KC1G3_RAT
ID KC1G3_RAT Reviewed; 448 AA.
AC Q62763;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Casein kinase I isoform gamma-3;
DE Short=CKI-gamma 3;
DE EC=2.7.11.1;
GN Name=Csnk1g3;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity).
CC {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 -!- TISSUE SPECIFICITY: Expressed in testis, brain, heart, kidney, lung,
CC liver and muscle.
CC -!- PTM: Autophosphorylated.
CC -!- MISCELLANEOUS: Triazolodiamine 1 is a commercial name for 5-amino-3-
CC ([4-(aminosulfonyl)phenyl]amino)-N-(2,6-difluorophenyl)-1H-1,2,4-
CC triazole-1-carbothioamide.
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; U22321; AAC52202.1; -; mRNA.
DR PIR; C56711; C56711.
DR RefSeq; NP_074046.1; NM_022855.2.
DR AlphaFoldDB; Q62763; -.
DR SMR; Q62763; -.
DR BioGRID; 249201; 1.
DR STRING; 10116.ENSRNOP00000022792; -.
DR PhosphoSitePlus; Q62763; -.
DR SwissPalm; Q62763; -.
DR jPOST; Q62763; -.
DR PaxDb; Q62763; -.
DR PRIDE; Q62763; -.
DR Ensembl; ENSRNOT00000103210; ENSRNOP00000093418; ENSRNOG00000016677.
DR GeneID; 64823; -.
DR KEGG; rno:64823; -.
DR UCSC; RGD:621408; rat.
DR CTD; 1456; -.
DR RGD; 621408; Csnk1g3.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000160646; -.
DR InParanoid; Q62763; -.
DR OrthoDB; 889559at2759; -.
DR PhylomeDB; Q62763; -.
DR TreeFam; TF313349; -.
DR BRENDA; 2.7.11.1; 5301.
DR PRO; PR:Q62763; -.
DR Proteomes; UP000002494; Chromosome 18.
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 Acetylation; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..448
FT /note="Casein kinase I isoform gamma-3"
FT /id="PRO_0000192847"
FT DOMAIN 43..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M4"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M4"
SQ SEQUENCE 448 AA; 51429 MW; 6065DEC2D98B3087 CRC64;
MDNKKKDKDK SDDRMARPSG RSGHSTRGTG SSSSGVLMVG PNFRVGKKIG CGNFGELRLG
KNLYTNEYVA IKLEPMKSRA PQLHLEYRFY KQLGSGDGIP QVYYFGPCGK YNAMVLELLG
PSLEDLFDLC DRTFSLKTVL MIAIQLISRM EYVHSKNLIY RDVKPENFLI GRPGNKAQQV
IHIIDFGLAK EYIDPETKKH IPYREHKSLT GTARYMSINT HLGKEQSRRD DLEALGHMFM
YFLRGSLPWQ GLKADTLKER YQKIGDTKRA TPIEVLCENF PEEMATYLRY VRRLDFFEKP
DYDYLRKLFT DLFDRKGYMF DYEYDWIGKQ LPTPVGAVQQ DPALSSNREA HQHRDKIQQS
KNQSADHRAA WDSQQANPHH LRAHLAADRH GGSVQVVSST NGELNTDDPT AGRSNAPITA
PTEVEVMDET KCCCFFKRRK RKTIQRHK
