RIOX2_BOVIN
ID RIOX2_BOVIN Reviewed; 462 AA.
AC Q5EA24; Q32KR4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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:0000312|EMBL:AAX08762.1};
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] {ECO:0000312|EMBL:AAX08762.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2] {ECO:0000312|EMBL:AAI09962.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus {ECO:0000312|EMBL:AAI09962.1};
RC TISSUE=Liver {ECO:0000312|EMBL:AAI09962.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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; BT020745; AAX08762.1; -; mRNA.
DR EMBL; BC109961; AAI09962.1; -; mRNA.
DR RefSeq; NP_001015675.1; NM_001015675.1.
DR RefSeq; XP_005201241.1; XM_005201184.3.
DR RefSeq; XP_005201242.1; XM_005201185.2.
DR RefSeq; XP_010799281.1; XM_010800979.2.
DR AlphaFoldDB; Q5EA24; -.
DR SMR; Q5EA24; -.
DR STRING; 9913.ENSBTAP00000020656; -.
DR PaxDb; Q5EA24; -.
DR PRIDE; Q5EA24; -.
DR GeneID; 540466; -.
DR KEGG; bta:540466; -.
DR CTD; 84864; -.
DR eggNOG; KOG3706; Eukaryota.
DR HOGENOM; CLU_013645_0_1_1; -.
DR InParanoid; Q5EA24; -.
DR OrthoDB; 693909at2759; -.
DR TreeFam; TF318659; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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..462
FT /note="Ribosomal oxygenase 2"
FT /id="PRO_0000308376"
FT DOMAIN 139..271
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IUF8"
FT CONFLICT 297
FT /note="Missing (in Ref. 2; AAI09962)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="F -> I (in Ref. 2; AAI09962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 52455 MW; FF8FAFBE331EE2CE CRC64;
MPKKARPAGD GKEQGPAPKQ VKVEAACGPS SPLNFDSPSG LFESFISPIK TETFFKEFWE
QKPLLIQRDD PALATYYQSL FRLSDLKSLC SWGIYYGRDV NVCRCVHGKK KVLNKDGRVH
FLQLRQDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGAQGLPPHY
DDVEVFILQL EGEKHWRLYQ PTVPLAREYS VEAEDRIGRP THEFTLKPGD LLYFPRGTIH
QADTPEGLAH STHVTISTYQ SSSWGDFLLD TISGLVFDTA KADVALRAGI PRQLLLQAES
IAVATRLSGF LRMLADRLEG TKELPSADMK KDFAMNRLPP YYMGDRAKLV APGGQLPGLD
STVRLQFRDH VVLTVGPYQD PSDETRGEMV YVYHSLRNRR DTHMMGNETE SYGLRFPLSY
MDALKQIWNS SAISVKDLKL TTDEEKQNLV LSLWTECLIQ VV
