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Database: UniProt
Entry: K7C5J0_PANTR
LinkDB: K7C5J0_PANTR
Original site: K7C5J0_PANTR 
ID   K7C5J0_PANTR            Unreviewed;      1397 AA.
AC   K7C5J0;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
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|EMBL:JAA19515.1};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|EMBL:JAA19515.1};
RN   [1] {ECO:0000313|EMBL:JAA19515.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Smooth vascular {ECO:0000313|EMBL:JAA19515.1};
RA   Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT   "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT   mRNA sequences.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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   EMBL; GABF01002630; JAA19515.1; -; mRNA.
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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; 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; 3.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS50005; TPR; 3.
PE   2: Evidence at transcript level;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methyltransferase {ECO:0000313|EMBL:JAA19515.1};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW   Transferase {ECO:0000313|EMBL:JAA19515.1}.
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   REPEAT          315..348
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          1092..1255
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          434..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          621..743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          755..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          807..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        807..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        914..934
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1073
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1397 AA;  154238 MW;  5073DFB56EE2EF4A CRC64;
     MKSCGVSLTT AAVAFGDEAK KMAAGKASRE GEEEPLSLTV EEREALGDMD SRLFGFVRLH
     EDGARTKTLL GKAVRCYESL ILKAEGKVES DFFCQLGHFN LLLEDYSKAL SAYQRYYSLQ
     ADYWKNAAFL YGLGLVYFYY NAFHWAIKAF QDVLYVDPSF CRAKEIHLRL GLMFKVNTDY
     ESSLKHFQLA LVDCNPCTLS NAEIQFHIAH LYETQRKYHS AKEAYEQLLQ TENLSAQVKA
     TVLQQLGWMH HTVDLLGDKA TKESYAIQYL QKSLEADPNS GQSWYFLGRC YSSIGKVQDA
     FISYRQSIDK SEASADTWCS IGVLYQQQNQ PMDALQAYIC AVQLDHGHAA AWMDLGTLYE
     SCNQPQDAIK CYLNAARSKR CSNTSTLAAR IKFLQAQLCN LPQSSLQNKT KLLPSIEEAW
     SLPIPAELTS RQGAMNTAQQ NTSDNWSGGH AVSHPPVQQQ AHSWCLTPQK LQHLEQLRAN
     RNNLNPAQKL MLEQLESQFV LMQQHQMRPT GVAQVRSTGI PNGPTADSSL PTNSVSGQQP
     QLALTRVPSV SQPGVRPACP GQPLANGPFS AGHVPCSTSR TLGSTDTILI GNNHITGSGS
     NGNVPYLQRN ALTLPHNRTN LTSSAEEPWK NQLSNSTQGL HKGQSSHSAG PNGERPLSST
     GPSQHLQAAG SGIQNQNGHP TLPSNSVTQG AALNHLSSHT ATSGGQQGIT LTKESKPSGN
     ILTVPETSRH TGETPNSTAS VEGLPNHVHQ MTADAVCSPS HGDSKSPGLL SSDNPQLSAL
     LMGKANNNVG TGTCDKVNNI HPAVHTKTDN SVASSPSSAI STATPSPKST EQTTTNSVTS
     LNSPHSGLHT INGEGMEESQ SPMKTDLLLV NHKPSPQIIP SMSVSIYPSS AEVLKACRNL
     GKNGLSNSSI LLDKCPPPRP PSSPYPPLPK DKLNPPTPSI YLENKRDAFF PPLHQFCTNP
     KNPVTVIRGL AGALKLDLGL FSTKTLVEAN NEHIVEVRTQ LLQPADENWD PTGTKKIWHC
     ESNRSHTTIA KYAQYQASSF QESLREENEK RSHHKDHSDS ESTSSDNSGR RRKGPFKTIK
     FGTNIDLSDD KKWKLQLHEL TKLPAFVRVV SAGNLLSHVG HTILGMNTVQ LYMKVPGSRT
     PGHQENNNFC SVNINIGPGD CEWFVVPEGY WGVLNDFCEK NNLNFLMGSW WPNLEDLYEA
     NVPVYRFIQR PGDLVWINAG TVHWVQAVGW CNNIAWNVGP LTACQYKLAV ERYEWNKLQS
     VKSIVPMVHL SWNMARNIKV SDPKLFEMIK YCLLRTLKQC QTLREALIAA GKEIIWHGRT
     KEEPAHYCSI CEVEVFDLLF VTNESNSRKT YIVHCQDCAR KTSRSLENFV VLEQYKIEDL
     IQVYDQFTLA LSLSSSS
//
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