ID A0A340XDB3_LIPVE Unreviewed; 1324 AA.
AC A0A340XDB3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525};
DE EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525};
GN Name=KDM6A {ECO:0000313|RefSeq:XP_007457025.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007457025.1};
RN [1] {ECO:0000313|RefSeq:XP_007457025.1}
RP IDENTIFICATION.
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(27)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, 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=1.14.11.68; Evidence={ECO:0000256|ARBA:ARBA00034421};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR RefSeq; XP_007457025.1; XM_007456963.1.
DR GeneID; 103073128; -.
DR CTD; 7403; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1370; -; 2.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR046941; KDM6_GATAL_sf.
DR InterPro; IPR048562; KDM6A_B-like_C-hel.
DR InterPro; IPR048560; KDM6A_B-like_GATAL.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR14017:SF9; LYSINE-SPECIFIC DEMETHYLASE 6A; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 132..165
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 320..353
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1018..1181
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 443..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..860
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 145417 MW; 094D93AF850877C8 CRC64;
MKSCGVSLAT AAAAAAAAAF GDEEKKMAAG KASGESEEAS PSLTAEEREA LGGLDSRLFG
FVRFHEDGAR TKALLGKAVR CYESLILKAE GKVESDFFCQ LGHFNLLLED YPKALSAYQR
YYSLQSDYWK NAAFLYGLGL VYFHYNAFQW AIKAFQEVLY VDPSFCRAKE IHLRLGLMFK
VNTDYESSLK HFQLALVDCN PCTLSNAEIQ FHIAHLYETQ RKYHSAKEAY EQLLQTENLS
AHVKATVLQQ LGWMHHTVDL LGDKATKESY AIQYLQKSLE ADPNSGQSWY FLGRCYSSIG
KVQDAFISYR QSIDKSEASA DTWCSIGVLY QQQNQPMDAL QAYICAVQLD HGHAAAWMDL
GTLYESCNQP QDAIKCYLNA TRSKSCSNTS ALAARIKYLQ NTSDNWSSGH AVSHPPVQQQ
GHSWCLTPQK LQMRQTGVAQ VRSTGIPNGP TADSSLPTNS VSGQQPQLAL TRVPSVSQPG
VRPACPGQPL ANGPFSAGHV PCSTSRTLGS TDTILIGNNH ITGSGSNGNV PYLQRNALTL
PHNRTNLTSS AEEPWKNQLS NSTQGLHKGQ SSHLAGPNGE RPLSSTGPSQ HLQAAGSGVQ
NQNGHPTLPS NSVTQGAALN HLSSHTATSG GQQGITLTKE SKPSGNTSMV PEISRHAGET
PDSTASVEGL PNHVHQVTAD AVCSPSHGDS KSPGLLSSDN PQLSALLMGK ANNNVGTGTC
DKVNNIHPAV HTKTDNSVAS SPSSAISTAT PSPKSTEQTT TNSVTSLNSP HSGLHTINGE
GMEESQSPMK TDLLLISHKP SPQIIPSMSV SIYPSSAEVL KACRNLGKNG LSNSSILLDK
CPPPRPPSSP YPPLPKDKLN PPTPSIYLEN KRDAFFPPLH QFCTNPNNPV TVIRGLAGAL
KLDLGLFSTK TLVEANNEHM VEVRTQLLQP ADENWDPTGT KKIWHCESNR SHTTIAKYAQ
YQASSFQESL REENEKRSHH KDHSDNESTS SDNSGRRRKG PFKTIKFGTN IDLSDDKKWK
LQLHELTKLP AFVRVVSAGN LLSHVGHTIL GMNTVQLYMR VPGSRTPGHQ ENNNFCSVNI
NIGPGDCEWF VVPEGYWGVL NDFCEKNNLN FLMGSWWPNL EDLYEANVPV YRFIQRPGDL
VWINAGTVHW VQAIGWCNNI AWNVGPLTAC QYKLAVERYE WNKLQSVKSI VPMVHLSWNM
ARNIKVSDPK LFEMIKYCLL RTLKQCQTLR EALIAAGKEI IWHGRTKEEP AHYCSICEVE
VFDLLFVTNE SNSQKTYIVH CQDCARKTSG NLENFVVLEQ YKMEDLMQVY DQFTLAPPLP
SSSS
//
