ID KC1G1_MACFA Reviewed; 381 AA.
AC Q4R9A9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=Casein kinase I isoform gamma-1;
DE Short=CKI-gamma 1;
DE EC=2.7.11.1;
GN Name=CSNK1G1; ORFNames=QtsA-10381;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
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; AB168187; BAE00312.1; -; mRNA.
DR AlphaFoldDB; Q4R9A9; -.
DR SMR; Q4R9A9; -.
DR STRING; 9541.ENSMFAP00000005479; -.
DR Ensembl; ENSMFAT00000024162.2; ENSMFAP00000005485.2; ENSMFAG00000002355.2.
DR eggNOG; KOG1165; Eukaryota.
DR GeneTree; ENSGT00940000155628; -.
DR Proteomes; UP000233100; Chromosome 7.
DR Bgee; ENSMFAG00000002355; Expressed in thymus and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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.
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..381
FT /note="Casein kinase I isoform gamma-1"
FT /id="PRO_0000364342"
FT DOMAIN 44..315
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..381
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..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
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 381 AA; 43986 MW; A02218007977CCCB CRC64;
MDHPSREKDE RQRTTKPMAQ RSAHCSRPSG SSSSSGVLMV GPNFRVGKKI GCGNFGELRL
GKNLYTNEYV AIKLEPIKSR APQLHLEYRF YKQLGSAGEG LPQVYYFGPC GKYNAMVLEL
LGPSLEDLFD LCDRTFTLKT VLMIAIQLLS RMEYVHSKNL IYRDVKPENF LIGRQGNKKE
HVIHIIDFGL AKEYIDPETK KHIPYREHKS LTGTARYMSI NTHLGKEQSR RDDLEALGHM
FMYFLRGSLP WQGLKADTLK ERYQKIGDTK RNTPIEALCE NFPEEMATYL RYVRRLDFFE
KPDYEYLRTL FTDLFEKKGY TFDYAYDWVG RPIPTPVGSV HVDSGASAIT RESHTHRDRP
SQQQPLRNQF SSSTNQTSNL K
//
