ID   KDM8_DANRE              Reviewed;         406 AA.
AC   A8E534;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
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; ORFNames=zgc:173863;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2007) 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; BC153446; AAI53447.1; -; mRNA.
DR   AlphaFoldDB; A8E534; -.
DR   SMR; A8E534; -.
DR   STRING; 7955.ENSDARP00000124888; -.
DR   PaxDb; A8E534; -.
DR   PeptideAtlas; A8E534; -.
DR   ZFIN; ZDB-GENE-040718-411; kdm8.
DR   eggNOG; KOG2132; Eukaryota.
DR   InParanoid; A8E534; -.
DR   PhylomeDB; A8E534; -.
DR   PRO; PR:A8E534; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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..406
FT                   /note="Lysine-specific demethylase 8"
FT                   /id="PRO_0000399814"
FT   DOMAIN          270..406
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   REGION          143..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         311
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         313
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ   SEQUENCE   406 AA;  46752 MW;  2FFEBDC69BCD7679 CRC64;
     MASVWTDIRA VLPSTVSEFP LDFSEKIDLS VLKCLELSRD QLYSEADCPV SAERAQIIID
     YSWEKLNIGT WRDVDKEWRR VYSYGCLFKV LSLCHGNPPQ NIIQEAVRTC DMSLLMGAAI
     MDNILQRLVG ILRNKIKTTC PNKAERSEEP FSKKRKHDCK SEPVLNPTKE VPRIHCPSLE
     RFRSDFLDPK KPVIIEGITD LWPAFTQHPW SIDYLRTVAG CRTVPIEVGS KYTDEEWSQK
     LITVNDFIDR YITGTEEDGV GYLAQHQLFD QVPELKEDIR IPDYCCLGEG DEDDITINAW
     FGPGGTVSPL HQDPQQNFLA QVVGRKYIRL YSPEDTKSLY PHESQLLHNT SQVEVENPDL
     VKFPDFSRAS YEECVLCPGD VLFIPLQHWY YVRSLELSFS VSFWWS