ID A0A6P6EDQ4_OCTDE Unreviewed; 1186 AA.
AC A0A6P6EDQ4;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 24.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN Name=Hr {ECO:0000313|RefSeq:XP_023570426.1};
OS Octodon degus (Degu) (Sciurus degus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Octodontidae;
OC Octodon.
OX NCBI_TaxID=10160 {ECO:0000313|Proteomes:UP000515203, ECO:0000313|RefSeq:XP_023570426.1};
RN [1] {ECO:0000313|RefSeq:XP_023570426.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9' of
CC histone H3, thereby playing a central role in histone code.
CC {ECO:0000256|RuleBase:RU369087}.
CC -!- FUNCTION: Histone demethylase that specifically demethylates both
CC mono- and dimethylated 'Lys-9' of histone H3. May act as a
CC transcription regulator controlling hair biology (via targeting of
CC collagens), neural activity, and cell cycle.
CC {ECO:0000256|ARBA:ARBA00060257}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + 2 2-oxoglutarate
CC + 2 O2 = L-lysyl(9)-[histone H3] + 2 formaldehyde + 2 succinate + 2
CC CO2; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.65;
CC Evidence={ECO:0000256|ARBA:ARBA00047648,
CC ECO:0000256|RuleBase:RU369087};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|RuleBase:RU369087};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|RuleBase:RU369087};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are known to mediate the
CC association with nuclear receptors. {ECO:0000256|RuleBase:RU369087}.
CC -!- DOMAIN: The JmjC domain and the C6-type zinc-finger are required for
CC the demethylation activity. {ECO:0000256|RuleBase:RU369087}.
CC -!- SIMILARITY: Belongs to the JHDM2 histone demethylase family.
CC {ECO:0000256|RuleBase:RU369087}.
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DR RefSeq; XP_023570426.1; XM_023714658.1.
DR AlphaFoldDB; A0A6P6EDQ4; -.
DR GeneID; 101564691; -.
DR CTD; 55806; -.
DR Proteomes; UP000515203; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:TreeGrafter.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:TreeGrafter.
DR GO; GO:0140683; F:histone H3K9me/H3K9me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:UniProtKB-ARBA.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070988; P:demethylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:TreeGrafter.
DR FunFam; 2.60.120.650:FF:000017; lysine-specific demethylase hairless isoform X1; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR045109; LSDs-like.
DR PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR PANTHER; PTHR12549:SF4; LYSINE-SPECIFIC DEMETHYLASE HAIRLESS; 1.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU369087};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369087};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369087};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000515203};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 943..1154
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 309..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..358
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1186 AA; 126891 MW; C498045753BE5DE1 CRC64;
MASTPSFLKD TPAWEKTVLE NGIVGQEPGT PPRDGLRHGS LCLGEPAPFW RGVLSTPDSW
LPPGFPQGPK DTLPLVEGEG PQNGERKASW LGSKDGLRWK EAMLAHPQAF CGPMCPPHYG
PLIPEHGGRQ PNSDLVAFRP LHCPFLLETK ILERAPFWVP TCLPPYLVSS LPPERPCDWP
LAPHPWMYPA GQHKAPSAFS LGSKGFYHKD PSMPRLAKEP SLAVLEPGLL GSAPGGLLQR
AREAEGPSLH QREGNLAAGR PKNLCSLFLG HPDTVPRTPW PTCPPGLVHT LSNVWTVPGS
GSLGYQLGPP VTPRCPSPGP STTQGGCCSS HPPAQEGDVS PCGKCQEGPE GISSGPAESG
EEASKAVSPR ACPPSHHTKL KKTWLTRHSE QFGCPRGWPG DEESPAVQLR ALKRAGSPEV
QGAMGGPALK RPSDPFPGTT GQGARGWQEA LDASVGSKAE AEQHNVQRGL RGGRASLQDP
RPQGTSGLTL PAVITQCQSC AQAAGEVEAL ACHSQEAQRS SLGAEPQQED SEEGGGSGSD
LLSMSLAKHL LSGLGDRLCR LLRREREALA WAQRESQGPA VTEDSPGTPR CCSRCHHGLF
NTHWRCPRCS HRLCVACGRM AGAGRAREKA ASPSHPAGSQ EQSLEECAQE AGHTACSLVL
TQFVSSQALA ELSTAMHQVW AKFDIRGHCL CQADARVWAP GAGGQQKEPT EKTPPTPQPS
CNGDSNRTKD IKEETPDSTE SPAEDRASRG PLPCPSLCEL LASTAVKLCL GHERIHMAFA
PVTPALPSDD RITNILDSII AQVVERKIQE KALGPGLRGG PGLRKGLGLS LSPVRPRLPP
PGALLCLQEP RPRRCFHLFQ EHWRQGQPVL VSGIQRTLQG GLWGVEALRA LGGQVQALSA
LGPPQPTGLD NVAFWEGFSR PESRPKPDEG SVFLLHRVLG DEDASRVENL ASSLPLPEYC
AHHGKLNLAS YLPPGLALRL LEPQLWAAHG VSPHRGHLGT KNLCVEVADL VSILVHAEAA
LPAWHRAQKD FLSGLDGEGL WSPGSQVSTV WHVFRAQDAQ RIRRFLQMVC PAGAGTLEPG
APGSCYLDAA LRRRLREEWG VSCWTLLQAP GEAVLVPAGA PHQVQGLVST VSVTQHFLSP
ETSVLSTQLC HQGPSLPPDC RLLYAQMDWA VFQAVKVAVG TLQEAQ
//
