RIOK1_CAEEL
ID RIOK1_CAEEL Reviewed; 506 AA.
AC O44959;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 5.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Serine/threonine-protein kinase RIO1 {ECO:0000255|PIRNR:PIRNR038147};
DE EC=2.7.11.1 {ECO:0000255|PIRNR:PIRNR038147};
GN Name=riok-1 {ECO:0000312|WormBase:M01B12.5a};
GN ORFNames=M01B12.5 {ECO:0000312|WormBase:M01B12.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24929033; DOI=10.1016/j.gep.2014.05.005;
RA Weinberg F., Schulze E., Fatouros C., Schmidt E., Baumeister R.,
RA Brummer T.;
RT "Expression pattern and first functional characterization of riok-1 in
RT Caenorhabditis elegans.";
RL Gene Expr. Patterns 15:124-134(2014).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25688864; DOI=10.1371/journal.pone.0117444;
RA Mendes T.K., Novakovic S., Raymant G., Bertram S.E., Esmaillie R.,
RA Nadarajan S., Breugelmans B., Hofmann A., Gasser R.B., Colaiacovo M.P.,
RA Boag P.R.;
RT "Investigating the role of RIO protein kinases in Caenorhabditis elegans.";
RL PLoS ONE 10:E0117444-E0117444(2015).
CC -!- FUNCTION: Involved in the final steps of cytoplasmic maturation of the
CC 40S ribosomal subunit (By similarity). Despite the protein kinase
CC domain is proposed to act predominantly as an ATPase (By similarity).
CC The catalytic activity regulates its dynamic association with the 40S
CC subunit (By similarity). Plays a role in oogenesis by regulating germ
CC cell proliferation, progression through diplotene and diakinesis stages
CC and oocyte maturation (PubMed:24929033, PubMed:25688864). Regulates
CC germline development probably by regulating the phosphorylation of mpk-
CC 1 (PubMed:25688864). Involved in larval development (PubMed:24929033,
CC PubMed:25688864). {ECO:0000250|UniProtKB:G0S3J5,
CC ECO:0000250|UniProtKB:Q12196, ECO:0000250|UniProtKB:Q9BRS2,
CC ECO:0000269|PubMed:24929033, ECO:0000269|PubMed:25688864}.
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:0000255|PIRNR:PIRNR038147};
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:0000255|PIRNR:PIRNR038147};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in vulva and uterine cells, uterine seam
CC cells (utse), spermatheca and in the nervous system including
CC chemosensory neurons in the head, nerve ring neurons (RID/RIF),
CC inhibitory motor neurons (DA/DD/VA/VD), mechanosensory neurons
CC (ALML/PLML) and tail sensory neurons (DVA//PDA) (PubMed:24929033,
CC PubMed:25688864). Also expressed in intestine and pharynx (procorpus)
CC and rectal valve and gland (PubMed:25688864).
CC {ECO:0000269|PubMed:24929033, ECO:0000269|PubMed:25688864}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the nervous system at all larval
CC stages. Expressed in somatic gonad and in the ventral nerve cord at L2
CC larval stage. Expressed in somatic gonad, in ventral uterine (VU/AC)
CC cells and in the committed anchor cell at L3 larval stage. Expressed in
CC vulF cells of the vulva, uterine cells and in uterine seam cells (utse)
CC at L4 larval stage. {ECO:0000269|PubMed:24929033}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes early larval
CC arrest. In adults, results in sterility. Causes malformations of the
CC gonad arms (empty or misshaped) and a protruding vulva
CC (PubMed:24929033). Abnormal germline development characterized by a
CC decrease in the number of proliferating germ cells in the mitotic and
CC transition zones. At the diplotene stage, cells are disorganized and
CC have enlarged nuclei. Oocytes have abnormal shape and large DNA
CC aggregates next to abnormally located sperm. In addition, 50 percent of
CC cells fails to decrease mpk-1 phosphorylation upon pachytene stage exit
CC (PubMed:24929033, PubMed:25688864). RNAi-mediated knockdown in a let-60
CC n1046 mutant background suppresses the formation of multivulva
CC (PubMed:24929033). {ECO:0000269|PubMed:24929033,
CC ECO:0000269|PubMed:25688864}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type Ser/Thr
CC kinase family. {ECO:0000305}.
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DR EMBL; BX284601; CCD67367.1; -; Genomic_DNA.
DR PIR; T33172; T33172.
DR RefSeq; NP_001021570.2; NM_001026399.7.
DR AlphaFoldDB; O44959; -.
DR SMR; O44959; -.
DR STRING; 6239.M01B12.5a.1; -.
DR EPD; O44959; -.
DR PaxDb; O44959; -.
DR PeptideAtlas; O44959; -.
DR PRIDE; O44959; -.
DR EnsemblMetazoa; M01B12.5a.1; M01B12.5a.1; WBGene00019698.
DR EnsemblMetazoa; M01B12.5a.2; M01B12.5a.2; WBGene00019698.
DR GeneID; 171883; -.
DR KEGG; cel:CELE_M01B12.5; -.
DR UCSC; M01B12.5a; c. elegans.
DR CTD; 171883; -.
DR WormBase; M01B12.5a; CE30555; WBGene00019698; riok-1.
DR eggNOG; KOG2270; Eukaryota.
DR GeneTree; ENSGT00940000157075; -.
DR HOGENOM; CLU_018693_4_3_1; -.
DR InParanoid; O44959; -.
DR OMA; QEINGCI; -.
DR OrthoDB; 1238900at2759; -.
DR PhylomeDB; O44959; -.
DR PRO; PR:O44959; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00019698; Expressed in embryo and 4 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0007281; P:germ cell development; IMP:WormBase.
DR GO; GO:0036093; P:germ cell proliferation; IMP:WormBase.
DR GO; GO:0008406; P:gonad development; IMP:WormBase.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IGI:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IGI:WormBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000687; RIO_kinase.
DR InterPro; IPR018935; RIO_kinase_CS.
DR InterPro; IPR017407; Ser/Thr_kinase_Rio1.
DR PIRSF; PIRSF038147; Ser/Thr_PK_RIO1; 1.
DR SMART; SM00090; RIO; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01245; RIO1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Hydrolase; Kinase; Magnesium; Meiosis;
KW Metal-binding; Nucleotide-binding; Reference proteome; Ribosome biogenesis;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..506
FT /note="Serine/threonine-protein kinase RIO1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434605"
FT DOMAIN 142..506
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 22..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..506
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 302
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 148..156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9BRS2"
SQ SEQUENCE 506 AA; 58664 MW; 96B856532CC0D64E CRC64;
MEKVEHLNLN IQNILEDVDI DTASSSSDDE PEQAVVKQEK LEAGEQIEEQ YDTDSDYDDD
IVEFAEATGD FTKKLNAARL NTIGPNAARN RLTVDVERHA DTSEDRKRKR VKDRADRATV
EQVLDPRTRL VLFRLLQRGT LLNIDGCIST GKEANVYHAT GTDNDLAIKI YKTSILTFKD
RERYVTGEFR YRHGYCKSNP RKMVAVWAEK EMRNLARMHE VGLPVPKPHL LKGHVLVMDF
LGKDGWPAPL LKNANLSQED AEPMYVGLVR DMRRLYRECK LVHADLSEFN MLVHDGKLWI
IDVSQSVEQD HPHALEFLRM DCNNVNKFFR ELGVPVLSVR RLFEVIVDPL MSSKEMETII
EEERVLVNSE DDSLFMNAFI PHKLEHVLHF ERDGKLAKEG VEANNPFQNI VSKIDLKGDG
FGEEHDDSDD NDDEENGKKS RKKRAEPTEE EIQEKERKIA MHTRNREETA EERKERKAAV
KEEKREQRKE KIPKHLKKRA HRQHMK
