KC1G_CAEEL
ID KC1G_CAEEL Reviewed; 407 AA.
AC Q8WQ99;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Casein kinase I gamma {ECO:0000303|PubMed:18694560};
DE Short=CKI-gamma {ECO:0000250|UniProtKB:P78368};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P78368};
GN Name=csnk-1 {ECO:0000312|WormBase:Y106G6E.6};
GN ORFNames=Y106G6E.6 {ECO:0000312|WormBase:Y106G6E.6};
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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18694560; DOI=10.1016/j.devcel.2008.06.002;
RA Panbianco C., Weinkove D., Zanin E., Jones D., Divecha N., Gotta M.,
RA Ahringer J.;
RT "A casein kinase 1 and PAR proteins regulate asymmetry of a PIP(2)
RT synthesis enzyme for asymmetric spindle positioning.";
RL Dev. Cell 15:198-208(2008).
CC -!- FUNCTION: Involved in the asymmetric cell division of the embryo
CC downstream of par-2 and par-3 by regulating the asymmetric cortical
CC distribution of pkk-1, a phosphatidylinositol 4,5-bisphosphate-
CC producing enzyme, which in turn regulates the asymmetrical distribution
CC of grp-1, grp-2 and lin-5. {ECO:0000269|PubMed:18694560}.
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:0000250|UniProtKB:P78368};
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:0000250|UniProtKB:P78368};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:18694560}. Cytoplasm {ECO:0000269|PubMed:18694560}.
CC Note=Cortical localization during all cell cycle stages. In the
CC cytoplasm, forms punctate structures around the asters during mitosis.
CC Enriched in the anterior region of the 1 cell-stage embryo.
CC {ECO:0000269|PubMed:18694560}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in 1-cell embryos results
CC in mislocalization of the pronuclei and the spindle towards the
CC anterior part of the embryo, spindle instability, and failure of
CC asymmetric cell division in 50 percent of embryos. In addition, spindle
CC pulling forces are increased. par-2 and par-3 mediated embryo polarity
CC is normal. Oocytes have increased cortical grp-1 and grp-2
CC localization. {ECO:0000269|PubMed:18694560}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR EMBL; AL032656; CAB60309.2; -; Genomic_DNA.
DR RefSeq; NP_492694.1; NM_060293.3.
DR AlphaFoldDB; Q8WQ99; -.
DR SMR; Q8WQ99; -.
DR STRING; 6239.Y106G6E.6; -.
DR EPD; Q8WQ99; -.
DR PaxDb; Q8WQ99; -.
DR PeptideAtlas; Q8WQ99; -.
DR PRIDE; Q8WQ99; -.
DR EnsemblMetazoa; Y106G6E.6.1; Y106G6E.6.1; WBGene00013709.
DR EnsemblMetazoa; Y106G6E.6.2; Y106G6E.6.2; WBGene00013709.
DR GeneID; 172891; -.
DR KEGG; cel:CELE_Y106G6E.6; -.
DR UCSC; Y106G6E.6.1; c. elegans.
DR CTD; 172891; -.
DR WormBase; Y106G6E.6; CE29604; WBGene00013709; csnk-1.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000160646; -.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; Q8WQ99; -.
DR OMA; HSTRKQH; -.
DR OrthoDB; 889559at2759; -.
DR PhylomeDB; Q8WQ99; -.
DR Reactome; R-CEL-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q8WQ99; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00013709; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005818; C:aster; IDA:WormBase.
DR GO; GO:0005938; C:cell cortex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP 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:0008356; P:asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0030590; P:first cell cycle pseudocleavage; IMP:UniProtKB.
DR GO; GO:0090217; P:negative regulation of 1-phosphatidylinositol-4-phosphate 5-kinase activity; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0032888; P:regulation of mitotic spindle elongation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051653; P:spindle localization; IMP:UniProtKB.
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 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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..407
FT /note="Casein kinase I gamma"
FT /id="PRO_0000432624"
FT DOMAIN 28..298
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 319..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 34..42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 407 AA; 46369 MW; FE8A4C3970ADE214 CRC64;
MTNTRGSNSA TSASTTNSQG VLMVGPNFKV GKKIGCGNFG ELRLGKNLYN NEHVAIKLEP
MKSKAPQLHL EYRFYKLLGQ AEGLPQVHYF GPCGKYNALV MELLGHSLED LFDLCDRHFS
LKTVAMVAMQ LIRRIEYVHT KHLIYRDVKP ENFLIGRYST RKQHVLHIID FGLAKEYIDC
DTGKHIAYRE HKSLTGTARY MSINTHLGKE QSRRDDLEAL GHMFMYFLRG SLPWQGLKAD
TLKERYQKIG DTKRQTAVEV LCEGFPDEFA QYLRYARRLD FFETPDYDFC YNLFKSVLDR
LGATYDYEFD WTPKLNNVST PSGSLHTSES KDVKRTDRGE LKVSQAAAHA QFGSTQVINS
NAGEVVEESR NTEGRTAAGD NSSGEVKCCC FRRRRRKHNN ATPATQK
