ID H2QEC3_PANTR Unreviewed; 519 AA.
AC H2QEC3; A0A2J8MPI1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Serine/threonine-protein kinase RIO3 {ECO:0000256|PIRNR:PIRNR038146};
DE EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR038146};
GN Name=RIOK3 {ECO:0000313|EMBL:JAA07005.1,
GN ECO:0000313|Ensembl:ENSPTRP00000016866.3,
GN ECO:0000313|VGNC:VGNC:13278};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000016866.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000016866.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:JAA07005.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA07005.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA39938.1}, Skin {ECO:0000313|EMBL:JAA31743.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA14401.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000016866.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|PIRNR:PIRNR038146}.
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 Evidence={ECO:0000256|ARBA:ARBA00001433,
CC ECO:0000256|PIRNR:PIRNR038146};
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; Evidence={ECO:0000256|ARBA:ARBA00000775,
CC ECO:0000256|PIRNR:PIRNR038146};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR038146};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000256|ARBA:ARBA00009196,
CC ECO:0000256|PIRNR:PIRNR038146}.
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DR EMBL; AACZ04065262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GABC01004333; JAA07005.1; -; mRNA.
DR EMBL; GABF01007744; JAA14401.1; -; mRNA.
DR EMBL; GABF01007743; JAA14402.1; -; mRNA.
DR EMBL; GABF01007742; JAA14403.1; -; mRNA.
DR EMBL; GABF01007741; JAA14404.1; -; mRNA.
DR EMBL; GABD01001357; JAA31743.1; -; mRNA.
DR EMBL; GABD01001356; JAA31744.1; -; mRNA.
DR EMBL; GABE01004801; JAA39938.1; -; mRNA.
DR EMBL; GABE01004800; JAA39939.1; -; mRNA.
DR EMBL; GABE01004799; JAA39940.1; -; mRNA.
DR RefSeq; XP_523888.2; XM_523888.6.
DR STRING; 9598.ENSPTRP00000093465; -.
DR PaxDb; 9598-ENSPTRP00000016866; -.
DR Ensembl; ENSPTRT00000018210.4; ENSPTRP00000016866.3; ENSPTRG00000009918.5.
DR GeneID; 468499; -.
DR CTD; 8780; -.
DR VGNC; VGNC:13278; RIOK3.
DR eggNOG; KOG2269; Eukaryota.
DR GeneTree; ENSGT00940000157008; -.
DR HOGENOM; CLU_018693_5_0_1; -.
DR OMA; HDPQLCA; -.
DR OrthoDB; 5481355at2759; -.
DR TreeFam; TF105831; -.
DR Proteomes; UP000002277; Chromosome 18.
DR Bgee; ENSPTRG00000009918; Expressed in bone marrow and 21 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05146; RIO3_euk; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR45723; SERINE/THREONINE-PROTEIN KINASE RIO1; 1.
DR PANTHER; PTHR45723:SF1; SERINE_THREONINE-PROTEIN KINASE RIO3; 1.
DR Pfam; PF01163; RIO1; 1.
DR PIRSF; PIRSF038146; Ser/Thr_PK_RIO3; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS01245; RIO1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Immunity {ECO:0000256|PIRNR:PIRNR038146};
KW Innate immunity {ECO:0000256|PIRNR:PIRNR038146};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038146};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR038146};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR038146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR038146};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW ECO:0000256|PIRNR:PIRNR038146};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038146}.
FT DOMAIN 222..470
FT /note="RIO kinase"
FT /evidence="ECO:0000259|SMART:SM00090"
FT REGION 121..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 519 AA; 59107 MW; BEA87612F5A2BB89 CRC64;
MDLVGVASPE PGTAAAWGPS KCPWAIPQNT ISCSLADVMS EQLAKELQLE EEAAIFPEVA
VAEGPFITGE NIDTSSDLML AQMLQMEYDR EYDAQLRREE KKFNGDSKVS ISFENYRKVH
PYEDSDSSED EVDWQDTRDD PYRPAKPVPT PKKGFIGKGK DITTKHDEVV CGRKNTARME
NFAPEFQVGD GIGMDLKLSN HVFNALKQHA YSEERRSARL HEKKEHSTAE KAVDPKTRLL
MYKMVNSGML ETITGCISTG KESVVFHAYG GSMEDEKEDS KVIPTECAIK VFKTTLNEFK
NRDKYIKDDF RFKDRFSKLN PRKIIRMWAE KEMHNLARMQ RAGIPCPTVV LLKKHILVMS
FIGHDQVPAP KLKEVKLNSE EMKEAYYQTL HLMRQLYHEC TLVHADLSEY NMLWHAGKVW
LIDVSQSVEP THPHGLEFLF RDCRNVSQFF QKGGVKEALS ERELFNAVSG LNITADNEAD
FLAEIEALEK MNEDHVQKNG RKAASFLKDD GDPPLLYDE
//
