RIOK3_BOVIN
ID RIOK3_BOVIN Reviewed; 519 AA.
AC Q1RMT7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Serine/threonine-protein kinase RIO3;
DE EC=2.7.11.1;
DE AltName: Full=RIO kinase 3;
GN Name=RIOK3;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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
CC within the C-terminal region interfering with IFIH1 filament assembly
CC on long dsRNA and resulting in attenuated IFIH1-signaling. Can inhibit
CC CASP10 isoform 7-mediated activation of the NF-kappaB signaling
CC pathway. May play a role in the biogenesis of the 40S ribosomal
CC subunit. Involved in the processing of 21S pre-rRNA to the mature 18S
CC rRNA. {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; BC114721; AAI14722.1; -; mRNA.
DR RefSeq; NP_001069304.1; NM_001075836.1.
DR AlphaFoldDB; Q1RMT7; -.
DR SMR; Q1RMT7; -.
DR STRING; 9913.ENSBTAP00000013242; -.
DR PaxDb; Q1RMT7; -.
DR PRIDE; Q1RMT7; -.
DR Ensembl; ENSBTAT00000013242; ENSBTAP00000013242; ENSBTAG00000010042.
DR GeneID; 522917; -.
DR KEGG; bta:522917; -.
DR CTD; 8780; -.
DR VEuPathDB; HostDB:ENSBTAG00000010042; -.
DR VGNC; VGNC:49977; RIOK3.
DR eggNOG; KOG2269; Eukaryota.
DR GeneTree; ENSGT00940000157008; -.
DR HOGENOM; CLU_018693_5_0_1; -.
DR InParanoid; Q1RMT7; -.
DR OMA; IPRCGFK; -.
DR OrthoDB; 1238900at2759; -.
DR TreeFam; TF105831; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000010042; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0089720; F:caspase binding; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:1990786; P:cellular response to dsDNA; IEA:Ensembl.
DR GO; GO:0071359; P:cellular response to dsRNA; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0039534; P:negative regulation of MDA-5 signaling pathway; IEA:Ensembl.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
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 2: Evidence at transcript 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_0000247807"
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 122
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14730"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBU3"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14730"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14730"
SQ SEQUENCE 519 AA; 58928 MW; 8DB7217FD5FE4740 CRC64;
MDLVRVASPE PGPAAAWGPN KCPWATPQNT ISCSLSDVMS EQLAKELQLE EEAAAFPEVT
VAEGPFITGE NIDTSSDLML AQMLQMEFDR EYDAQLRREE KKFNGDSKVC ISFENYRKVH
PYEDSDSSED EVDWQDTRDD PYRPAKPIPT PKKGFIGKGK DITTKHDEVV CGRKNTARME
NFAPGFQVGD GIGMDLKLSN HVFNALKQHA YSEERRSARL HEKKEHSTAE KAVDPKTRLL
MYKMVNSGML ETITGCISTG KESVVFHAYG GSMEDGKEDS KVIPTECAIK VFKTTLNEFK
NRDKYIKDDF RFKDRFSKLN PRKIIRMWAE KEMHNLTRMQ RAGIPCPTVV LLKKHILVMS
FIGHDQVPAP KLKEVKLSSE EMKDAYYQTL HLMQQLYDEC TLVHADLSEY NMLWHAGKVW
LIDVSQSVEP THPHGLEFLF RDCRNVSQFF QKGGVKEALG ERELFNAVSG LNISADNEAD
FLAEIEALEK MNEDHVQKNG RKAASFLKDD GGPPILYDE
