ID A0A2K5IPC6_COLAP Unreviewed; 1192 AA.
AC A0A2K5IPC6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
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:ENSCANP00000018430.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000018430.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC succinate; 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|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 AlphaFoldDB; A0A2K5IPC6; -.
DR STRING; 336983.ENSCANP00000018430; -.
DR Ensembl; ENSCANT00000041385.1; ENSCANP00000018430.1; ENSCANG00000032640.1.
DR Proteomes; UP000233080; Unplaced.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070988; P:demethylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR InterPro; IPR045109; JHDM2-like.
DR InterPro; IPR003347; JmjC_dom.
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 Iron {ECO:0000256|RuleBase:RU369087};
KW Metal-binding {ECO:0000256|RuleBase:RU369087};
KW Nucleus {ECO:0000256|RuleBase:RU369087};
KW Reference proteome {ECO:0000313|Proteomes:UP000233080}.
FT DOMAIN 949..1160
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1192 AA; 127743 MW; 0541165F9FE2A0A7 CRC64;
MESTPSFLKG TWEKTAAENG IVRQEPSSPP RDGLHRGPLC LGEPAPFWGG IPNTPDSWLP
PGFPQGPKDT LPLVEGEGPQ NGERKVNWLG SKEGLRWKEA MLTHPLAFCG PACPPRCGPL
MPEHSGGHLK SDPVAFRPWS CPFLLETKIL ERAPFWVPTC LPPYLVSGLP PERPRDWPLA
PHPWIHSGGQ PKVPSAFSLG SKGFYHKDPS ILRLAKEPLA AAEPGLLGLN PGGHLQRAGE
AERPSLHQRD GEMGGGRQQN PCPLFLGQPD TVPRTPWPAY PPGFFHTLGN VWAGPSGGSL
GYQLGPAATP RCPSPEPPIT QRGCCSSYPP TKDGGLGPCG KCQEGLEGGA SGASEPSEEV
NKASDPRACS TSHHTKLKKT WLTRHSEQFE CPRGCPEAEE RPVAQLRALK RAGSPEIQGA
VGGPAPKRPP DPFPGTAEQG AGGWQEVRDT SIGNKEADSG QHDDQRGPRD GQASLQNSGL
QDIPCLARPA KLAQCQSCAQ AAGEGGGPAG HFQQVQRSPL GGEPQQEEDT AANSSSEEGP
GSGPDGGLST GLAKHLLSGL GDRLCRLLRR EREALAWAQR EAGQGPAVTE DNLGIPRCCS
RCHHGLFNTH WRCPCCSHRL CVACGRVAGA GRARDKAGSR EQSTEECTQE AGHAACSLML
THFLSDYPSP KSLAELNTAM HQVWVKFDIR GHCPCQADAR VWAPGDAGQQ KELTQKMPPT
PQPSCNGDTH RTKSIKEETP DSTETPAEDR AGQAPLPCPS LCELLASTAV KLCLGHERIH
MAFAPVTPAL PSDDRITNIL DSIIAQVVER KIQEKALGPG LRAGPGLRKG LGLPLSPVRP
RLPPLGALLW LQEPRPRPRR GFHLFQEHWR QGQPVLVSGI QRTLQGNLWG TEALGALGGQ
VQALSPLGPP QPTSLGSTAF WEGFSWPELR PKSDEGSVLL LHRALGDEDT SRVENLAASL
PLPEYCAHHG KLNLASYLPP GLALRPLEPQ LWAAYGVSPH RGHLGTKNLC VEVADLVSIL
VHAEAPLPAW HRAQKDFLSG LDGEGLWSPG SQVSTVWHVF RAQDAQRIRR FLQMVCPAGA
GALEPGAPGS CYLDAGLRRR LREEWGVSCW TLLQAPGEAV LVPAGAPHQV QGLVSTVSVT
QHFLSPETSA LSAQLCHQGS SLHPDCRLLC AQMDWAVFQA VKVAVGTLQE AK
//
