAKP SPLASSTTAS SATSICVCGK
VPDGVGTLQC DLCQDWFHGQ CVSVPRILSS SRPSPTSSPL LAWWEWDTKF LCPLCMRSRR
PRLETILALL VALQRLPVRL PEGEALQCLT ERAIVWQGRA RQVLASKDVT TLLGQLAELR
HQLQAETRLQ EPYHSTLACA ALREGSGRDM PKQVPGLLPN VDSTSSHEKI ANVQGSDLEV
LSSLLSQLSG PVLDLPEATR VPLEELMLEG DLLEVTLDEN HRIWQLLQAG QPPDLERIRT
LLELEKPEHK GSRTRGRALE KQRRRQQQEV DLGMKSKNLV QEELQSKKAR NSGSKSEEGQ
EKKKSLKRKE IVKIFS
//
