RIOX1_RAT
ID RIOX1_RAT Reviewed; 597 AA.
AC D3ZU57;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Ribosomal oxygenase 1 {ECO:0000312|RGD:1307704};
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 {ECO:0000312|RGD:1307704}; Synonyms=Mapjd, No66;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-65, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 on 'His-
CC 216'. Acts as a regulator of osteoblast differentiation via its
CC interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby
CC inhibiting SP7/OSX-mediated promoter activation. May also play a role
CC in ribosome biogenesis and in the replication or remodeling of certain
CC heterochromatic region. Participates in MYC-induced transcriptional
CC activation (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;
CC Note=Binds 1 Fe(2+) ion per subunit.;
CC -!- SUBUNIT: Interacts with SP7/OSX; the interaction is direct (By
CC similarity). Interacts with MYC. Interacts with PHF19; leading to its
CC recruitment to H3K36me3 sites (By similarity). {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}.
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DR EMBL; CH473982; EDL81467.1; -; Genomic_DNA.
DR RefSeq; NP_001101510.1; NM_001108040.1.
DR AlphaFoldDB; D3ZU57; -.
DR SMR; D3ZU57; -.
DR IntAct; D3ZU57; 1.
DR MINT; D3ZU57; -.
DR STRING; 10116.ENSRNOP00000013431; -.
DR iPTMnet; D3ZU57; -.
DR PhosphoSitePlus; D3ZU57; -.
DR jPOST; D3ZU57; -.
DR PaxDb; D3ZU57; -.
DR PeptideAtlas; D3ZU57; -.
DR Ensembl; ENSRNOT00000013431; ENSRNOP00000013431; ENSRNOG00000010126.
DR GeneID; 314300; -.
DR KEGG; rno:314300; -.
DR UCSC; RGD:1307704; rat.
DR CTD; 79697; -.
DR RGD; 1307704; Riox1.
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR HOGENOM; CLU_013645_4_1_1; -.
DR InParanoid; D3ZU57; -.
DR OMA; EWGCMAG; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; D3ZU57; -.
DR TreeFam; TF318659; -.
DR PRO; PR:D3ZU57; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000010126; Expressed in thymus and 19 other tissues.
DR Genevisible; D3ZU57; RN.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005506; F:iron ion binding; ISO:RGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISO:RGD.
DR GO; GO:0034720; P:histone H3-K4 demethylation; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
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 SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Dioxygenase; Iron; Metal-binding;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..597
FT /note="Ribosomal oxygenase 1"
FT /id="PRO_0000417667"
FT DOMAIN 250..395
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 361
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6W3"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6W3"
SQ SEQUENCE 597 AA; 67455 MW; 0B6AF59002A0FCE6 CRC64;
MDELPNGNGA APLKRGRGRR RRQPQPRGAS VLALPLRPRK VRRHRKSAAS RVAALRARAL
LSEDSDSNVE SVRGKRERPA ELPEASRSAE PRPVPVRPRP ASATLPRRVE GRAALSRNLG
KPAPLPGSHV DDPERPWDSP LQQVLAELNG IPSSRRRAAR LFEWLLAPLP PDHFYRRLWE
REAVLVRRQD HSYYEGLFST SDLDWMLRYE DVHFGQHLDA ARYIDGRRET LNPPGRALPA
AAWSLYQAGC SLRLLCPQAF SPTVWQFLAV LQEQFGSMAG SNVYLTPPNS QGFAPHYDDI
EAFVLQLEGR KLWRVYRPRD PSEELALTSS PNFSQEDLGE PVLQTVLEPG DLLYFPRGFI
HQAECQDGVH SLHLTLSTYQ RNTWGDFLEA VLPLAMQAAI EENVEFRRGL PRDFMDYMGA
QHSDSKDPRR TAFMEKVRVL VARLGHFAPV DAVADQRAKD FIHDSLPPVL TDRERALSVH
GLPIRWEAGE PVNVGAQLTT ETQVHMLQDG IARLVGEGGR LFLYYTVENS RVYHLEEPKC
LEIYPQQADA MELLLRSYPE FVRVGDLPCD SVEDQLSLAT MLYDKGLLLT KTPLVLS
