RIOX1_DANRE
ID RIOX1_DANRE Reviewed; 544 AA.
AC A3KP59;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Ribosomal oxygenase 1;
DE AltName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66;
DE EC=1.14.11.-;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:Q9H6W3};
DE AltName: Full=Histone lysine demethylase NO66;
GN Name=riox1; Synonyms=no66; ORFNames=zgc:162967;
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=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase
CC and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-
CC 4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a
CC central role in histone code. Preferentially demethylates trimethylated
CC H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues,
CC while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2).
CC Also catalyzes the hydroxylation of 60S ribosomal protein L8. Acts as a
CC regulator of osteoblast differentiation via its interaction with
CC SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting
CC SP7/OSX-mediated promoter activation. May also play a role in ribosome
CC biogenesis and in the replication or remodeling of certain
CC heterochromatic region (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidyl-[protein] + O2 = (3S)-3-hydroxy-L-
CC histidyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:54256,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:13840, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:138021;
CC Evidence={ECO:0000250|UniProtKB:Q9H6W3};
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 Evidence={ECO:0000250|UniProtKB:Q9H6W3};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ROX family. NO66 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC134172; AAI34173.1; -; mRNA.
DR RefSeq; NP_001082857.1; NM_001089388.1.
DR AlphaFoldDB; A3KP59; -.
DR SMR; A3KP59; -.
DR STRING; 7955.ENSDARP00000088500; -.
DR PaxDb; A3KP59; -.
DR PeptideAtlas; A3KP59; -.
DR GeneID; 560815; -.
DR KEGG; dre:560815; -.
DR CTD; 79697; -.
DR ZFIN; ZDB-GENE-041008-221; riox1.
DR eggNOG; KOG3706; Eukaryota.
DR InParanoid; A3KP59; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; A3KP59; -.
DR PRO; PR:A3KP59; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; 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:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; ISS:UniProtKB.
DR GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB.
DR GO; GO:0034720; P:histone H3-K4 demethylation; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR039994; JmjC_protein.
DR InterPro; IPR013109; NO66.
DR PANTHER; PTHR13096; PTHR13096; 1.
DR PANTHER; PTHR13096:SF4; PTHR13096:SF4; 1.
DR Pfam; PF08007; Cupin_4; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..544
FT /note="Ribosomal oxygenase 1"
FT /id="PRO_0000390977"
FT DOMAIN 197..342
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 243
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 245
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 544 AA; 61517 MW; 11D2291931E0B1AF CRC64;
MERKHMSALS IYQSLSGGKT PQAEDKAPPA KKVKRKENGV RPSKKATKKK GTKPLKSSVR
SSSSEKEKHE GERDCREMNG KRFDNVALDI LLTDLAKVNN SRDRANRLFQ WLIHPVQDKS
FFRDNWEKKP ILIQRQNADY YKGLFSTAEF DRILRNDDVQ YGVNLDVTSY TNGKRETHNP
PGRALPYTVW DFYESGCSIR MLNPQAFSST VWQVLSVLQE KFGSMAGANV YLTPPGTQGF
APHFDDIEAF VVQLEGRKHW RVYNPRCEDE VLSLVSSPNF SQDEIGEPVM DVVLEAGDLL
YFPRGFVHQG DCLPDAHSLH ITISSYQRNS WGDLMLKLMP AALEVAMEED VEFRKGLPLD
YLQYMGVQNS EKEDPRRDRF MAHIQGLMKK LVSFAPVDAA VDQKAKDFLH DCLPPLLTAE
EKAGSVYGAP ARWGDSEALD VAVELKSQTR IKLVRAGAAR LCSDGDTVHL YYTTENSRVY
HKEASKSFEM KTEHIDAMEF LIHSYPKFVS VASLPCETAE AKMSLAELLF EKGLIFTAEP
LTAQ
