ID   RIOX2_PONAB             Reviewed;         465 AA.
AC   Q5R673;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Ribosomal oxygenase 2;
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; Synonyms=MINA {ECO:0000250|UniProtKB:Q8IUF8};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1] {ECO:0000312|EMBL:CAH92743.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex {ECO:0000312|EMBL:CAH92743.1};
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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'. May play an important role
CC       in cell growth and survival. May be involved in ribosome biogenesis,
CC       most likely during the assembly process of pre-ribosomal particles (By
CC       similarity). {ECO:0000250}.
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; CR860623; CAH92743.1; -; mRNA.
DR   RefSeq; NP_001127580.1; NM_001134108.1.
DR   AlphaFoldDB; Q5R673; -.
DR   SMR; Q5R673; -.
DR   STRING; 9601.ENSPPYP00000015228; -.
DR   Ensembl; ENSPPYT00000015835; ENSPPYP00000015228; ENSPPYG00000013621.
DR   GeneID; 100174658; -.
DR   KEGG; pon:100174658; -.
DR   CTD; 84864; -.
DR   eggNOG; KOG3706; Eukaryota.
DR   GeneTree; ENSGT00390000000083; -.
DR   InParanoid; Q5R673; -.
DR   OrthoDB; 693909at2759; -.
DR   Proteomes; UP000001595; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
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_0000308379"
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;  52614 MW;  705B3EBC9DC4BA84 CRC64;
     MPKKAKPAGS GKEEGPVPCK QMKVEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE
     QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH
     FLQLRKDFDQ KRATIQLHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY
     DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH
     QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDAA KEDVELRAGI PRQLLLQVES
     TTVATRRLSG FLRTLADRLE GTKEVLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL
     DSVVRLQFKD HIVLTVLPDQ DQSDEAQEKM VYIYHSLKNS REIHMMGNEE ETESHGLRFP
     LSHLDALKQI WNSPAISVND LKLTTDEEKE SLVLSLWTEC LIQVV