ID A0A2K5HRV3_COLAP Unreviewed; 1677 AA.
AC A0A2K5HRV3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000007068.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000007068.1}
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 -!- 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_011813955.1; XM_011958565.1.
DR Ensembl; ENSCANT00000026321.1; ENSCANP00000007068.1; ENSCANG00000023322.1.
DR GeneID; 105523630; -.
DR KEGG; cang:105523630; -.
DR CTD; 23135; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000233080; Unplaced.
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; -; 1.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
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 PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR14017:SF5; LYSINE-SPECIFIC DEMETHYLASE 6B; 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 SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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:UP000233080}.
FT DOMAIN 1334..1497
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 52..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..658
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..900
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..987
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1677 AA; 180312 MW; 680C8302D65231A5 CRC64;
MHRAVDPPGA RAAREAFALG GLSCAGAWSS CPPHPPPRSA WLPGGRCSAS IGQPPLPAPL
PPSHGSSSGH PNKPYYAPGA PTPRPLHGKL ESLHGCVQAL LREPAQPGLW EQLGQLYESE
HDSEEATRCY HSALRYGGSF AELGPRIGRL QQAQLWNFHT GSCQHRAKVL PPLEQVWNLL
HLEHKRNYGA KRGGPPVKRA AEPPVVQPVP PAALSGPSGE EGLSPGGKRR RGCNSEQTGL
PPGLPLPPPP LPPPPPPPPL PGLATSPPFQ LTKPGLWSTL HGDAWGPERK GSAPPERQEQ
RHSLPHPYPY PAPAYTTHPP GHRLVPAAPP GPGPRPPGAE SHGCLPATRP PGSDLRESRV
QRSRMDSSVS PAATTACVPY APSRPPGLPG TTTTSSSSSS SSNTGLRGVE PNPGIPGADH
YQTPSLEVSH QGRLGPSVHS SRKPFLGAPA ATPHLSLPPG PSSPPPPPCP RLLRPPPPPA
WLKGPACRAA REDGEILEEL FFGTEGPPRP APPPLPHREG FLGPPASRFS VGTQDSHTPP
TPPAPTTSSS NSNNGSHSSS PAGPVSFPPP PYLARSIDSL PRPPSPAQNP QDPPLVPLTL
ALPPAPPSSC HQNTSGSFRR PESPRPRVSF PKTPEVGPGP PPGPLSKAPQ PVPPGVGELP
ARGPRLFDFP PTPLEDQFEE PAEFKILPDG LANIMKMLDE SIRKEEEQQQ HEAGVAPPPP
LKEPFASLQP PFPTDTAPTT TAPAAAVTIT TTTTTATQEE EKKPPPALPP PPPLAKFPPP
PQPQPPPPPP ANPASLLKSL ASVLEGQKYC YRGTGAAVST RPGPLPTTQY SPGPPSGATA
PPPTSVAPSA QGSPQPSASS SSQFSTSGGP WARERRAGEE PVPGPTTPTQ PPPPLPLPPA
RSESEVLEEI SRACETLVER VGRSAPDPAD PADTAEPVDS GTERLLPPAQ AKEEGGGVVA
VAVTGSCKRR QKEHQKEHRR HRRACKDSVG RRPREGRAKA KTKAPKEKSR RVLGNLDLQS
EEIQGREKSR PDLGGASKVK PPTAPAPPPA PAPSAQPTPP SASVPGKKAR EEAPGPPGVS
RADMLKLRSL SEGPPKELKI RLIKVESGDK ETFIASEVEE RRLRMADLTI SHCAADVVRA
SKNAKVKGKF RESYLSPAQS VKPKINTEEK LPREKLNPPT PSIYLESKRD AFSPVLLQFC
TDPRNPITVI RGLAGSLRLN LGLFSTKTLV EASGEHTVEV RTQVQQPSDE NWDLTGTRQI
WPCESSRSHT TIAKYAQYQA SSFQESLQEE KESEDEESEE PDSTTGTPPS STPDPKNHHI
IKFGTNIDLS DAKRWKPQLQ ELLKLPAFMR VTSTGNMLSH VGHTILGMNT VQLYMKVPGS
RTPGHQENNN FCSVNINIGP GDCEWFAVHE HYWETISAFC DRHGVDYLTG SWWPILDDLY
ASNIPVYRFV QRPGDLVWIN AGTVHWVQAT GWCNNIAWNV GPLTAYQYQL ALERYEWNEV
KNVKSIVPMI HVSWNVARTV KISDPDLFKM IKFCLLQSMK HCQVQRESLV RAGKKIAYQG
RVKDEPAYYC NECDVEVFNI LFVTSENGSR NTYLVHCEGC ARRRSAGLQG VVVLEQYRTE
ELAQAYDAFT LVRARRARGQ RRRALGQAAG TGFGSPAAPF PEPPLAFSPQ APASTSR
//
