ID   Q9R0P1_MOUSE            Unreviewed;       339 AA.
AC   Q9R0P1;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAA86229.1};
RN   [1] {ECO:0000313|EMBL:BAA86229.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129Ola {ECO:0000313|EMBL:BAA86229.1};
RX   PubMed=12060709; DOI=10.1073/pnas.122254599;
RA   Jishage K., Nezu J., Kawase Y., Iwata T., Watanabe M., Miyoshi A., Ose A.,
RA   Habu K., Kake T., Kamada N., Ueda O., Kinoshita M., Jenne D.E., Shimane M.,
RA   Suzuki H.;
RT   "Role of Lkb1, the causative gene of Peutz-Jegher's syndrome, in
RT   embryogenesis and polyposis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8903-8908(2002).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. LKB1 subfamily. {ECO:0000256|ARBA:ARBA00009985}.
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DR   EMBL; AB026255; BAA86229.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9R0P1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030295; F:protein kinase activator activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030010; P:establishment of cell polarity; IEA:InterPro.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
DR   CDD; cd14119; STKc_LKB1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR039154; LKB1_c.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43895; CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE KINASE-RELATED; 1.
DR   PANTHER; PTHR43895:SF25; SERINE_THREONINE-PROTEIN KINASE STK11; 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   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAA86229.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..212
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          300..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAA86229.1"
SQ   SEQUENCE   339 AA;  38308 MW;  73F4DB9438443A6C CRC64;
     EIQLLRRLRH RNVIQLVDVL YNEEKQKMYM VMEYCVCGMQ EMLDSVPEKR FPVCQAHGYF
     RQLIDGLEYL HSQGIVHKDI KPGNLLLTTN GTLKISDLGV AEALHPFAVD DTCRTSQGSP
     AFQPPEIANG LDTFSGFKVD IWSAGVTLYN ITTGLYPFEG DNIYKLFENI GRGDFTIPCD
     CGPPLSDLLR GMLEYEPAKR FSIRQIRQHS WFRKKHPLAE ALVPIPPSPD TKDRWRSMTV
     VPYLEDLHGR AEEEEEEDLF DIEDGIIYTQ DFTVPGQVLE EEVGQNGQSH SLPKAVCVNG
     TEPQLSSKVK PEGRPGTANP ARKVCSSNKI RRLSACKQQ
//