ID W5NQR5_SHEEP Unreviewed; 1071 AA.
AC W5NQR5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=KDM4A {ECO:0000313|Ensembl:ENSOARP00000000505.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000000505.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000000505.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000000505.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000000505.1}
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; AMGL01001121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5NQR5; -.
DR SMR; W5NQR5; -.
DR STRING; 9940.ENSOARP00000000505; -.
DR PaxDb; 9940-ENSOARP00000000505; -.
DR Ensembl; ENSOART00000000533.1; ENSOARP00000000505.1; ENSOARG00000000493.1.
DR eggNOG; KOG0958; Eukaryota.
DR HOGENOM; CLU_001442_0_1_1; -.
DR OMA; SGQYDMT; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000000493; Expressed in gastric lymph node and 53 other cell types or tissues.
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; cd15713; ePHD_JMJD2A; 1.
DR CDD; cd15575; PHD_JMJD2A; 1.
DR CDD; cd20463; Tudor_JMJD2A_rpt1; 1.
DR CDD; cd20466; Tudor_JMJD2A_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; IPR047482; JMJD2A_ePHD.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4-like_Tudor.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR047479; Tudor_KDM4A_rpt1.
DR InterPro; IPR047481; Tudor_KDM4A_rpt2.
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:SF119; LYSINE-SPECIFIC DEMETHYLASE 4A; 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:UP000002356};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 14..56
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 142..312
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 779..892
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 365..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1071 AA; 121129 MW; C009087814DD5079 CRC64;
MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP KEWKPRASYD
DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI ANSDKYCTPR YSEFEELERK
YWKNLTFNPP IYGADVNGTL YEKHVDEWNI GRLRTILDLV EKESGITIEG VNTPYLYFGM
WKTSFAWHTE DMDLYSINYL HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH
KMTLISPLML KKYGIPFDKV SGLRTQQSLA YTETPLSGYH AGFNHGFNCA ESTNFATRRW
IEYGKQAVLC SCRKDMVKIS MDVFVRKFQP ERYKLWKAGK DSTIIDHTLP TPEAAEFLKE
SELVPRAQKE EDCPEEETEG LEDGEEGDLR RSLAKHRIGT KRHRVCLEIP QEVSQSELFP
KEELGSGQYD MAECQAALAP VRPTHSSVRQ VEDGLTFPDY SDSTEVKFEE LKNVKLEEED
EDEEEEHESA ALDLSVNPAS LGGRLVFSGS KKKSSSSLGS GSSQDSVSSD SETSEPLSCR
AQGQTGVLTV HSYAKGDGRV PSGEPCARKK GGATRSISER ELAEVADEYM FSLEESKKSK
GRRQPLSKLP RHHPLVLQDC VSDDELPEQL TPEEEAEETE AWAKPLSQLW QNRPPNFEAE
KEFNEAMAQQ APHCAVCMIF QTYHQVEFGG FGQSCGSAPD LAPQIERTKP LIPEMCFTST
GCTSTDINLS TPYLEEDGTS LLVSCKKCSV RVHASCYGVP PAKASEDWMC SRCSANALEE
DCCLCSLRGG ALQRANDDRW VHVSCAVAIL EARFVNIAER SPVDVSKIPL PRFKLKCVFC
KKRRKRTAGC CVQCSHGRCP TAFHVSCAQA AGVMMQPDDW PFVVFITCFR HKIPNLERAK
GALQSITAGQ KVISKHKNGR FYQCEVVRLT TETFYEVNFD DGSFSDNLYP EDIVSQDCLQ
LGPPAEGEVV QVRWTDGQVY GAKFVASHPI QMYQVEFEDG SQLVVKRDDV YTLDEELPKR
VKSRLSVASD MRFNEIFTEK EVKQEKKRQR VINSRYREDY IEPALYRAIM E
//
