STK11_CHICK
ID STK11_CHICK Reviewed; 440 AA.
AC Q0GGW5;
DT 14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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;
GN Name=STK11 {ECO:0000250|UniProtKB:Q15831, ECO:0000312|EMBL:ABI23430.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABI23430.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Duodenum {ECO:0000312|EMBL:ABI23430.1};
RX PubMed=16343965; DOI=10.1016/j.cbpb.2005.10.009;
RA Proszkowiec-Weglarz M., Richards M.P., Ramachandran R., McMurtry J.P.;
RT "Characterization of the AMP-activated protein kinase pathway in
RT chickens.";
RL Comp. Biochem. Physiol. 143B:92-106(2006).
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;
CC Evidence={ECO:0000250|UniProtKB:Q15831};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q15831};
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 {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues tested. High
CC levels were observed in duodenum and skeletal muscle, lower levels in
CC liver and pancreas. {ECO:0000269|PubMed:16343965}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. LKB1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ864976; ABI23430.1; -; mRNA.
DR RefSeq; NP_001039298.1; NM_001045833.1.
DR AlphaFoldDB; Q0GGW5; -.
DR SMR; Q0GGW5; -.
DR PaxDb; Q0GGW5; -.
DR GeneID; 420105; -.
DR KEGG; gga:420105; -.
DR CTD; 6794; -.
DR VEuPathDB; HostDB:geneid_420105; -.
DR InParanoid; Q0GGW5; -.
DR OrthoDB; 856506at2759; -.
DR PhylomeDB; Q0GGW5; -.
DR PRO; PR:Q0GGW5; -.
DR Proteomes; UP000000539; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:AgBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IDA:AgBase.
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:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:1901610; P:positive regulation of vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:AgBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 2: Evidence at transcript 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..440
FT /note="Serine/threonine-protein kinase STK11"
FT /id="PRO_0000260033"
FT DOMAIN 49..309
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 370..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 55..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 336
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 365
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 435
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 440 AA; 49793 MW; EE79DB8129E4770A CRC64;
MDMQESQQLG MFGESELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY
GKVKEMLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ LLRRLRHKNV IQLVDVLYNE
EKQKMYMVME YCVCGMQEML DSVPEKRFPV FQAHGYFCQL IDGLEYLHSQ GIVHKDIKPG
NLLLTTNGTL KISDLGVAEA LHPFAEDDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS
AGVTLYNITT GLYPFEGDNI YKLFENIGKG DFTIPEDCGP PLSDLLRGML EYDPAKRFSI
QQIRQHNWFR KKHAQAETLV PIPPSPETKD KWRSMTAVPY LEDLHGYNED EDDDLYDIED
DIIYTQDFTV PGQVPEEEAG QNGQSRGRGL PKAICMNGTE PGQLSTKSKA ERRASASSNP
SRKACSASSK IRKLSTCKQQ
