KC1G1_RAT
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 03-AUG-2022, entry version 156.
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.ENSRNOP00000048274; -.
DR PhosphoSitePlus; Q62761; -.
DR SwissPalm; Q62761; -.
DR PaxDb; Q62761; -.
DR Ensembl; ENSRNOT00000042369; ENSRNOP00000048274; ENSRNOG00000016620.
DR GeneID; 64086; -.
DR KEGG; rno:64086; -.
DR UCSC; RGD:621404; rat.
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; 889559at2759; -.
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 tissues.
DR ExpressionAtlas; Q62761; baseline and differential.
DR Genevisible; Q62761; RN.
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 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
