ID A0A2R8NEK6_CALJA Unreviewed; 1337 AA.
AC A0A2R8NEK6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
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=UTY {ECO:0000313|Ensembl:ENSCJAP00000066584.3};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000066584.3, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000066584.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000066584.3}
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(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 Ensembl; ENSCJAT00000080958.3; ENSCJAP00000066584.3; ENSCJAG00000074089.1.
DR GeneTree; ENSGT00940000155202; -.
DR Proteomes; UP000008225; Chromosome Y.
DR Bgee; ENSCJAG00000010889; Expressed in cerebellum and 6 other cell types or tissues.
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:SF25; HISTONE DEMETHYLASE UTY; 1.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 5.
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:UP000008225};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 90..123
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 127..160
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1028..1191
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 407..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1337 AA; 148655 MW; 02BC6BB046DEC62B CRC64;
MNSCGVSLTT AVLAFGDEAK KMAAGKASGD SQEESFTLTL EERQALGGMD SRLFGFVRLH
EDGARSKTLL GKAIRCYESL ILKAEGKVDS NLFCQLGHFN LLLEDYSKAL SAYQRYYSLQ
DDYWKNAAFL YGLGLVYFYY NAFHWAIKAF QDVLYIDPSF CRAKEIHLRL GLMFKVNTDY
RSSLKHFQLA LIDCNPCTLS SAESKKYHSA KEAYEQLLQT ENLPAQVKAT VLQQLGWMHH
NMDLVGDKAT KESYAIQYLQ KSLEADPNSG QSWYFLGRCY SSIGKVQDAF ISYRQSIDKS
EASYVYKHTY ICAVQLDHGH AAAWMDLGTL YESCNQPQDA IKCYLNATRS KHCSNTSTLA
ARIKFLQAYK PHDPNTEPVL NHSQTPILQQ PLSLHMITPS QVEGLSCPAK KTRTSSQTKN
VSDNWNSGQS VSHHPELQQL YSLCLTPQKL QHQLEQLESQ FALADSSLST NSISNRQPHA
ALTQVSSVSQ PEVHPACTEK SLFSGAFSAG CIPCGTLKIL GSIDTILVGS NCIAGSESNG
NVPYLQQNTF ILPHNHTDLN SSTEGPWRKQ LSNPAQGLHK SQSSCLSGTT EEQLLFSTGC
AQYHQATSTG FKKQNEHLTL CSNSGPQKVA DSHLPSHIAT SNGQQGIIFT KESKPSKHRS
LVPETSRHTG DTSNGSADVN GLSNHVHHTI ADVVSGPNHG VSPNLLISDN PQLSALLIGK
ASDSMGTGTC DKVNNIRPTV HTKTDNSVVS LPSSAISTAT SSPKSTEQTS TNSVTSLNSS
HSGLHTVNGE GLENSQSSTK IDLPLVSHRS ACQIIPSMSV SICPSSAEVL KACRNLGKNG
LFNSCISLDK CPPPRPPTSP YPPLPKDKLN PPTPSIYLEN KRDAFFPPLH QFCTNPKNPV
TVIRGLAGAL KLDLGLFSTK TLVEANNEHM VEVRTQLLQP SDENWDPTGT KKIWRCESNR
SHTTIAKYAQ YQASSFQESL REENEKRTQH KDHSDNESTT SENSGRRKKG PFKTIKFGTN
IDLSDNKKWK LQLHELTKLP AFVRVVSAGN LLSHVGHTIL GMNTVQLYMK VPGSRTPGHQ
ENNNFCSVNI NIGPGDCEWF VVPEDYWGVL NDFCEKNNLN FLMSSWWPNL EDLYEANVPV
YRFIQRPGDL VWINAGTVHW VQAVGWCNNI AWNVGPLTAC QYKLAVERYE WNKFQSVKSL
VPMVHLSWNM ARNIKVSDPK LFEMIKYCLL KILKQCQTLR EALIAAGKDV IWHGRTNDEP
AHYCSICEVE VFNLLFVTIE SNTQKTYIVH CQDCARKTSR SLENFVVLEQ YKMEDLIQVY
DQFKLGSDRY VSTLRGV
//
