CSK2A_CAEEL
ID CSK2A_CAEEL Reviewed; 360 AA.
AC P18334;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II subunit alpha;
DE EC=2.7.11.1;
GN Name=kin-3; ORFNames=B0205.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2318883; DOI=10.1016/s0021-9258(19)34086-4;
RA Hu E., Rubin C.S.;
RT "Casein kinase II from Caenorhabditis elegans. Properties and developmental
RT regulation of the enzyme; cloning and sequence analyses of cDNA and the
RT gene for the catalytic subunit.";
RL J. Biol. Chem. 265:5072-5080(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16481400; DOI=10.1091/mbc.e05-10-0935;
RA Hu J., Bae Y.-K., Knobel K.M., Barr M.M.;
RT "Casein kinase II and calcineurin modulate TRPP function and ciliary
RT localization.";
RL Mol. Biol. Cell 17:2200-2211(2006).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. The alpha chain contains the catalytic site. May
CC participate in Wnt signaling. Modulates two aspects of male mating
CC behavior; response to hermaphrodite contact and vulval location, acting
CC in the same pathway as lov-1 and pkd-2. {ECO:0000269|PubMed:16481400}.
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 -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC -!- INTERACTION:
CC P18334; P28548: kin-10; NbExp=5; IntAct=EBI-367861, EBI-317777;
CC P18334; Q11184: let-756; NbExp=3; IntAct=EBI-367861, EBI-3843983;
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:16481400}. Cell projection, cilium
CC {ECO:0000269|PubMed:16481400}. Cell projection, dendrite
CC {ECO:0000269|PubMed:16481400}. Perikaryon
CC {ECO:0000269|PubMed:16481400}. Note=Enriched in cilia in male sensory
CC neurons.
CC -!- TISSUE SPECIFICITY: Expressed in a subset of the adult male sensory
CC neurons: CEM head neurons, ray RnB neurons, and hook HOB tail neurons.
CC {ECO:0000269|PubMed:16481400}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; J05274; AAA27984.1; -; Genomic_DNA.
DR EMBL; FO080112; CCD61302.1; -; Genomic_DNA.
DR PIR; A35562; A35562.
DR RefSeq; NP_492811.1; NM_060410.4.
DR AlphaFoldDB; P18334; -.
DR SMR; P18334; -.
DR BioGRID; 38389; 23.
DR IntAct; P18334; 5.
DR STRING; 6239.B0205.7; -.
DR EPD; P18334; -.
DR PaxDb; P18334; -.
DR PeptideAtlas; P18334; -.
DR PRIDE; P18334; -.
DR EnsemblMetazoa; B0205.7.1; B0205.7.1; WBGene00002191.
DR GeneID; 172978; -.
DR KEGG; cel:CELE_B0205.7; -.
DR UCSC; B0205.7; c. elegans.
DR CTD; 172978; -.
DR WormBase; B0205.7; CE17321; WBGene00002191; kin-3.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; P18334; -.
DR OMA; FQSYDYS; -.
DR OrthoDB; 1098380at2759; -.
DR PhylomeDB; P18334; -.
DR BRENDA; 2.7.11.1; 1045.
DR Reactome; R-CEL-1483191; Synthesis of PC.
DR Reactome; R-CEL-201688; WNT mediated activation of DVL.
DR Reactome; R-CEL-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR Reactome; R-CEL-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-CEL-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-CEL-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR PRO; PR:P18334; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00002191; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0097730; C:non-motile cilium; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:CAFA.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:CAFA.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0034606; P:response to hermaphrodite contact; IMP:WormBase.
DR GO; GO:0034608; P:vulval location; IMP:WormBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR InterPro; IPR045216; CK2_alpha.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24054; PTHR24054; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Behavior; Cell projection; Cilium; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..360
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085898"
FT DOMAIN 38..323
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 334..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 360 AA; 42257 MW; B98DF039F6B566FA CRC64;
MPPIPSRARV YAEVNPSRPR EYWDYEAHMI EWGQIDDYQL VRKLGRGKYS EVFEGFKMST
DEKVVVKILK PVKKKKIKRE IKILENLRGG TNIITLLDVV KDPISRTPAL IFEHVNNSDF
KQLYQTLSDY DIRYYLYELL KALDFCHSQG IMHRDVKPHN VMIDAEKREL RLIDWGLAEF
YHPRQDYNVR VASRYFKGPE LLVDYQCYDY SLDMWSLGCM LASMIFRKEP FFHGHDNYDQ
LVRIAKVLGT DELYEYIARY HIDLDPRFND ILGRHSRKRW ERFIHAENQH LVTPEALDFL
DKLLRYDHAE RLTAQEAMGH EYFRPVVEAH ARANGTEQAD GQGASNSASS QSSDAKIDGA
