KC1G2_RAT
ID KC1G2_RAT Reviewed; 415 AA.
AC Q62762; Q6IMY5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Casein kinase I isoform gamma-2;
DE Short=CKI-gamma 2;
DE EC=2.7.11.1;
GN Name=Csnk1g2; Synonyms=Ck1g2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
RC TISSUE=Testis;
RX PubMed=7759525; DOI=10.1074/jbc.270.21.12717;
RA Zhai L., Graves P.R., Robinson L.C., Italiano M., Culbertson M.R.,
RA Rowles J., Cobb M.H., Depaoli-Roach A.A., Roach P.J.;
RT "Casein kinase I gamma subfamily. Molecular cloning, expression, and
RT characterization of three mammalian isoforms and complementation of defects
RT in the Saccharomyces cerevisiae YCK genes.";
RL J. Biol. Chem. 270:12717-12724(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Serine/threonine-protein kinase. Casein kinases are
CC operationally defined by their preferential utilization of acidic
CC proteins such as caseins as substrates. It can phosphorylate a large
CC number of proteins. Participates in Wnt signaling (By similarity).
CC Phosphorylates COL4A3BP/CERT, MTA1 and SMAD3. Involved in brain
CC development and vesicular trafficking and neurotransmitter releasing
CC from small synaptic vesicles. Regulates fast synaptic transmission
CC mediated by glutamate. SMAD3 phosphorylation promotes its ligand-
CC dependent ubiquitination and subsequent proteasome degradation, thus
CC inhibiting SMAD3-mediated TGF-beta responses. Hyperphosphorylation of
CC the serine-repeat motif of COL4A3BP/CERT leads to its inactivation by
CC dissociation from the Golgi complex, thus down-regulating ER-to-Golgi
CC transport of ceramide and sphingomyelin synthesis. Triggers PER1
CC proteasomal degradation probably through phosphorylation (By
CC similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Stimulated by estrogen. {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with MTA1 (short isoform) in the cytoplasm.
CC Interacts with SMAD3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:P78368}. Cytoplasm
CC {ECO:0000250|UniProtKB:P78368}.
CC -!- TISSUE SPECIFICITY: Testis.
CC -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC sufficient and important for interaction with phospholipids permitting
CC cortical localization (By similarity). Phosphorylation of the PRBH
CC motif by aPKC inhibits the association of the protein with the cortical
CC membrane (By similarity). {ECO:0000250|UniProtKB:P78368}.
CC -!- PTM: Autophosphorylated (PubMed:7759525). Phosphorylated by aPKC which
CC promotes dissociation from the cell cortex (By similarity).
CC {ECO:0000250|UniProtKB:P78368, ECO:0000269|PubMed:7759525}.
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; U22297; AAC52201.1; -; mRNA.
DR EMBL; BC072533; AAH72533.1; -; mRNA.
DR PIR; B56711; B56711.
DR RefSeq; NP_001029042.1; NM_001033870.1.
DR RefSeq; NP_075590.2; NM_023102.2.
DR RefSeq; XP_006241064.1; XM_006241002.3.
DR AlphaFoldDB; Q62762; -.
DR SMR; Q62762; -.
DR STRING; 10116.ENSRNOP00000025266; -.
DR SwissPalm; Q62762; -.
DR jPOST; Q62762; -.
DR PaxDb; Q62762; -.
DR PRIDE; Q62762; -.
DR Ensembl; ENSRNOT00000080342; ENSRNOP00000072196; ENSRNOG00000018529.
DR GeneID; 65278; -.
DR KEGG; rno:65278; -.
DR UCSC; RGD:621407; rat.
DR CTD; 1455; -.
DR RGD; 621407; Csnk1g2.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000156470; -.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; Q62762; -.
DR OMA; HSTRKQH; -.
DR OrthoDB; 889559at2759; -.
DR PhylomeDB; Q62762; -.
DR BRENDA; 2.7.11.1; 5301.
DR Reactome; R-RNO-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:Q62762; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000018529; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q62762; baseline and differential.
DR Genevisible; Q62762; RN.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IDA:RGD.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR022247; Casein_kinase-1_gamma_C.
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; PF12605; CK1gamma_C; 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; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1..415
FT /note="Casein kinase I isoform gamma-2"
FT /id="PRO_0000192844"
FT DOMAIN 46..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..415
FT /note="Phospho-regulated basic and hydrophobic (PRBH)
FT motif"
FT /evidence="ECO:0000250|UniProtKB:P78368"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 52..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 75
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 59..60
FT /note="EL -> DV (in Ref. 1; AAC52201)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="Missing (in Ref. 1; AAC52201)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 47636 MW; 6BE480CE200FBEBB CRC64;
MDFDKKGGKG ELEEGRRMSK TGTNRSNHGV RNSGTSSGVL MVGPNFRVGK KIGCGNFGEL
RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSTTE GVPQVYYFGP CGKYNAMVLE
LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI TRMEYVHTKS LIYRDVKPEN FLVGRPGSKR
QHSIHIIDFG LAKEYIDPET KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH
MFMYFLRGSL PWQGLKADTL KERYQKIGDT KRATPIEVLC ESFPEEMATY LRYVRRLDFF
EKPDYDYLRK LFTDLFDRSG YVFDYEYDWA GKPLPTPIGT VHPDVPSQPP HRDKAQLHTK
NQALNSTNGE LNTDDPTAGH SNAPIAAPAE VEVADETKCC CFFKRRKRKS LQRHK
