CST1_CAEBR
ID CST1_CAEBR Reviewed; 494 AA.
AC A8XJW8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Serine/threonine-protein kinase cst-1 {ECO:0000250|UniProtKB:Q13188};
DE EC=2.7.11.1;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase cst-1 37kDa subunit;
DE Contains:
DE RecName: Full=Serine/threonine-protein kinase cst-1 18kDa subunit;
GN Name=cst-1; ORFNames=CBG14395;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
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: Serine/threonine-protein kinase which extends lifespan and
CC delays tissue aging, probably by activating daf-16.
CC {ECO:0000250|UniProtKB:Q9NB31}.
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:Q13188};
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:Q13188};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13188};
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis which
CC results in kinase activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000255}.
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DR EMBL; HE600983; CAP32944.2; -; Genomic_DNA.
DR AlphaFoldDB; A8XJW8; -.
DR SMR; A8XJW8; -.
DR STRING; 6238.CBG14395; -.
DR EnsemblMetazoa; CBG14395.1; CBG14395.1; WBGene00034914.
DR WormBase; CBG14395; CBP35565; WBGene00034914; Cbr-cst-1.
DR eggNOG; KOG0574; Eukaryota.
DR HOGENOM; CLU_000288_63_23_1; -.
DR InParanoid; A8XJW8; -.
DR OMA; WSEEFND; -.
DR OrthoDB; 967913at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0055001; P:muscle cell development; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR Gene3D; 4.10.170.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024205; Mst1_SARAH_domain.
DR InterPro; IPR036674; p53_tetramer_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011524; SARAH_dom.
DR Pfam; PF11629; Mst1_SARAH; 1.
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; PS50951; SARAH; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..494
FT /note="Serine/threonine-protein kinase cst-1"
FT /id="PRO_0000396640"
FT CHAIN 1..332
FT /note="Serine/threonine-protein kinase cst-1 37kDa subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000413723"
FT CHAIN 333..494
FT /note="Serine/threonine-protein kinase cst-1 18kDa subunit"
FT /evidence="ECO:0000250"
FT /id="PRO_0000413724"
FT DOMAIN 35..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 443..490
FT /note="SARAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00310"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 41..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 332..333
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 494 AA; 55215 MW; 4477585E1728F8D0 CRC64;
MPPSTDSSRR NSEEGFSDGF KLDSSALNKP PEEVFDIVGK LGEGSYGSVH KAIHKESGHV
LAIKKVPVDT DLQEIIKEIS IMQQCKSKYV VKYYGSYFKN SDLWIVMEYC GAGSISDIMR
ARRKPLSEKE ISAVLRDTLK GLQYLHDLKK IHRDIKAGNI LLNTDGIAKL ADFGVAGQLT
DTMAKRNTVI GTPFWMAPEV IEEIGYDTKA DIWSLGITAI EMAEGRPPYS DIHPMRAIFM
IPTKPPPTFK KPEEWSSEFN DFIRCCLIKK PEERKTALRL CEHTFIENAP GCDVLQAMIL
DAQEKVLLGQ APVAVAGADA TLLSEGMSTM IDGGDATLVQ YKDNYVTAQS LRSQMESLKI
GGEIPKSAYG SSRNNGSPRV QPPGHTASAC DPSNNPPFAE EGTGPNFQIG TSESSYKDAS
YNMMNTEAEY ENRFQRAVCD GDFEFLRNIT LDELIRRKES LDSEMEEEIR ELQRRYKTKR
QPILDVIEIK KRLN
