ID A0A3B3WUL9_9TELE Unreviewed; 458 AA.
AC A0A3B3WUL9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Casein kinase I isoform gamma-1 {ECO:0000256|ARBA:ARBA00040035};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000006491.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000006491.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 RefSeq; XP_014868340.1; XM_015012854.1.
DR AlphaFoldDB; A0A3B3WUL9; -.
DR STRING; 48701.ENSPMEP00000006491; -.
DR Ensembl; ENSPMET00000005727.1; ENSPMEP00000006491.1; ENSPMEG00000008033.1.
DR GeneID; 106933549; -.
DR CTD; 53944; -.
DR OrthoDB; 1534388at2759; -.
DR Proteomes; UP000261480; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU000304};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304};
KW Transferase {ECO:0000256|RuleBase:RU000304};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 44..315
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 458 AA; 52586 MW; A1EFE1B6F32469B3 CRC64;
MDQQREKYGE RTTRSTKVNQ GNRSGHRPSG SSNTSGVLMV GPNFRVGKKI GCGNFGELKL
GKNLYTNEYV AIKLEPVKSR APQLHLEYRF YKSLGTTAEG VPQVFYFGPC GKYNAMVMEL
LGPSLEDLFD LCDRTFSLKT VLMIAIQLIS RMEYVHSKNL IYRDVKPENF LIGRQGNKKE
HIIHIIDFGL AKEYIDPETK KHIPYREHKS LTGTARYMSI NTHLGKEQSR RDDLEALGHM
FMYFLRGSLP WQGLKADTLK ERYQKIGDTK RNTPIEVLCE NFPEEMATYL RYVRRLDFFE
KPDYEYLRTL FTELFERKGY TFDYTYDWVG RQIPTPVGSV HIDSGASAVT RESHPHRERP
SQHPPVRNQT AGSDRRGAWE VQPTRQANSS YLTSHLAADR HGGSVQVVSS TNGELNADDP
LAQSNTPITP QADVEVVDEP KCCCFFRRKR KKNTQRHK
//
