KC1G3_BOVIN
ID KC1G3_BOVIN Reviewed; 276 AA.
AC P35509;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Casein kinase I isoform gamma-3;
DE Short=CKI-gamma 3;
DE EC=2.7.11.1;
DE Flags: Fragment;
GN Name=CSNK1G3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1946367; DOI=10.1073/pnas.88.21.9548;
RA Rowles J., Slaughter C., Moomaw C., Hsu J., Cobb M.H.;
RT "Purification of casein kinase I and isolation of cDNAs encoding multiple
RT casein kinase I-like enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:9548-9552(1991).
CC -!- FUNCTION: Casein kinases are operationally defined by their
CC preferential utilization of acidic proteins such as caseins as
CC substrates. It can phosphorylate a large number of proteins.
CC Participates in Wnt signaling (By 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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Testis.
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; M76542; AAA30454.1; -; mRNA.
DR PIR; D56406; D56406.
DR RefSeq; NP_001098799.2; NM_001105329.2.
DR AlphaFoldDB; P35509; -.
DR SMR; P35509; -.
DR STRING; 9913.ENSBTAP00000023329; -.
DR PaxDb; P35509; -.
DR PRIDE; P35509; -.
DR GeneID; 407190; -.
DR KEGG; bta:407190; -.
DR CTD; 1456; -.
DR eggNOG; KOG1165; Eukaryota.
DR HOGENOM; CLU_019279_2_0_1; -.
DR InParanoid; P35509; -.
DR OrthoDB; 889559at2759; -.
DR Proteomes; UP000009136; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 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; 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; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN 1..>276
FT /note="Casein kinase I isoform gamma-3"
FT /id="PRO_0000192845"
FT DOMAIN 29..>276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 35..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT NON_TER 276
SQ SEQUENCE 276 AA; 31510 MW; 69E9364A2E50C34C CRC64;
MARPSGRLGH NTRGTGSSSS GVLMVGPNFR VGKKIGCGNF GELRLGKNLY TNEYVAIKLE
PMKSRAPQLH LEYRFYKQLG SGDGIPQVYY FGPCGKYNAM VLELLGPSLE DLFDLCDRTF
SLKTVLMIAI QLISRMEYVH SKNLIYRDVK PENFLIGRPG NKTQQVIHII DFGLAKEYID
PETKKHIPYR EHKSLTGTAR YMSINTHLGK EQSRRDDLEA LGHMFMYFLR GSLPWQGLKA
DTLKERYQKI GDTKRATPIE VLCENFPEMA TYLRYV
