AAPK1_CAEEL
ID AAPK1_CAEEL Reviewed; 589 AA.
AC P45894; Q3HKC8; Q3HKC9; Q5VKL2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-1;
DE Short=AMPK subunit alpha-1;
DE EC=2.7.11.1;
GN Name=aak-1; ORFNames=PAR2.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RX PubMed=15574588; DOI=10.1101/gad.1255404;
RA Apfeld J., O'Connor G., McDonagh T., DiStefano P.S., Curtis R.;
RT "The AMP-activated protein kinase AAK-2 links energy levels and insulin-
RT like signals to lifespan in C. elegans.";
RL Genes Dev. 18:3004-3009(2004).
RN [2]
RP ERRATUM OF PUBMED:15574588.
RA Apfeld J., O'Connor G., McDonagh T., DiStefano P.S., Curtis R.;
RL Genes Dev. 19:188-188(2005).
RN [3]
RP ERRATUM OF PUBMED:15574588.
RA Apfeld J., O'Connor G., McDonagh T., DiStefano P.S., Curtis R.;
RL Genes Dev. 19:411-411(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [6]
RP FUNCTION.
RX PubMed=20110331; DOI=10.1242/dev.042044;
RA Narbonne P., Hyenne V., Li S., Labbe J.C., Roy R.;
RT "Differential requirements for STRAD in LKB1-dependent functions in C.
RT elegans.";
RL Development 137:661-670(2010).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26439621; DOI=10.1371/journal.pgen.1005520;
RA Possik E., Ajisebutu A., Manteghi S., Gingras M.C., Vijayaraghavan T.,
RA Flamand M., Coull B., Schmeisser K., Duchaine T., van Steensel M.,
RA Hall D.H., Pause A.;
RT "FLCN and AMPK Confer Resistance to Hyperosmotic Stress via Remodeling of
RT Glycogen Stores.";
RL PLoS Genet. 11:E1005520-E1005520(2015).
CC -!- FUNCTION: Probably does not act as a sensor that couples lifespan to
CC information about energy levels and insulin-like signals
CC (PubMed:15574588). Together with aak-2, involved in the establishment
CC of germline stem cell (GSC) quiescence during dauer development
CC (PubMed:20110331). Plays a role in the maintenance of glycogen stores
CC which are necessary for resistance to hyperosmotic stress
CC (PubMed:26439621). {ECO:0000269|PubMed:15574588,
CC ECO:0000269|PubMed:20110331, ECO:0000269|PubMed:26439621}.
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 -!- 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;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P45894-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P45894-2; Sequence=VSP_017190;
CC -!- DISRUPTION PHENOTYPE: Reduced survival as a result of hyperosmotic
CC stress induced by NaCl. Double knockout with aak-2 results in reduced
CC glycogen accumulation. {ECO:0000269|PubMed:26439621}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000305}.
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DR EMBL; AY347272; AAR06927.1; -; mRNA.
DR EMBL; FO081577; CCD72533.1; -; Genomic_DNA.
DR EMBL; FO081577; CCD72534.1; -; Genomic_DNA.
DR PIR; S44859; S44859.
DR RefSeq; NP_741254.3; NM_171216.4. [P45894-1]
DR RefSeq; NP_741255.3; NM_171217.4.
DR AlphaFoldDB; P45894; -.
DR SMR; P45894; -.
DR BioGRID; 41433; 1.
DR STRING; 6239.PAR2.3a; -.
DR EPD; P45894; -.
DR PaxDb; P45894; -.
DR PeptideAtlas; P45894; -.
DR EnsemblMetazoa; PAR2.3a.1; PAR2.3a.1; WBGene00019801. [P45894-1]
DR EnsemblMetazoa; PAR2.3b.1; PAR2.3b.1; WBGene00019801. [P45894-2]
DR GeneID; 176230; -.
DR KEGG; cel:CELE_PAR2.3; -.
DR UCSC; PAR2.3b.1; c. elegans. [P45894-1]
DR CTD; 176230; -.
DR WormBase; PAR2.3a; CE39167; WBGene00019801; aak-1. [P45894-1]
DR WormBase; PAR2.3b; CE39168; WBGene00019801; aak-1. [P45894-2]
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_000288_59_3_1; -.
DR InParanoid; P45894; -.
DR OMA; PECENES; -.
DR OrthoDB; 1127668at2759; -.
DR PhylomeDB; P45894; -.
DR Reactome; R-CEL-1632852; Macroautophagy.
DR Reactome; R-CEL-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-CEL-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:P45894; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019801; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005634; C:nucleus; 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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR InterPro; IPR028375; KA1/Ssp2_C.
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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; SSF103243; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..589
FT /note="5'-AMP-activated protein kinase catalytic subunit
FT alpha-1"
FT /id="PRO_0000085598"
FT DOMAIN 24..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 147
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 30..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..171
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_017190"
FT CONFLICT 205
FT /note="L -> P (in Ref. 1; AAR06927)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="R -> H (in Ref. 1; AAR06927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 65620 MW; AED4E43EFBFDD863 CRC64;
MPPSGRFDRT IALAGTGHLK IGNFVIKETI GKGAFGAVKR GTHIQTGYDV AIKILNRGRM
KGLGTVNKTR NEIDNLQKLT HPHITRLFRV ISTPSDIFLV MELVSGGELF SYITRKGALP
IRESRRYFQQ IISGVSYCHN HMIVHRDLKP ENLLLDANKN IKIADFGLSN YMTDGDLLST
ACGSPNYAAP ELISNKLYVG PEVDLWSCGV ILYAMLCGTL PFDDQNVPTL FAKIKSGRYT
VPYSMEKQAA DLISTMLQVD PVKRADVKRI VNHSWFRIDL PYYLFPECEN ESSIVDIDVV
QSVAEKFDVK EEDVTGALLA EDHHHFLCIA YRLEVNHKRN ADESSQKAME DFWEIGKTMK
MGSTSLPVGA TTKTNVGRKI LEGLKKEQKK LTWNLGIRAC LDPVETMKHV FLSLKSVDME
WKVLSMYHII VRSKPTPINP DPVKVSLQLF ALDKKENNKG YLLDFKGLTE DEEAVPPSRC
RSRAASVSVT LAKSKSDLNG NSSKVPMSPL SPMSPISPSV NIPKVRVDDA DASLKSSLNS
SIYMADIENS MESLDEVSTQ SSEPEAPIRS QTMEFFATCH IIMQALLAE
