ID A0A340WIB2_LIPVE Unreviewed; 2358 AA.
AC A0A340WIB2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lysine-specific demethylase {ECO:0000256|RuleBase:RU369087};
DE EC=1.14.11.65 {ECO:0000256|RuleBase:RU369087};
GN Name=JMJD1C {ECO:0000313|RefSeq:XP_007446859.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007446859.1};
RN [1] {ECO:0000313|RefSeq:XP_007446859.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_007446859.1; XM_007446797.1.
DR GeneID; 103084362; -.
DR CTD; 221037; -.
DR OrthoDB; 3473445at2759; -.
DR Proteomes; UP000265300; 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:SF6; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 2C-RELATED; 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:UP000265300}.
FT DOMAIN 2092..2316
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 76..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1853..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2358 AA; 262976 MW; 0EAF65BDF03E906F CRC64;
MQGPYSLNGY RVRVYRQDSA TQWFTGIITH HDLFTRTMIV MNDQVLEPQN VDPSMVQMTF
LDDVVHSLLK GENIGITSRR RSRASQSSNT VHGHYTRAQA NSPRPAMNSQ AAVPKQNSHQ
QQRNIRPNKR KGSDSSIPDE EKMKEEKYDY IARGENAKGK NKQVMNKRRK PEEDEKKLNM
KRLRTDNVSD FSESSDSENS NKRIINNSSE QKPEYELKNK NTSKINGEEG KSQNNEKAGE
ETLIDSQPPW DQIQEDKKHE ETEKQKSADS QIQEKMIIRS SEQATLSDHN SNDLLLQERN
MEKTHTVELL PKEKFVSRPP TPKCVIDITN DTNTEKVAQE NSSTFGLQTL QKMDPNTSDS
KHSVTNTKYL ETANQDSDQS WVSDVVKVDL TQSNVRNASS GNENLNMEKE RNQYVSYISS
LSAVSVTEDK LHKRSPPPET IKSKLNTSVD AHKTKSNSSP ELVKPKINHS PDSIKSKPTF
ANSQTAGERR LANKVEHELS RCSFHPVPTR GSTLETTKSP LIIDKNEHFT VYRDPALVGS
DTGANHISPF LSQHPFPLHS SSHRTCLNPG THHPALSPAP HLLAGSSSQT PLPTINTHPL
TSGPHHSVHH PHLLSAVLPG VPTASLLGGH PRLETAHASS LSHLALAHQQ QQQLLQHQSP
HLLGQAHPSA SYNQLGLYPI IWQYPNGTHA YSGLGLPSSK WVHPENAVNA ESSLRRNSPS
PWLHQPTPVT SADGIGLLSH IPVRPSSAEP HRPLKITAHS SPPLTKCLVD HHKEELERKA
FIEPLRSVAS ASAKNDLDLN RSQTGKDGHL HRHFVDPVLN QLQRPPQETG ERLNKYKEEH
RRILQESIDV APYTTKIKGL EGERDNYSRV ASSSSSPKSH VIKQDKDVEC SVSDLYKMKH
SVPQSLPQSN YFTTLSNSVV NEPPRSYPSK EVSNIYTEKQ SNTLGAAAAN PQTLTSFISS
LSKPPPLIKH QPESEGLVGK VPEHIPHQIA SHSVTTFRND CRSPTHLTVS STSTLRSMPA
LHRAPVFHPP IHHSLERKES SYSSLSPPTL TPVMPVNAGG KVQESQKPPT LIPEPKDTQA
NFKGSSEQSL TEMWKSNNNL SKEKAEWHVE KSSGKSQAAM ASVIVRPPSS AKLDSMPAMQ
LASKDRVSER SSIGANQTDC LKSAEAGESG RIILPSVNSD SAHIKSEKNF QAVSQGSIPS
SVMSAVNTMC NTKTDIFTSA ATTTSVSSWG GSEIIYSLSN TILASKSLEC TSSKSVNHSV
AQTQECRVSM TAPVTPASSK TGSAVQSSSG FSGTTDFIHL KKHKAALAAA QYKSSNVSEP
EPNAVKNQTS SASPLLDSTV VCSTINKANS VGNGQASQTS QPNYHTKLKK AWLTRHSEED
KNTNKMENSG NSVSEIIKPC SVNLIASTSN DLQNSVDSKI IVDKFVKDDK VNRRKAKRTY
ESGSESGDSD ESESKSEQRT KRQPKPTYKK KQNDLQKRKG EIEEDLKPNG VLSRSAKEKS
KLKLQSNNNT GIPRSVLKDW RKVKKLKQTG ESFLQDDSCC EIGPNLQKCR ECRLIRSKKG
EEPTHSPVFC RFYYFRRLSF SKNGVVRIDG FSSPDQYDDE AMSLWTHENY EDDEVDIETS
KYILDIIGDK FCQLVTSEKT ALSWVKKDAK IAWKRAVRGV REMCDACEAT LFNIHWVCQK
CGFVVCLDCY KAKERKSSRD KELYAWMKCV KGQPHDHKHL MPTQIIPGSV LTDLLDAMHT
LREKYGIISH CHCTNKQNIQ VGNFSAMNGV SQVLQNVLNH SNKISLCMPE SQQQNTPQKP
ESNGNSSPES DVSTDSKLTP PESQSPLHWL ADLAEQKARE EKKENKEFAL EKQIKEEREQ
DNPDSPNSRT SPPVSQNNEQ GSTLRDLLTT TAGKLRVGST DAGIAFAPVY SMGTPSGKSG
RTMPNILDDI IASVVENKIP PNKASKINVK PELKEEPKEN RKPAMDENNK LYSDIPHSWI
CEKHILWLKD YKNINNWKLF KECWKHGQPA VVSGVHKKMN ISLWKADSIS LDFGDHQADL
LNCKDSIISN ANVKEFWDGF EEVSKRQKTK GGETVVLKLK DCPSGEDFKT MMPARYEDLL
KSLPLPEYCN PEGKFNLASH LPGFFVRPDL GPRLCSAYGV AAAKDHDIGT TNLHVEVSDI
VNILVYVGIA KGNGILSKAG ILKKFEEEDL DDILRKRLKD SSEIPGALWH IYAGKDVDKI
REFLQKISKE QGLEVLPEHD PIRDQSWYVN KNLRQRLLEE YGVKACTLIQ FLGDAIVLPA
GALHQVQNFH SCIQVTEDFV SPEHLVQSFH LTQELRLLKE EINYDDKLQV KNILYHADKE
MVRTLKIHED QVEAMEEN
//
