ID   KC1G1_RAT               Reviewed;         390 AA.
AC   Q62761;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Casein kinase I isoform gamma-1;
DE            Short=CKI-gamma 1;
DE            EC=2.7.11.1;
GN   Name=Csnk1g1;
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].
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=Testis;
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. Regulates fast
CC       synaptic transmission mediated by glutamate. Phosphorylates CLSPN (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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Autophosphorylated.
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; U22296; AAC52200.1; -; mRNA.
DR   EMBL; BC078831; AAH78831.1; -; mRNA.
DR   PIR; A56711; A56711.
DR   RefSeq; NP_071624.1; NM_022288.1.
DR   RefSeq; XP_017451381.1; XM_017595892.1.
DR   AlphaFoldDB; Q62761; -.
DR   SMR; Q62761; -.
DR   BioGRID; 248970; 1.
DR   STRING; 10116.ENSRNOP00000074148; -.
DR   PhosphoSitePlus; Q62761; -.
DR   SwissPalm; Q62761; -.
DR   PaxDb; 10116-ENSRNOP00000048274; -.
DR   Ensembl; ENSRNOT00000042369.4; ENSRNOP00000048274.2; ENSRNOG00000016620.7.
DR   Ensembl; ENSRNOT00055043403; ENSRNOP00055035401; ENSRNOG00055025170.
DR   Ensembl; ENSRNOT00060030964; ENSRNOP00060025071; ENSRNOG00060018022.
DR   GeneID; 64086; -.
DR   KEGG; rno:64086; -.
DR   UCSC; RGD:621404; rat.
DR   AGR; RGD:621404; -.
DR   CTD; 53944; -.
DR   RGD; 621404; Csnk1g1.
DR   eggNOG; KOG1165; Eukaryota.
DR   GeneTree; ENSGT00940000155628; -.
DR   HOGENOM; CLU_019279_2_0_1; -.
DR   InParanoid; Q62761; -.
DR   OrthoDB; 1534388at2759; -.
DR   BRENDA; 2.7.11.1; 5301.
DR   PRO; PR:Q62761; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000016620; Expressed in testis and 18 other cell types or tissues.
DR   ExpressionAtlas; Q62761; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; 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:SF156; CASEIN KINASE I ISOFORM GAMMA-1; 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; Q62761; RN.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Wnt signaling pathway.
FT   CHAIN           1..390
FT                   /note="Casein kinase I isoform gamma-1"
FT                   /id="PRO_0000192841"
FT   DOMAIN          44..315
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         50..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCP0"
SQ   SEQUENCE   390 AA;  45127 MW;  8B9D8F5952D40762 CRC64;
     MDHSNREKDD RQRTTKTMAQ RNTHCSRPSG TSTSSGVLMV GPNFRVGKKI GCGNFGELRL
     GKNLYTNEYV AIKLEPIKSR APQLHLEYRF YKQLGSAGEG LPQVYYFGPC GKYNAMVLEL
     LGPSLEDLFD LCDRTFTLKT VLMIAIQLLS RMEYVHSKNL IYRDVKPENF LIGRQGNKKE
     HVIHIIDFGL AKEYIDPETK KHIPYREHKS LTGTARYMSI NTHLGKEQSR RDDLEALGHM
     FMYFLRGSLP WQGLKADTLK ERYQKIGDTK RSTPIEALCE NFPEEMMTYL RYVRRLDFFE
     KPDYEYLRNL FTDLFERKGY TFDYAYDWVG RPIPTPVGSV HVDSGASAIT RESHTHRDRP
     SQQQPLRNQP RSLTAEWFVL APLSHPPAPT
//