ID A0A2Y9IGG3_ENHLU Unreviewed; 1083 AA.
AC A0A2Y9IGG3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=LOC111139444 {ECO:0000313|RefSeq:XP_022347416.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022347416.1};
RN [1] {ECO:0000313|RefSeq:XP_022347416.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022347416.1};
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(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=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_022347416.1; XM_022491708.1.
DR AlphaFoldDB; A0A2Y9IGG3; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 1.20.58.1370; -; 2.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR048562; KDM6A_B-like_C-hel.
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 SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 67..100
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 885..1048
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 223..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..727
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1083 AA; 118895 MW; 3122141F91DF9540 CRC64;
MHHNVDLLGD KATKESYAIQ YLQKSLEADP NSGQSWYFLG RCYSSIGKVQ DAFISYRQSI
DKSEASADTW CSIGVLYQQQ NQPMDALQAY ICAVQLDHGH AAAWMDLGTL YESCNQPQDA
IKCYLNATRS KSCNNISTLA GRIKFLQAQL CNLPQCSLQN KTKLLPSIEE AWSLPIPAEL
TSRQGAMNTT QQAYKAHHPN TEPVLGLSQI PLSQQSLPVH MITSSQVDGP SSPAKKKRTS
SPTKNSSENW NRTVSLNPVQ QQVHSWYLTP QKLQQLEQLR ANRDNLNSAQ KLMLEQLESQ
FVLMQQGQTG QTTGIPNGPV ANSSLPTNFS QQPHSSLPRE SSVSHPEVRS ACFEKPLSSG
PFTGGCAPFG TSKSLGNTDI TLVGNNYVTG SGSNGNVPYL QQNILTLPHN CTNLTSSTEE
PWRKQLSNST QGLHKDQSSH LAGPSDEQPP FSTGPAQYLQ AASTAIQKQT GLRTLPNNSV
TQGAAFNHLS SPIPTSGGQQ GITFTKEGKP SGNRSLVPET SRHVGDKPNG CAGVKGLSNH
VQQLIAEPVC SPNHGDSTSP NVQISDNPQV SALLVGKAND SGGSGACDKV SNFHPTVCTK
TNNSVASSPS SVISTATPSP KSSEHTAVHS VPSLNSPHSR LHTFNGEGLE NSQSSVKTDL
PIISQKPGPH IIPSISVSIY SSSSEVLKAC RNLGKNGLSN SHILLDKCPP PRPPTSPYPP
LPKDKLNPPT PSIYLENKRD AFFPPLHQFC TNPKNPVTVI RGLAGALKLD LGLFSTKTLV
EANNEHTVEV RTQLLQPADE NWDPTGTKKI WRCESNRSHT TIAKYAQYQA SSFQESLREE
NEKRTQHKEY SDTESISSDS SGRRRKGPFK TIKFGTNIDL SDDKKWKLQL HELTKLPAFV
RVVSAGNLLS HLGHTILGMN TVQLYMKVPG SRTPGHQENN NFCSVNINIG PGDCEWFVVP
EDYWGVLNDF CEKNNLNFLM SSWWPNLEDL YEANVPVYRF IQRPGDLVWI NAGTVHWVQA
VGWCNNIAWN VGPLTACQYK LAVERYEWNR LQSVKSVVPM VHLSWNMARN IKVSDPKLFE
MIK
//
