RIOK3_MOUSE
ID RIOK3_MOUSE Reviewed; 519 AA.
AC Q9DBU3; Q3UI51; Q8CIC1;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Serine/threonine-protein kinase RIO3;
DE EC=2.7.11.1;
DE AltName: Full=RIO kinase 3;
GN Name=Riok3;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-127 AND SER-128, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-127; SER-128 AND
RP SER-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Involved in regulation of type I interferon (IFN)-dependent
CC immune response which plays a critical role in the innate immune
CC response against DNA and RNA viruses. May act as an adapter protein
CC essential for the recruitment of TBK1 to IRF3. Phosphorylates IFIH1 on
CC 'Ser-828' interfering with IFIH1 filament assembly on long dsRNA and
CC resulting in attenuated IFIH1-signaling. Can inhibit CASP10 isoform 7-
CC mediated activation of the NF-kappaB signaling pathway. May play a role
CC in the biogenesis of the 40S ribosomal subunit. Involved in the
CC processing of 21S pre-rRNA to the mature 18S rRNA.
CC {ECO:0000250|UniProtKB:O14730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with CASP10. Interacts with IRF3; RIOK3 probably
CC mediates the interaction of TBK1 with IRF3. Associated with 40S pre-
CC ribosomal particles. {ECO:0000250|UniProtKB:O14730}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14730}.
CC -!- PTM: Autophosphorylated (in vitro). {ECO:0000250|UniProtKB:O14730}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; AK004748; BAB23529.1; -; mRNA.
DR EMBL; AK147074; BAE27655.1; -; mRNA.
DR EMBL; BC033271; AAH33271.1; -; mRNA.
DR EMBL; CH466622; EDL01557.1; -; Genomic_DNA.
DR CCDS; CCDS29062.1; -.
DR RefSeq; NP_077144.2; NM_024182.4.
DR AlphaFoldDB; Q9DBU3; -.
DR SMR; Q9DBU3; -.
DR BioGRID; 211783; 2.
DR STRING; 10090.ENSMUSP00000025270; -.
DR iPTMnet; Q9DBU3; -.
DR PhosphoSitePlus; Q9DBU3; -.
DR EPD; Q9DBU3; -.
DR jPOST; Q9DBU3; -.
DR MaxQB; Q9DBU3; -.
DR PaxDb; Q9DBU3; -.
DR PRIDE; Q9DBU3; -.
DR ProteomicsDB; 253291; -.
DR Antibodypedia; 967; 198 antibodies from 30 providers.
DR DNASU; 66878; -.
DR Ensembl; ENSMUST00000025270; ENSMUSP00000025270; ENSMUSG00000024404.
DR GeneID; 66878; -.
DR KEGG; mmu:66878; -.
DR UCSC; uc008eby.1; mouse.
DR CTD; 8780; -.
DR MGI; MGI:1914128; Riok3.
DR VEuPathDB; HostDB:ENSMUSG00000024404; -.
DR eggNOG; KOG2269; Eukaryota.
DR GeneTree; ENSGT00940000157008; -.
DR HOGENOM; CLU_018693_5_0_1; -.
DR InParanoid; Q9DBU3; -.
DR OMA; IPRCGFK; -.
DR OrthoDB; 1238900at2759; -.
DR PhylomeDB; Q9DBU3; -.
DR TreeFam; TF105831; -.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 66878; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Riok3; mouse.
DR PRO; PR:Q9DBU3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9DBU3; protein.
DR Bgee; ENSMUSG00000024404; Expressed in blood and 270 other tissues.
DR ExpressionAtlas; Q9DBU3; baseline and differential.
DR Genevisible; Q9DBU3; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0089720; F:caspase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:1990786; P:cellular response to dsDNA; ISO:MGI.
DR GO; GO:0071359; P:cellular response to dsRNA; ISO:MGI.
DR GO; GO:0098586; P:cellular response to virus; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0030490; P:maturation of SSU-rRNA; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISO:MGI.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017406; Ser/Thr_kinase_Rio3.
DR PIRSF; PIRSF038146; Ser/Thr_PK_RIO3; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 1: Evidence at protein level;
KW Antiviral defense; ATP-binding; Cytoplasm; Immunity; Innate immunity;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ribosome biogenesis; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..519
FT /note="Serine/threonine-protein kinase RIO3"
FT /id="PRO_0000213530"
FT DOMAIN 251..519
FT /note="Protein kinase"
FT REGION 122..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 406
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 257..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14730"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14730"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18630941,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 141
FT /note="P -> T (in Ref. 1; BAB23529)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="I -> V (in Ref. 3; AAH33271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 58704 MW; 4DB90CAFA81C8AC7 CRC64;
MDLVGVSSPE PGPAAAWGPS KCPWATPQNT VSCSLTEVMS EELAKELQLE EEAAAFPEVV
VAEGPFISGE NIDTSSDLML AQMLQMEFDR EYDAQLRREE KKFNGDSKVS ISFENYRKVH
PFEDSDSSED EVDWQDTRDD PYRPAKPIPT PKKGFIGKGK DITTKHDEVV CGRKNTARME
NFAPGFQVGD GIGMDLKLSN HVFNALKQHA YSEERRSARL HEKKEHSTAE KAVDPKTRLL
MYKMVNSGML ETITGCISTG KESVVFHAYG GSLEDEKEDG KAIPTECAIK VFKTTLNEFK
NRDKYIKDDF RFKDRFSKLN PRKIIRMWAE KEMHNLTRMQ KAGIPCPTVV LLKKHILVMS
FIGHDQVPAP KLKEVKLSNE EMKDAYYQTL HLMQQLYNEC TLVHADLSEY NMLWHAGKVW
LIDVSQSVEP THPHGLEFLF RDCRNVSQFF QKGGVTEALN ERELFNAVSG LNISADNEAD
FLAEIEALEK MNEDHIQKNG RKAASFLKDD GSPPVLSAD
