GSK3_CAEBR
ID GSK3_CAEBR Reviewed; 359 AA.
AC A8X5H5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Glycogen synthase kinase-3 {ECO:0000250|UniProtKB:Q9U2Q9};
DE EC=2.7.11.26;
GN Name=gsk-3; ORFNames=CBG07972;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP27886.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP27886.1};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Phosphorylates oma-1, a regulator of the oocyte-to-embryo
CC transition, enabling its degradation. Phosphorylates skn-1, preventing
CC it from accumulating in nuclei and thus inhibiting phase II gene
CC expression in the oxidative stress defense. Involved in mesendoderm
CC specification and mitotic spindle orientation in EMS blastomeres.
CC Thought to be a branch point in these processes as proteins downstream
CC are not required. Negatively regulates Wnt signaling in vulval
CC precursor cells and acts as a Wnt-independent repressor of med-1 and
CC med-2 in the C lineage inhibiting mesoderm development. Required for
CC normal lifespan and LiCl-induced lifespan extension (By similarity).
CC {ECO:0000250|UniProtKB:Q9U2Q9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC Evidence={ECO:0000250|UniProtKB:P49841};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P49841};
CC -!- SUBUNIT: Monomer. Interacts with axl-1. {ECO:0000250|UniProtKB:Q9U2Q9,
CC ECO:0000250|UniProtKB:Q9WV60}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000255}.
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DR EMBL; HE600996; CAP27886.1; -; Genomic_DNA.
DR RefSeq; XP_002646100.1; XM_002646054.1.
DR AlphaFoldDB; A8X5H5; -.
DR SMR; A8X5H5; -.
DR STRING; 6238.CBG07972; -.
DR PRIDE; A8X5H5; -.
DR EnsemblMetazoa; CBG07972.1; CBG07972.1; WBGene00029853.
DR GeneID; 8588159; -.
DR KEGG; cbr:CBG_07972; -.
DR CTD; 8588159; -.
DR WormBase; CBG07972; CBP01995; WBGene00029853; Cbr-gsk-3.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; A8X5H5; -.
DR OMA; CLHAFFD; -.
DR OrthoDB; 990896at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; 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:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IEA:EnsemblMetazoa.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IEA:EnsemblMetazoa.
DR GO; GO:0007281; P:germ cell development; IEA:EnsemblMetazoa.
DR GO; GO:0070986; P:left/right axis specification; IEA:EnsemblMetazoa.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IEA:EnsemblMetazoa.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IEA:EnsemblMetazoa.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0060069; P:Wnt signaling pathway, regulating spindle positioning; IEA:EnsemblMetazoa.
DR CDD; cd14137; STKc_GSK3; 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 InterPro; IPR039192; STKc_GSK3.
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 3: Inferred from homology;
KW ATP-binding; Developmental protein; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Stress response;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..359
FT /note="Glycogen synthase kinase-3"
FT /id="PRO_0000349135"
FT DOMAIN 36..320
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 330..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 359 AA; 40551 MW; F60E3D91F8D651EE CRC64;
MNKQLLSCSL KSGKQVTMVV ASVATDGVDQ QVEISYYDQK VIGNGSFGVV FLAKLSTTNE
MVAIKKVLQD KRFKNRELQI MRKLNHPNIV KLKYFFYSSG DKKDELYLNL ILEYVPETVY
RVARHYSKQR QSIPMIYVKL YMYQLLRSLA YIHSIGICHR DIKPQNLLID PETGILKLCD
FGSAKYLVRN EPNVSYICSR YYRAPELIFG ATNYTNSIDV WSAGTVIAEL LLGQPIFPGD
SGVDQLVEII KVLGTPTREQ IQSMNPNYKE FKFPQIKAHP WNKVFRVHTP AEAIDLISKI
IEYTPTSRPT PQAACQHAFF DELRSPDARL PSGRALPQLE MDGPNEVSAT GGDMAGPSA
