ID A0A3P9AL39_ESOLU Unreviewed; 1424 AA.
AC A0A3P9AL39;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525};
DE EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000041773.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000041773.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000041773.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR STRING; 8010.ENSELUP00000041773; -.
DR Ensembl; ENSELUT00000035239.2; ENSELUP00000041773.2; ENSELUG00000022870.2.
DR GeneTree; ENSGT00940000166518; -.
DR Proteomes; UP000265140; LG22.
DR Bgee; ENSELUG00000022870; Expressed in spleen and 15 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; 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; PF13431; TPR_17; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 4.
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:UP000265140};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 98..131
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 135..168
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 289..322
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 323..356
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1123..1286
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 20..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..573
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..965
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1424 AA; 154512 MW; 5EA6052093BB6196 CRC64;
MQSCGVSLAV AACAAARSLG SASGGDEEKK MAAGKASETE EDFPTLTAQE RDSLVGIDSS
LFGFQRLHED GARTKALLLK AVRCYDSLIL KAEGKVEPEL FCQLGHFNLL LEEYAKALSA
YQRYYSLQSD YWKNAAFLYG LGMVYFHYNA FQWAIKAFQE VLYIDPSFSR AKEIHLRLGL
MFKVNTDYES SLKHFQLALI DSNPCTLSKA EIQFHIAHLY EIQKRYRAAK EAYESLLKTE
NLPAQVKATT LQQLGWMHHT VEQLGDRANK DSYAIQCLQK SLEADPNSGQ SWYYLGRCYS
SIGKVQDAFI SYRQSIDKSE ASADTWCSIG VLYQQQNQPM DALQAYICAV QLDHGHAAAW
MDLGTLYESC SQPHDAVKCY INATRSKSCT NAAALTQRIK CLQACKPQHG LEGGGSGPAL
PPHVGPVGPG EDQSSPAKRR RASSPAKSQT DPWASNSAQQ PVPNWYLSPQ KLQVSAANVT
HTPPPCVLGP PHVNHPIRAT HPRLLPVCAQ LLDQLRSNRA SLKPPQLQML EQLEAQLNLM
QQHQQQMRQL RPTLPNGPLG TNSLPPPHPS LPTSRPHVAS QGSSRPPCPP QPLANGPLAA
GAPHGHSDAL SVGNNDSNNH PAAAPGPNGP NGDVPYLQPG ALLPHTCTST QSQDTARRAL
HLNATQGLLM GSAPHWAGPN GDGPLPSSGG STHPLSHPQT PHNQVGHSTA PAGAPSPRQP
ALNHLPSPPA PPPQSATSGG APGHAPATKE SMPLGNGPTA AATEGPGGAS TTANSTATVA
EGLSNHVQPA PAGEDGHSSD NPKGVDPAPS APHKTVNNVH PAVSSAASSP ISAMSTATPS
PKSTEPGQST GMHGLNSPSI TTASSSAGPT TVLNGNGKGG ISEDSQSPLK ADPPATCRRP
TPPHARTPSS SSSSSVSIYP SSTDVLKACR NLGKNGLSSS SILLDKCPPP RLPPPPSPAL
PKDKLNPPTP SIYLENKRDA FFPPLHQFCT NPSNPVTVIR GLAGALKLDL GLFSTKTLVE
ANPDHLVEVR TQLAQPADEN WDLSGTKKMW RCESGRAHTT IAKYAQYQAA SFQESLREEN
EKKALKEPSD TEPASADGVA RKRRGPLKHI KFGTNIDVSD ERKWKLQLQE LSKLPAFSRV
VSAGNLLSHV GHTILGMNTV QLYMKVPGSR IAGHQEHNNF CSVNINIGPG DCEWFAVPEP
YWGVMSNFCE KNNINFLMGS WWPNLEDLYE ADVPVYRFIQ RPGDLVWLNT GTVHWVQAIG
WCNNIAWNVG PLTAHQYKLA VERYEWNKLQ SVKSHVPMVH LSWNMARNIK VSDHKLFEMI
KYCLLRTLKQ CQSVKEALVA AGKETVLQPR NRDEPAHYCT ICEVEVFNLL FVRSELFSRK
QKPYVVHCQD CARKGSAELE NFVVIEQHRM EDLMQVYDQF TLVS
//
