ID   KDM5C_CRIGR             Reviewed;         180 AA.
AC   P41228;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Lysine-specific demethylase 5C;
DE            EC=1.14.11.67 {ECO:0000250|UniProtKB:P41229};
DE   AltName: Full=Histone demethylase JARID1C;
DE   AltName: Full=Jumonji/ARID domain-containing protein 1C;
DE   AltName: Full=Protein SmcX;
DE   AltName: Full=Protein Xe169;
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase 5C {ECO:0000305};
DE   Flags: Fragment;
GN   Name=KDM5C; Synonyms=JARID1C, SMCX, XE169;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7951318; DOI=10.1038/ng0894-491;
RA   Wu J., Salido E., Yen P., Mohandas T., Shapiro L.J.;
RT   "The murine Xe169 gene escapes X-inactivation like its human homologue.";
RL   Nat. Genet. 7:491-496(1994).
CC   -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-4' of
CC       histone H3, thereby playing a central role in histone code. Does not
CC       demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79'
CC       or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not
CC       monomethylated H3 'Lys-4'. Participates in transcriptional repression
CC       of neuronal genes by recruiting histone deacetylases and REST at
CC       neuron-restrictive silencer elements. Represses the CLOCK-ARNTL/BMAL1
CC       heterodimer-mediated transcriptional activation of the core clock
CC       component PER2. {ECO:0000250|UniProtKB:P41229,
CC       ECO:0000250|UniProtKB:P41230}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC         [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC         H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC         Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC         Evidence={ECO:0000250|UniProtKB:P41229};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P41229};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:P41229};
CC   -!- SUBUNIT: Part of two distinct complexes, one containing E2F6, and the
CC       other containing REST. {ECO:0000250|UniProtKB:P41229}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC       {ECO:0000305}.
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DR   EMBL; L29564; AAA62383.1; -; mRNA.
DR   AlphaFoldDB; P41228; -.
DR   STRING; 10029.XP_007639140.1; -.
DR   eggNOG; KOG1246; Eukaryota.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Chromatin regulator; Dioxygenase; Iron; Metal-binding;
KW   Nucleus; Oxidoreductase; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           <1..>180
FT                   /note="Lysine-specific demethylase 5C"
FT                   /id="PRO_0000200585"
FT   REGION          116..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41229"
FT   NON_TER         1
FT   NON_TER         180
SQ   SEQUENCE   180 AA;  19964 MW;  89D2A3C50B4A703A CRC64;
     QDWFHGRCVT VPRLLSSQRP GFTSSPLLAW WEWDTKFLCP LCMRSRRPRL ETILALLVAL
     QRLPVRLPEG EALQCLTERA ISWQGRARQV LASEEVTALL GRLAELRQRL QAESKPEESL
     AYSSDAGEGA GHIPKVQGLL ENGDSVTSPE KVATEEGSGK RDLELLSSLL PQLTGPVLEL