RIOX2_MOUSE
ID RIOX2_MOUSE Reviewed; 465 AA.
AC Q8CD15; Q8QZX1; Q9CQ03;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ribosomal oxygenase 2 {ECO:0000312|MGI:MGI:1914264};
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|MGI:MGI:1914264};
GN Synonyms=Mina, Mina53 {ECO:0000303|PubMed:16533354};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD60965.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Stomach {ECO:0000312|EMBL:BAD60965.1};
RX PubMed=16533354; DOI=10.1111/j.1365-2605.2005.00572.x;
RA Tsuneoka M., Nishimune Y., Ohta K., Teye K., Tanaka H., Soejima M.,
RA Iida H., Inokuchi T., Kimura H., Koda Y.;
RT "Expression of Mina53, a product of a Myc target gene in mouse testis.";
RL Int. J. Androl. 29:323-330(2006).
RN [2] {ECO:0000312|EMBL:BAC27503.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC27503.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB28860.1},
RC Embryonic testis {ECO:0000312|EMBL:BAC27503.1}, and
RC Pancreas {ECO:0000312|EMBL:BAB25275.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:AAH23462.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58242.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH23462.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH23462.1}, and
RC Olfactory epithelium {ECO:0000312|EMBL:AAH58242.1};
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:16533354}.
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:0000269|PubMed:16533354}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:16533354}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed at
CC high levels in spleen, thymus, and colon, but barely detectable in
CC brain, skeletal muscle, and seminal vesicle (at protein level).
CC {ECO:0000269|PubMed:16533354}.
CC -!- DEVELOPMENTAL STAGE: In testis, expressed in the nuclei of
CC spermatogonia at all stages of the seminiferous epithelial cycle, and
CC in meiotic prophase cells such as preleptotene, leptotene and zygotene,
CC and weakly in early pachytene spermatocytes, but is absent in late
CC pachytene spermatocytes, spermatids and mature sperm (at protein
CC level). {ECO:0000269|PubMed:16533354}.
CC -!- INDUCTION: Up-regulated in experimentally-induced cryptorchid testis.
CC {ECO:0000269|PubMed:16533354}.
CC -!- SIMILARITY: Belongs to the ROX family. MINA53 subfamily. {ECO:0000305}.
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DR EMBL; AB177385; BAD60965.1; -; mRNA.
DR EMBL; AK007810; BAB25275.1; -; mRNA.
DR EMBL; AK013451; BAB28860.1; -; mRNA.
DR EMBL; AK031671; BAC27503.1; -; mRNA.
DR EMBL; BC023462; AAH23462.1; -; mRNA.
DR EMBL; BC025109; AAH25109.1; -; mRNA.
DR EMBL; BC058242; AAH58242.1; -; mRNA.
DR CCDS; CCDS28257.1; -.
DR RefSeq; NP_080186.3; NM_025910.3.
DR RefSeq; XP_006522542.1; XM_006522479.3.
DR AlphaFoldDB; Q8CD15; -.
DR SMR; Q8CD15; -.
DR STRING; 10090.ENSMUSP00000023407; -.
DR iPTMnet; Q8CD15; -.
DR PhosphoSitePlus; Q8CD15; -.
DR EPD; Q8CD15; -.
DR MaxQB; Q8CD15; -.
DR PaxDb; Q8CD15; -.
DR PeptideAtlas; Q8CD15; -.
DR PRIDE; Q8CD15; -.
DR ProteomicsDB; 253245; -.
DR Antibodypedia; 2005; 390 antibodies from 37 providers.
DR DNASU; 67014; -.
DR Ensembl; ENSMUST00000023407; ENSMUSP00000023407; ENSMUSG00000022724.
DR Ensembl; ENSMUST00000160571; ENSMUSP00000125297; ENSMUSG00000022724.
DR GeneID; 67014; -.
DR KEGG; mmu:67014; -.
DR UCSC; uc007zph.2; mouse.
DR CTD; 84864; -.
DR MGI; MGI:1914264; Riox2.
DR VEuPathDB; HostDB:ENSMUSG00000022724; -.
DR eggNOG; KOG3706; Eukaryota.
DR GeneTree; ENSGT00390000000083; -.
DR HOGENOM; CLU_013645_0_1_1; -.
DR InParanoid; Q8CD15; -.
DR OMA; GSPTHEF; -.
DR OrthoDB; 693909at2759; -.
DR PhylomeDB; Q8CD15; -.
DR TreeFam; TF318659; -.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 67014; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Mina; mouse.
DR PRO; PR:Q8CD15; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8CD15; protein.
DR Bgee; ENSMUSG00000022724; Expressed in otic placode and 255 other tissues.
DR ExpressionAtlas; Q8CD15; baseline and differential.
DR Genevisible; Q8CD15; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
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:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
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:0042127; P:regulation of cell population proliferation; ISO:MGI.
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 1: Evidence at protein 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_0000308378"
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"
FT CONFLICT 15
FT /note="A -> E (in Ref. 3; AAH25109/AAH23462)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="S -> N (in Ref. 2; BAC27503)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="D -> E (in Ref. 3; AAH25109/AAH23462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 53517 MW; E0504FE459FFC47A CRC64;
MPKKVQPTGD ENEEASVPCK RVKEELPETL SVLNFDSPSS FFESLISPIK VETFFKEFWE
QKPLLIQRDD PVLAKYYQSL FSLSDLKRLC KKGVYYGRDV NVCRSISGKK KVLNKDGRAH
FLQLRKDFDQ KRATIQFHQP QRYKDELWRI QEKLECYFGS LVGSNVYMTP AGSQGLPPHY
DDVEVFILQL EGTKHWRLYS PTVPLAHEYS VESEDRIGTP THDFLLKPGD LLYFPRGTIH
QAETPSGLAY SIHLTISTYQ NNSWGDCLLD SISGFVFDIA KEDVALRSGM PRRMLLNVET
PADVTRKLSG FLRTLADQLE GREELLSSDM KKDFVKHRLP PFFEGNGTET MDPGKQLPRL
DNIIRLQFKD HIVLTVGPDK NPFDEAQQKV VYIYHSLKNV RQMHMIGEEE ESEIFGLRFP
LSHVDALKQI WCGSPIRVKD LKLDTDEEKE NLALSLWSES LIQVL
