STK11_XENLA
ID STK11_XENLA Reviewed; 432 AA.
AC Q91604; Q6DE91;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Serine/threonine-protein kinase stk11 {ECO:0000250|UniProtKB:Q15831};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q15831};
DE AltName: Full=Liver kinase B1 homolog;
DE Short=lkb1;
DE AltName: Full=Serine/threonine-protein kinase XEEK1;
GN Name=stk11 {ECO:0000250|UniProtKB:Q15831}; Synonyms=eek1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-192, MUTAGENESIS OF
RP LYS-81 AND THR-192, AND SUBCELLULAR LOCATION.
RC TISSUE=Ovary;
RX PubMed=8662877; DOI=10.1074/jbc.271.24.14430;
RA Su J.Y., Erikson E., Maller J.L.;
RT "Cloning and characterization of a novel serine/threonine protein kinase
RT expressed in early Xenopus embryos.";
RL J. Biol. Chem. 271:14430-14437(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Tumor suppressor serine/threonine-protein kinase that
CC controls the activity of AMP-activated protein kinase (AMPK) family
CC members, thereby playing a role in various processes such as cell
CC metabolism, cell polarity, apoptosis and DNA damage response. Acts by
CC phosphorylating the T-loop of AMPK family proteins, leading to promote
CC their activity (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q15831};
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:0000250|UniProtKB:Q15831};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Catalytic component of a trimeric complex composed of
CC STK11/LKB1, STRAD (STRADA or STRADB) and CAB39/MO25 (CAB39/MO25alpha or
CC CAB39L/MO25beta). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:8662877}.
CC -!- TISSUE SPECIFICITY: Oocytes, eggs and early embryos.
CC -!- DEVELOPMENTAL STAGE: Its expression peaks in the oocyte and
CC unfertilized egg, begins to decrease gradually after fertilization, and
CC disappears during the gastrulation stage.
CC -!- PTM: Phosphorylated by a cAMP-dependent protein kinase.
CC Autophosphorylated in a reaction that prefers Mn(2+) to Mg(2+).
CC {ECO:0000269|PubMed:8662877}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. LKB1 subfamily. {ECO:0000305}.
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DR EMBL; U24435; AAC59904.1; -; mRNA.
DR EMBL; BC077243; AAH77243.1; -; mRNA.
DR RefSeq; NP_001083758.1; NM_001090289.1.
DR AlphaFoldDB; Q91604; -.
DR SMR; Q91604; -.
DR BioGRID; 100426; 1.
DR IntAct; Q91604; 1.
DR iPTMnet; Q91604; -.
DR DNASU; 399100; -.
DR GeneID; 399100; -.
DR KEGG; xla:399100; -.
DR CTD; 399100; -.
DR Xenbase; XB-GENE-955285; stk11.L.
DR OMA; GMFAESE; -.
DR OrthoDB; 856506at2759; -.
DR BRENDA; 2.7.11.1; 6725.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 399100; Expressed in ovary and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0001944; P:vasculature development; ISS:UniProtKB.
DR CDD; cd14119; STKc_LKB1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR039154; LKB1_c.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cell cycle; Cytoplasm; DNA damage; Kinase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Tumor suppressor.
FT CHAIN 1..432
FT /note="Serine/threonine-protein kinase stk11"
FT /id="PRO_0000086700"
FT DOMAIN 52..312
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 398..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 58..66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 192
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:8662877"
FT MOD_RES 427
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MUTAGEN 81
FT /note="K->I: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8662877"
FT MUTAGEN 192
FT /note="T->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:8662877"
SQ SEQUENCE 432 AA; 49073 MW; F4D98A06C52560F7 CRC64;
MLCPSSMDEE GSEEIGFLGD LSVGMDTFIH RIDSTEVIYQ PRRKRAKLVG KYLMGDLLGE
GSYGKVKEML DSDTLCRRAV KILKKKKLRR IPNGEANVKK EIQLLRRLRH RNVIQLVDVL
YNEEKQKMYM VMEYCVCGMQ EMLDSVQDKH FPVFQAHGYF CQLIDGLEYL HSQGIVHKDI
KPGNLLLTTD GTLKISDLGV AEALHPFAEG DTCRTSQGSP AFQPPEIANG LDTFSGFKVD
IWSAGVTLYN ITTGLYPFEG DNIYKLFENI GKGDYSIPEE CGPLLSDLLR GMLEYDPAKR
FSIQQIRQHN WFRKKHPHMD PIVPIPPSPE TKDRWRSLTV VPYLEDLHGY SEEEDLCDFE
DDIIYTQDFT VPGQVAEDDY FAQTQSTAPS KQLCMNGTES QLKTERRVSS SSQRKASTTG
SKVRKLSACK QQ
