ID   CDK18_RAT               Reviewed;         451 AA.
AC   O35832;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Cyclin-dependent kinase 18;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 18;
DE   AltName: Full=PCTAIRE-motif protein kinase 3;
DE   AltName: Full=Serine/threonine-protein kinase PCTAIRE-3;
GN   Name=Cdk18; Synonyms=Pctaire3, Pctk3;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9370357; DOI=10.1111/j.1432-1033.1997.t01-1-00481.x;
RA   Hirose T., Tamaru T., Okumura N., Nagai K., Okada M.;
RT   "PCTAIRE 2, a Cdc2-related serine/threonine kinase, is predominantly
RT   expressed in terminally differentiated neurons.";
RL   Eur. J. Biochem. 249:481-488(1997).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-66, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-417 AND
RP   SER-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: May play a role in signal transduction cascades in terminally
CC       differentiated cells.
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=2.7.11.22;
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=2.7.11.22;
CC   -!- TISSUE SPECIFICITY: In brain, kidney, intestine and at a much lower
CC       level, in fetal tissues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR   EMBL; AB005541; BAA21472.1; -; mRNA.
DR   RefSeq; NP_001093976.1; NM_001100506.1.
DR   RefSeq; XP_006249813.1; XM_006249751.3.
DR   AlphaFoldDB; O35832; -.
DR   SMR; O35832; -.
DR   STRING; 10116.ENSRNOP00000010976; -.
DR   iPTMnet; O35832; -.
DR   PhosphoSitePlus; O35832; -.
DR   jPOST; O35832; -.
DR   PaxDb; 10116-ENSRNOP00000010976; -.
DR   GeneID; 289019; -.
DR   KEGG; rno:289019; -.
DR   UCSC; RGD:1309523; rat.
DR   AGR; RGD:1309523; -.
DR   CTD; 5129; -.
DR   RGD; 1309523; Cdk18.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_154_3_1; -.
DR   InParanoid; O35832; -.
DR   OrthoDB; 244018at2759; -.
DR   PhylomeDB; O35832; -.
DR   TreeFam; TF106508; -.
DR   BRENDA; 2.7.11.22; 5301.
DR   PRO; PR:O35832; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; PTHR24056; CELL DIVISION PROTEIN KINASE; 1.
DR   PANTHER; PTHR24056:SF52; CYCLIN-DEPENDENT KINASE 18; 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.
DR   Genevisible; O35832; RN.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..451
FT                   /note="Cyclin-dependent kinase 18"
FT                   /id="PRO_0000086493"
FT   DOMAIN          121..402
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          39..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        242
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         127..135
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100,
FT                   ECO:0007744|PubMed:22673903"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100,
FT                   ECO:0007744|PubMed:22673903"
FT   MOD_RES         109
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q04899"
FT   MOD_RES         417
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   451 AA;  51882 MW;  C3E4688F51B142E8 CRC64;
     MNKMKNFKRR LSLSVPRPET IEESLTEFTE QFNQLHTQRN EDGRDEPGQL SPGVQYQQRQ
     NQRRFSMEDL NKRLSLPMDI RLPQEFLQKL QLENPGLPKP LTRMSRRASL SDIGFGKLET
     YVKLDKLGEG TYATVFKGRS KLTENLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV
     TLHDLIHTDR SLTLVFEYLD SDLKQYLDHC GNLMNMHNVK IFMFQLLRGL AYCHRRKILH
     RDLKPQNLLI NERGELKLAD FGLARAKSVP TKTYSNEVVT LWYRPPDVLL GSTEYSTPID
     MWGVGCILYE MATGKPLFPG STVKEELHLI FRLLGTPTEE SWPGVTSISE FRAYNFPRYL
     PQPLLSHAPR LDTEGINLLT SLLLYESKSR MSAEAALSHP YFQSLGERVH QLDDTASIFS
     LKEIQLQKDP GYRGLAFQHP GRGKSRRQSI F
//