RIOX1_CHICK
ID RIOX1_CHICK Reviewed; 601 AA.
AC Q5ZMM1;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=RCJMB04_1k4;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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}.
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DR EMBL; AJ719363; CAG31022.1; -; mRNA.
DR RefSeq; NP_001026367.1; NM_001031196.1.
DR AlphaFoldDB; Q5ZMM1; -.
DR SMR; Q5ZMM1; -.
DR STRING; 9031.ENSGALP00000031993; -.
DR PaxDb; Q5ZMM1; -.
DR GeneID; 423249; -.
DR KEGG; gga:423249; -.
DR CTD; 79697; -.
DR VEuPathDB; HostDB:geneid_423249; -.
DR eggNOG; KOG3706; Eukaryota.
DR InParanoid; Q5ZMM1; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; Q5ZMM1; -.
DR PRO; PR:Q5ZMM1; -.
DR Proteomes; UP000000539; 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..601
FT /note="Ribosomal oxygenase 1"
FT /id="PRO_0000390976"
FT DOMAIN 254..399
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 365
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
SQ SEQUENCE 601 AA; 65685 MW; 1662A8B6AECAF3FF CRC64;
MAACGAEERQ RTGRLSALSV YRRAAGPGRL ERRRRGTPLP AGGKRTKARL RRGAAGGGGP
ERAAPPQGAA VSDRVERAGS SEAKQGDLKT NPSGPPAKAP AGNLETKSPG GPLTTSVGPR
AKAPAGSPEA KPPGDPATSP GGGGVPGLLR RLGRLEDSRR RAAELFRWLV APAAPEEFAR
QHWERAPLLV QRGDPGYYAG LFSTADFDAI LRSGDVHFGT HLDVTSYAEG VRETHNPVGR
ALPAVVWDFY QNGCSLRLLS PQAFSTTVWH FLSILQEHFG SMAGANTYLT PPGTQGFAPH
YDDIEAFVLQ LEGKKHWRVY GPRTSSEALP QFSSANLTQA ELGEPLLEVV LEAGDLLYFP
RGFIHQADCL PDAHSLHITV SSYQRNSWGD FLEKLLPAAL QMALEEDLEY RQGLPMDCLG
YMGVANSDAV DARRTAFVEK VQHLIKKLVD YAPIDAAMDQ RAKSFLHDCL PPVLTQSEKQ
LSVYGFPARW QDGGPRNVDI QITKDTEVRL LHHGVVRLCN EEAGVMLYYT TENSRVYHKE
EPKYLEIDPE YTDSIEFLLS SYPNHVSVDT LPCDALEDKI SLATLLFEKG ILTTKKPLVQ
V
