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   24-JAN-2024, entry version 172.
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. SMAD3 phosphorylation
CC       promotes its ligand-dependent ubiquitination and subsequent proteasome
CC       degradation, thus inhibiting SMAD3-mediated TGF-beta responses.
CC       Hyperphosphorylation of the serine-repeat motif of COL4A3BP/CERT leads
CC       to its inactivation by dissociation from the Golgi complex, thus down-
CC       regulating ER-to-Golgi transport of ceramide and sphingomyelin
CC       synthesis. Triggers PER1 proteasomal degradation probably through
CC       phosphorylation (By similarity). Involved in brain development and
CC       vesicular trafficking and neurotransmitter releasing from small
CC       synaptic vesicles. Regulates fast synaptic transmission mediated by
CC       glutamate (By similarity). Involved in regulation of reactive oxygen
CC       species (ROS) levels (By similarity). {ECO:0000250|UniProtKB:P48729,
CC       ECO:0000250|UniProtKB:P78368, ECO:0000250|UniProtKB:Q8BVP5}.
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.
CC       {ECO:0000250|UniProtKB:P78368}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with MTA1 (short isoform)
CC       in the cytoplasm (By similarity). Interacts with SMAD3 (By similarity).
CC       Interacts with DUOXA2 (By similarity). {ECO:0000250|UniProtKB:P48730,
CC       ECO:0000250|UniProtKB:P78368}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000250|UniProtKB:P78368}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P78368}.
CC   -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:7759525}.
CC   -!- DOMAIN: The phospho-regulated basic and hydrophobic (PRBH) motif is
CC       sufficient and important for interaction with phospholipids permitting
CC       cortical localization. Phosphorylation of the PRBH motif by aPKC
CC       inhibits the association of the protein with the cortical membrane.
CC       {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.ENSRNOP00000072196; -.
DR   PhosphoSitePlus; Q62762; -.
DR   SwissPalm; Q62762; -.
DR   jPOST; Q62762; -.
DR   PaxDb; 10116-ENSRNOP00000025266; -.
DR   Ensembl; ENSRNOT00000080342.2; ENSRNOP00000072196.1; ENSRNOG00000018529.8.
DR   Ensembl; ENSRNOT00055055292; ENSRNOP00055045663; ENSRNOG00055031957.
DR   Ensembl; ENSRNOT00060052517; ENSRNOP00060043689; ENSRNOG00060030231.
DR   Ensembl; ENSRNOT00065031018; ENSRNOP00065024705; ENSRNOG00065018469.
DR   GeneID; 65278; -.
DR   KEGG; rno:65278; -.
DR   UCSC; RGD:621407; rat.
DR   AGR; RGD:621407; -.
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   OrthoDB; 1534388at2759; -.
DR   PhylomeDB; Q62762; -.
DR   BRENDA; 2.7.11.1; 5301.
DR   PRO; PR:Q62762; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000018529; Expressed in testis and 20 other cell types or tissues.
DR   ExpressionAtlas; Q62762; baseline and differential.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd14126; STKc_CK1_gamma; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR11909:SF157; CASEIN KINASE I ISOFORM GAMMA-2; 1.
DR   PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR   Pfam; PF12605; CK1gamma_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q62762; RN.
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
//