RIOX1_BOVIN
ID RIOX1_BOVIN Reviewed; 667 AA.
AC A5PK74;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=MAPJD, NO66;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-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 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; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
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}.
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; BC142386; AAI42387.1; -; mRNA.
DR RefSeq; NP_001093172.1; NM_001099702.1.
DR AlphaFoldDB; A5PK74; -.
DR SMR; A5PK74; -.
DR STRING; 9913.ENSBTAP00000054807; -.
DR PaxDb; A5PK74; -.
DR PRIDE; A5PK74; -.
DR Ensembl; ENSBTAT00000035624; ENSBTAP00000054807; ENSBTAG00000025372.
DR GeneID; 511031; -.
DR KEGG; bta:511031; -.
DR CTD; 79697; -.
DR VEuPathDB; HostDB:ENSBTAG00000025372; -.
DR VGNC; VGNC:55141; RIOX1.
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR InParanoid; A5PK74; -.
DR OMA; EWGCMAG; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000025372; Expressed in rumen papilla and 107 other tissues.
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 Acetylation; Chromatin regulator; Dioxygenase; Iron; Metal-binding;
KW Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..667
FT /note="Ribosomal oxygenase 1"
FT /id="PRO_0000390975"
FT DOMAIN 322..467
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 368
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 370
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 433
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 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZU57"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZU57"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6W3"
SQ SEQUENCE 667 AA; 74349 MW; 88854B02A35A3ED7 CRC64;
MDGLRASAGL LRRGRLRRRR QQQPHSGSVL ALPLRPRKIR RQLRRSVSSR MAALRAQTLQ
SEDSEDSRVE STVGEPGDPL AGGTAALSDA TGREPHGQLG PVELLEASPA SRSLQTPRAL
VEAQTPAARL VEAQTPAARL VEAHTPAARL VEAHTPPARL VEASALPARL VETSALLCST
QHLAAVPPSV APAMLSGPQG ESTGEELPWD SPLQRILAEL NRIPSSRRRA ARLFEWLISP
MPPDHFYRRL WEREAVLVRR QDHSYYQGLF STAVLDSILR NEEVQFGQHL DAARYINGRR
ETLNPPGRAL PAAAWSLYRA GCSLRLLCPQ AFSTTVWQFL AVLQEQFGSM AGSNVYLTPP
NSQGFAPHYD DIEAFVLQLE GRKLWRVYRP RVPTEELALT SSPNFSQDDL GEPVLQTVLE
PGDLLYFPRG FIHQAECQDG VHSLHLTLST FQRNTWGDFL EAVLPLAVQA AMEENVEFRR
GLPRDFMDYM GAQHSDSKDP RRTAFMEKVR VLVARLGHFA PVDAVADQRA KDFIHDSLPP
VLTDRERALS VYGLPIRWEA GEPVNVGAQL TTETEVHMLQ DGIARLVGEG GHLFLYYTVE
NSRVYHLEEP KCLEIYPQQA DAMELLLRSY PEFVRVGDLP CDTVEDQLSL ATMLYDKGLL
LTKMPLT
