RIOX2_RAT
ID RIOX2_RAT Reviewed; 465 AA.
AC Q8CFC1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ribosomal oxygenase 2 {ECO:0000312|RGD:708521};
DE AltName: Full=Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA;
DE EC=1.14.11.-;
DE AltName: Full=Histone lysine demethylase MINA;
DE AltName: Full=MYC-induced nuclear antigen;
GN Name=Riox2 {ECO:0000312|RGD:708521};
GN Synonyms=Mina, Mina53 {ECO:0000312|EMBL:BAC16362.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC16362.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12091391; DOI=10.1074/jbc.m204458200;
RA Tsuneoka M., Koda Y., Soejima M., Teye K., Kimura H.;
RT "A novel myc target gene, mina53, that is involved in cell proliferation.";
RL J. Biol. Chem. 277:35450-35459(2002).
RN [2] {ECO:0000312|EMBL:AAH87650.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary {ECO:0000312|EMBL:AAH87650.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Oxygenase that can act as both a histone lysine demethylase
CC and a ribosomal histidine hydroxylase. Is involved in the demethylation
CC of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an
CC increase in ribosomal RNA expression. Also catalyzes the hydroxylation
CC of 60S ribosomal protein L27a on 'His-39' (By similarity). May play an
CC important role in cell growth and survival. May be involved in ribosome
CC biogenesis, most likely during the assembly process of pre-ribosomal
CC particles. {ECO:0000250, ECO:0000269|PubMed:12091391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-histidyl-[ribosomal protein uL15] + O2 =
CC (3S)-3-hydroxy-L-histidyl-[ribosomal protein uL15] + CO2 + succinate;
CC Xref=Rhea:RHEA:54024, Rhea:RHEA-COMP:13760, Rhea:RHEA-COMP:13761,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:30031, ChEBI:CHEBI:138021;
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 {ECO:0000250|UniProtKB:Q8IUF8}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q8IUF8}.
CC -!- SIMILARITY: Belongs to the ROX family. MINA53 subfamily. {ECO:0000305}.
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DR EMBL; AB083195; BAC16362.1; -; mRNA.
DR EMBL; BC087650; AAH87650.1; -; mRNA.
DR RefSeq; NP_695221.1; NM_153309.2.
DR AlphaFoldDB; Q8CFC1; -.
DR SMR; Q8CFC1; -.
DR IntAct; Q8CFC1; 1.
DR STRING; 10116.ENSRNOP00000002285; -.
DR iPTMnet; Q8CFC1; -.
DR PhosphoSitePlus; Q8CFC1; -.
DR Ensembl; ENSRNOT00000100511; ENSRNOP00000081634; ENSRNOG00000001680.
DR GeneID; 266670; -.
DR KEGG; rno:266670; -.
DR UCSC; RGD:708521; rat.
DR CTD; 84864; -.
DR RGD; 708521; Riox2.
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR InParanoid; Q8CFC1; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; Q8CFC1; -.
DR TreeFam; TF318659; -.
DR Reactome; R-RNO-3214842; HDMs demethylate histones.
DR PRO; PR:Q8CFC1; -.
DR Proteomes; UP000002494; Chromosome 11.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IBA:GO_Central.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; IMP:RGD.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IBA:GO_Central.
DR GO; GO:0034720; P:histone H3-K4 demethylation; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR039994; JmjC_protein.
DR PANTHER; PTHR13096; PTHR13096; 1.
DR Pfam; PF08007; Cupin_4; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Transcription;
KW Transcription regulation.
FT CHAIN 1..465
FT /note="Ribosomal oxygenase 2"
FT /id="PRO_0000308380"
FT DOMAIN 139..271
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 179
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 181
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUF8"
SQ SEQUENCE 465 AA; 53216 MW; 4CDC8038AA81B5AA CRC64;
MPKKVKPTGD ENEEESVPCK QVKEELPNTL SVLNFDSPSS FFESLISPIK VETFFKEFWE
QKPLLIQRDD PSLAAYYQSL FSLSDLRSLC SQGLYYGRDV NVCRCIGGKK KVLNKDGKAQ
FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYMTP AGSQGLPPHY
DDVEVFILQL EGRKRWRLYS PTVPLAREYS VEPEDRIGTP THDFLLKPGD LLYFPRGTIH
QAETPSGLAH SIHLTISTYQ NNSWGDYLLD SISGLVFDIA KEDVALRTGM PRRMLMNVET
PADVTRKLSG FLRTLADQLE GRKELLSSDM KKDFVMHRLP PFCVGNGTES MNPGGKLPRL
NSIVRLQFKD HIVLTVGPDQ NQSDEAQQKV VYIYHSLKNE RQTHMMGKEV ETEIYGLRFP
LSYVDALKQI WCGSPVRVKD LKLGTDEEKE NLAVSLWTEC LVHVL
