ID A0A1S3MWW1_SALSA Unreviewed; 1442 AA.
AC A0A1S3MWW1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=LOC106575616 {ECO:0000313|RefSeq:XP_014007703.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014007703.1};
RN [1] {ECO:0000313|RefSeq:XP_014007703.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014007703.1};
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=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 RefSeq; XP_014007703.1; XM_014152228.1.
DR Ensembl; ENSSSAT00000134505; ENSSSAP00000100013; ENSSSAG00000052473.
DR GeneID; 106575616; -.
DR KEGG; sasa:106575616; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000087266; Chromosome ssa17.
DR Bgee; ENSSSAG00000052473; Expressed in ovary and 13 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; PF13432; TPR_16; 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; 2.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 3.
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:UP000087266};
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 323..356
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 1135..1298
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 439..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..977
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1442 AA; 156892 MW; B04A266D6B79270C CRC64;
MQSCGVSLAV AACAAARSLG SASGGDEEKK MAAGKASETE EDFPTLTAQE RDSLVGIDSS
LFGFQRLHED GARTKALLLK AVRSYDSLIL KAEGKVEPEL FCQLGHFNLL LEDYAKALSA
YQRYYSLQSD YWKNAAFLYG LGMVYFHYNA FQWAIKAFQE VLYIDPSFSR AKEIHLRLGL
MFKVNTDYES SLKHFQLALI DSNPCTLSKA EIQFHIAHLY EIQKRYRAAK EAYESLLQTE
NLPAQVKATT LQQLGWMHHT VEQLGDRANK DSYAIQCLQK SLEADPNSGQ SWYFLGRCYS
SIGKVQDAFV SYRQSIDKSE ASADTWCSIG VLYQQQNQPM DALQAYICAV QLDHGHAAAW
MDLGTLYESC SQPHDAIKCY INAMRSKACS NATALTQRIK CLQAQLSNPQ VTSLQSKSKM
LPLIDEAWSL PIPAELTSRQ GGLNTAPQAC KPQHSSEGGG SGQALPPHVG PMGQGEDQSS
PAKRRRASSP AKSQPDSWPS NSAQQPVPNW YLSPQKLQLL DQLRSNRASL KPLQLQMLEQ
LEAQLNLMQQ HQQQMRQNAS GQLRPSLPNG PSATNSLPPP HSSLPPSRPH LAPQGLLRPP
CPPGPLANGP LAGGTPHGHS DTLSVGNNNN NNDDDPVAAT GPNGDVPYLQ PGALLPHTCT
STQSQDTARR ALHLNSTQGL QKGSAPHWAG PNGDGSLSSS GGSTHPLSHP QTPHNQVGHS
ATPSPRQQAL NHLPSPPSPP HSATSGGAPG TPATKESTPL GNGPTATATK GPGETTTANS
TAAAESLSNH IQSAAGDGGT SNRSPHHSSD NPKGGDHTPT TSAPHKKINN IHPAVSSAAS
SPISAMSTAT PSPKSTEPGQ STGPHGLNSP STTTAALSSA GPTTVVNGNG KGGISEDSQS
PLKADPPATC RRPTPPHART PPSSSSSVSI YPSSTDVLKA CRNLGKNGLS SSSILLDKCP
PPRLPPSPSP VLPKDKLNPP TPSIYLENKR DAFFPPLHQF CTNPSNPVTV IRGLAGALKL
DLGLFSTKTL VEANPDHLVE CRTQLSQPAD ENWDLSGTKK MWRCESGRAH TTIAKYAQYQ
AASFQESLRE ENEKKALKEP SDTEPASAES AARKRRGPLK HIKFGTNIDV SDERKWKLQL
QELSKLPAFA RVVSAGNLLS HVGHTILGMN TVQLYMKVPG SRIPGHQEHN NFCSVNINIG
PGDCEWFAVP EPYWGVMSNF CEKNNINFLM GSWWPNLEDL YEADVPVYRF IQRPGDLVWL
NTGTVHWVQA IGWCNNIAWN VGPLSAHQYK LAVERYEWNK LQSVKSHVPM VHLSWNMARN
IKVSDHKLFQ MIKYCLLRTL KQCQSVKEAL AAAGKETVLQ SRNRDEPAHY CTICEVEVFN
LLFVRSELLS RKQKQYVVHC QDCARKGSAE LDNFVVVEKH RMDDLMQVYD QFTLAPLHSS
SS
//
