ID   A0JPL2_RAT              Unreviewed;       337 AA.
AC   A0JPL2;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   02-SEP-2026, entry version 128.
DE   RecName: Full=Serine/threonine-protein {ECO:0000256|PROSITE-ProRule:PRU10027};
DE            EC=2.7.11.1 {ECO:0000256|PROSITE-ProRule:PRU10027};
GN   Name=Csnk1a1 {ECO:0000313|EMBL:AAI27487.1, ECO:0000313|RGD:71098};
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 {ECO:0000313|EMBL:AAI27487.1};
RN   [1] {ECO:0000313|EMBL:AAI27487.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000313|EMBL:AAI27487.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. Can phosphorylate a large number of proteins. Participates
CC       in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate
CC       PER1 and PER2. May play a role in segregating chromosomes during
CC       mitosis. May play a role in keratin cytoskeleton disassembly and
CC       thereby, it may regulate epithelial cell migration. Acts as a positive
CC       regulator of mTORC1 and mTORC2 signaling in response to nutrients by
CC       mediating phosphorylation of DEPTOR inhibitor. Acts as an inhibitor of
CC       NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3.
CC       {ECO:0000256|ARBA:ARBA00057915}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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|PROSITE-ProRule:PRU10027};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00047899, ECO:0000256|PROSITE-
CC         ProRule:PRU10027};
CC   -!- SUBUNIT: Interacts with the Axin complex. Interacts with TUT1, leading
CC       to TUT1 phosphorylation. Interacts with FAM83A, FAM83B, FAM83C, FAM83D,
CC       FAM83E, FAM83F, FAM83G and FAM83H (via DUF1669). Interaction with
CC       FAM83H recruits CSNK1A1 to keratin filaments. Interacts with FAM170A.
CC       {ECO:0000256|ARBA:ARBA00096432}.
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, cilium basal
CC       body {ECO:0000256|ARBA:ARBA00004120}. Nucleus speckle
CC       {ECO:0000256|ARBA:ARBA00004324}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. Casein kinase I subfamily.
CC       {ECO:0000256|ARBA:ARBA00005926}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000256|PROSITE-ProRule:PRU00159}.
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DR   EMBL; BC127486; AAI27487.1; -; mRNA.
DR   RefSeq; NP_446067.2; NM_053615.2.
DR   AlphaFoldDB; A0JPL2; -.
DR   SMR; A0JPL2; -.
DR   jPOST; A0JPL2; -.
DR   PeptideAtlas; A0JPL2; -.
DR   GeneID; 113927; -.
DR   KEGG; rno:113927; -.
DR   CTD; 1452; -.
DR   RGD; 71098; Csnk1a1.
DR   HOGENOM; CLU_019279_2_0_1; -.
DR   Bgee; ENSRNOG00000017106; Expressed in esophagus and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-ARBA.
DR   GO; GO:0016607; C:nuclear speck; 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-EC.
DR   CDD; cd14128; STKc_CK1_alpha; 1.
DR   FunFam; 1.10.510.10:FF:000120; Casein kinase I isoform alpha; 1.
DR   FunFam; 3.30.200.20:FF:000538; Putative Casein kinase I; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR050235; CK1_Ser-Thr_kinase-like.
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; CASEIN KINASE-RELATED; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cell cycle {ECO:0000256|ARBA:ARBA00022776};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PROSITE-
KW   ProRule:PRU00159}; Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PROSITE-ProRule:PRU00159};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU00159}; Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          17..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          309..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..325
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        136
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10027"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   337 AA;  38915 MW;  1B2085AE33CAFAC2 CRC64;
     MASSSGSKAE FIVGGKYKLV RKIGSGSFGD IYLAINITNG EEVAVKLESQ KARHPQLLYE
     SKLYKILQGG VGIPHIRWYG QEKDYNVLVM DLLGPSLEDL FNFCSRRFTM KTVLMLADQM
     ISRIEYVHTK NFIHRDIKPD NFLMGIGRHC NKLFLIDFGL AKKYRDNRTR QHIPYREDKN
     LTGTARYASI NAHLGIEQSR RDDMESLGYV LMYFNRTSLP WQGLKAATKK QKYEKISEKK
     MSTPVEVLCK GFPAEFAMYL NYCRGLRFEE APDYMYLRQL FRILFRTLNH QYDYTFDWTM
     LKQKAAQQAA SSSGQGQQAQ TPTGKQTDKT KSNMKGF
//