ID   KDM8_XENTR              Reviewed;         443 AA.
AC   B2GUS6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Lysine-specific demethylase 8;
DE            EC=1.14.11.27;
DE   AltName: Full=JmjC domain-containing protein 5;
DE   AltName: Full=Jumonji domain-containing protein 5;
GN   Name=kdm8; Synonyms=jmjd5;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone demethylase required for G2/M phase cell cycle
CC       progression (By similarity). Specifically demethylates dimethylated
CC       'Lys-36' (H3K36me2) of histone H3, an epigenetic repressive mark,
CC       thereby acting as a transcription activator (By similarity). May play a
CC       role in the regulation of the circadian clock (By similarity).
CC       {ECO:0000250|UniProtKB:Q8N371, ECO:0000250|UniProtKB:Q9CXT6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC         + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC         succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:61976; EC=1.14.11.27;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q8N371};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8N371};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N371}.
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DR   EMBL; BC166391; AAI66391.1; -; mRNA.
DR   RefSeq; NP_001121525.1; NM_001128053.1.
DR   AlphaFoldDB; B2GUS6; -.
DR   SMR; B2GUS6; -.
DR   STRING; 8364.ENSXETP00000025844; -.
DR   PaxDb; B2GUS6; -.
DR   GeneID; 100158649; -.
DR   KEGG; xtr:100158649; -.
DR   CTD; 79831; -.
DR   Xenbase; XB-GENE-5811534; kdm8.
DR   eggNOG; KOG2132; Eukaryota.
DR   InParanoid; B2GUS6; -.
DR   OrthoDB; 1385616at2759; -.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000021748; Expressed in ovary and 12 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR041667; Cupin_8.
DR   InterPro; IPR003347; JmjC_dom.
DR   Pfam; PF13621; Cupin_8; 1.
DR   SMART; SM00558; JmjC; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Cell cycle; Chromatin regulator; Dioxygenase; Iron;
KW   Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..443
FT                   /note="Lysine-specific demethylase 8"
FT                   /id="PRO_0000399816"
FT   DOMAIN          298..443
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   REGION          139..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         348
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         350
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         427
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ   SEQUENCE   443 AA;  50251 MW;  0252E1BB8A61EF0D CRC64;
     MHRSVPEQVS AELPATLEQF QITLGADVED RVEECVREAA RCLYRGAIVQ CGALGELLID
     YSWEKLNARN WREVGREWRA VYSYGCLFRA VGLCSVTGSI EEALQVCDIG LLMGAEIMDN
     LLGRIISVLQ RIAPSREETK LEAERGVREP GLESSKLHSP GEHSNKKSFA SVTGRKRIRE
     GPEADFDPKG CSISEKVPCL LVPVLDSETA IPKLHCPSLE HFRDHYLVPQ KPVVLEGVID
     HWPCLKKWSV EYIQRVAGCR TVPVELGSRY TDAEWSQRLM TVNEFITKYI LDKQNGIGYL
     AQHQLFEQIP ELKEDICIPD YCCLGEASED EITINAWFGP AGTVSPLHQD PQQNFLAQIV
     GRKYIRVYSV AETEKLYPFD SSILHNTSQV DVESPDQNKF PRFSQASYQE CILSPGQVLF
     IPVKWWHYIR ALDLSFSVSF WWS