ID A0A7J7YGG3_MYOMY Unreviewed; 1374 AA.
AC A0A7J7YGG3;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
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 ORFNames=mMyoMyo1_020305 {ECO:0000313|EMBL:KAF6360898.1};
OS Myotis myotis (Greater mouse-eared bat) (Vespertilio myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6360898.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6360898.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6360898.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6360898.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 2-
CC oxoglutarate + 2 O2 = N(6)-methyl-L-lysyl(27)-[histone H3] + 2
CC formaldehyde + 2 succinate + 2 CO2; Xref=Rhea:RHEA:60224, Rhea:RHEA-
CC 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:ARBA00048695};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6360898.1}.
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DR EMBL; JABWUV010000004; KAF6360898.1; -; Genomic_DNA.
DR VEuPathDB; HostDB:GeneID_118653897; -.
DR Proteomes; UP000527355; Unassembled WGS sequence.
DR GO; GO:0044666; C:MLL3/4 complex; IEA:TreeGrafter.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:TreeGrafter.
DR GO; GO:0071558; F:histone H3K27me2/H3K27me3 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:TreeGrafter.
DR GO; GO:0007507; P:heart development; IEA:TreeGrafter.
DR GO; GO:0010468; P:regulation of gene expression; IEA:TreeGrafter.
DR FunFam; 1.25.40.10:FF:000022; lysine-specific demethylase 6A isoform X1; 1.
DR FunFam; 1.20.58.1370:FF:000001; lysine-specific demethylase 6A isoform X2; 1.
DR FunFam; 2.10.110.20:FF:000001; lysine-specific demethylase 6A isoform X2; 1.
DR FunFam; 2.60.120.650:FF:000002; lysine-specific demethylase 6A isoform X2; 1.
DR FunFam; 1.25.40.10:FF:000011; lysine-specific demethylase 6A isoform X3; 1.
DR FunFam; 1.20.58.1370:FF:000002; lysine-specific demethylase 6A isoform X6; 1.
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; IPR051630; Corepressor-Demethylase.
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_rpt.
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; 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; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
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:UP000527355};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REPEAT 131..164
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 319..352
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1068..1231
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 429..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..806
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..904
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1374 AA; 150561 MW; 27449C0BA8EF199D CRC64;
MKSCGVSLAT AAAAAAAAFG DEEKKMAAGK ASGESEEASP SLTAEEREAL GGLDSRLFGF
VRFHEDGART KALLGKAVRC YESLILKAEG KVESDFFCQL GHFNLLLEDY PKALSAYQRY
YSLQSDYWKN AAFLYGLGLV YFHYNAFQWA IKAFQEVLYV DPSFCRAKEI HLRLGLMFKV
NTDYESSLKH LQLALVDCNP CTLSNAEIQF HIAHLYETQR KYHSAKEAYE QLLQTENLSA
QVKATVLQQL GWMHHTIDLL GDKAAKENCA IQYLQKSLEA DPNSGQSWYF LGRCYSSIGK
VQDAFISYRQ SIDKSEASAD TWCSIGVLYQ QQNQPMDALQ AYICAVQLDH GHAAAWMDLG
TLYESCNQPQ DAIKCYLNAT RSKSCSNTSA LAARIKYLQA CKPHHPNTEP VLGLSQTPIS
QQSLPLHTIP SSQVDGLSSP AKRKRTSSPT KNTSDNWSSG HAVSHPPVQQ PSHSWCLPPQ
KLQVRQTGVA QVRSTGIPNG PAADSSLPTN SVSGQQPPLA LTRVPSASQP GVRPACPGQP
LANGPFSAGH APCSTRMLGS TDTLLIGNNH ITGSGSNGNV PYPQRNALTL PHNRTNLTSS
AEEPWKNQLS NSTQGLHKGQ SSHLAGPNGE RPLSSTGPSQ HLQAAGSGIQ NQNGHPTLPS
NSVTQGAALN HLSSHTATSG GQQGITLTKE SKPSGNTSTV PDTSRHTGET PNSTASVEGL
PNHVHQVTAD AVCSPSHGDS KSPGLLSSDN PQLSALLMGK ANNNVGTGTC DKVNNIHPAV
HTKTDNSVAS SPSSAISTAT PSPKSTEQTT TNSVTSLNSP HSGLHTINGE GMEESQSPVK
TDLLLISHKP SPQIIPSMSV SIYPSSAEVL KACRNLGKNG LSNSSILLDK CPPPRPPSSP
YPPLPKDKLN PPTPSIYLEN KRDAFFPPLH QFCTNPNNPV TVIRGLAGAL KLDLGLFSTK
TLVEANNEHM VEVRTQLLQP ADENWDPTGT KKIWHCESNR SHTTIAKYAQ YQASSFQESL
REENEKRSHH KEHSDSESTS SDNSGRRRKG PFKTIKFGTN IDLSDDKKWK LQLHELTKLP
AFVRVVSAGN LLSHVGHTIL GMNTVQLYMK VPGSRTPGHQ ENNNFCSVNI NIGPGDCEWF
VVPEGYWGVL NDFCEKNNLN FLMGSWWPNL EDLYEANVPV YRFIQRPGDL VWINAGTVHW
VQAIGWCNNI AWNVGPLTAC QYKLAVERYE WNKLQSVKSI VPMVHLSWNM ARNIKVSDPK
LFEMIKYCLL RTLKQCQTLR EALIAAGKEI IWHGRTKEEP AHYCSICEVE VFNLLFVTNE
SISRKTYVVH CQDCARKTSR NLDNFVVLEQ YKMEDLMQVY DQFTLAPPLP SSSS
//
