ID   KDM8_SALSA              Reviewed;         404 AA.
AC   B5XF11;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 38.
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   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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; BT049630; ACI69431.1; -; mRNA.
DR   AlphaFoldDB; B5XF11; -.
DR   SMR; B5XF11; -.
DR   STRING; 8030.ENSSSAP00000032593; -.
DR   PRIDE; B5XF11; -.
DR   OMA; PPKWWHH; -.
DR   Proteomes; UP000087266; Genome assembly.
DR   Bgee; ENSSSAG00000040804; Expressed in semen and 16 other tissues.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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..404
FT                   /note="Lysine-specific demethylase 8"
FT                   /id="PRO_0000399815"
FT   DOMAIN          268..404
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         309
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
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         388
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ   SEQUENCE   404 AA;  46254 MW;  AE371BED8373F9C1 CRC64;
     MAELWSAISA ALPVTEAEFP LDFSEKVEPS VVDVLKRCRQ QLYTGSGRWR QNAQIILDFS
     WEKLNTGTWR DVDKEWRCLY SYGCLFKVAA LCRDDASPAT VQEAIRTCDL GLLMGAAIMD
     NILQTFVKIL QNEIRKRHSN EENLSEGVSA KKMKVDCVSV PVVKQALAVP RIHCPSLESF
     KKDYLDPQKP VILEGIIDHW PAFKNHPWSI EYLQTVAGCR TVPVEVGSRY TDEEWSQTLL
     TVNEFIDRYI VVKDASSLGY LAQHQLFDQV PELKDDIRIP DYCCLGEGEE DDITINAWFG
     PGGTVSPLHQ DPQQNFLAQV VGRKYIRLYS PEDTEKLYPH QLQLLHNTSQ VEVESPDVVR
     FPEFVKAPYL ECVLQPGEVL FIPVKHWHYV RSLELSFSVS FWWS