ID A0A3Q1M652_BOVIN Unreviewed; 464 AA.
AC A0A3Q1M652;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Casein kinase I isoform gamma-1 {ECO:0000256|ARBA:ARBA00040035};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=CSNK1G1 {ECO:0000313|Ensembl:ENSBTAP00000069207.1,
GN ECO:0000313|VGNC:VGNC:50095};
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 {ECO:0000313|Ensembl:ENSBTAP00000069207.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000069207.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069207.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000069207.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069207.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. Casein kinase I subfamily.
CC {ECO:0000256|ARBA:ARBA00005926}.
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DR AlphaFoldDB; A0A3Q1M652; -.
DR Ensembl; ENSBTAT00000067085.1; ENSBTAP00000069207.1; ENSBTAG00000016823.5.
DR VEuPathDB; HostDB:ENSBTAG00000016823; -.
DR VGNC; VGNC:50095; CSNK1G1.
DR GeneTree; ENSGT00940000155628; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000016823; Expressed in semen and 111 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1M652; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
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; 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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT TRANSMEM 438..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 43..304
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 53388 MW; EFCC770E19292444 CRC64;
MDHPSREKDE RQRTTKPMAQ RREHCSRPSG STSSGVLMVG PNFRVGKKIG CGNFGELRLG
KNLEPIKSRA PQLHLEYRFY KQLGSAGEGL PQVYYFGPCG KYNAMVLELL GPSLEDLFDL
CDRTFTLKTV LMIAIQLLSR MEYVHSKNLI YRDVKPENFL IGRQGNKKEH VIHIIDFGLA
KEYIDPETKK HIPYREHKSL TGTARYMSIN THLGKEQSRR DDLEALGHMF MYFLRGSLPW
QGLKADTLKE RYQKIGDTKR NTPIEVLCEN FPEEMATYLR YVRRLDFFEK PDYEYLRTLF
TDLFERKGYT FDYAYDWVGR PIPTPVGSVH VDSGASAITR ESHTHRDRPS QQPLRNQTAS
SERRGEWEIQ PSRQTNTSYL TSHLAADRHG GSVQVVSSTN GELNVDDPTG AHSNAPITAH
AEVEVVEEAK WTFCCCRFEF FVCFSFTVFF FFPAFLSFSL PINI
//
