EAK4_CAEEL
ID EAK4_CAEEL Reviewed; 247 AA.
AC G5EBR8;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Protein eak-4 {ECO:0000305};
DE AltName: Full=Enhancer of akt-1 null 4 {ECO:0000312|WormBase:F53B2.3};
GN Name=eak-4 {ECO:0000312|WormBase:F53B2.3};
GN ORFNames=F53B2.3 {ECO:0000312|WormBase:F53B2.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:ABI83732.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, MUTAGENESIS OF GLY-2; GLY-85 AND TYR-96, AND MYRISTOYLATION AT
RP GLY-2.
RX PubMed=16839187; DOI=10.1371/journal.pgen.0020099;
RA Hu P.J., Xu J., Ruvkun G.;
RT "Two membrane-associated tyrosine phosphatase homologs potentiate C.
RT elegans AKT-1/PKB signaling.";
RL PLoS Genet. 2:E99-E99(2006).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [3]
RP FUNCTION, AND MUTAGENESIS OF GLY-85.
RX PubMed=24385923; DOI=10.1371/journal.pgen.1004020;
RA Ferguson A.A., Roy S., Kormanik K.N., Kim Y., Dumas K.J., Ritov V.B.,
RA Matern D., Hu P.J., Fisher A.L.;
RT "TATN-1 mutations reveal a novel role for tyrosine as a metabolic signal
RT that influences developmental decisions and longevity in Caenorhabditis
RT elegans.";
RL PLoS Genet. 9:e1004020-e1004020(2013).
CC -!- FUNCTION: Together with eak-6 and sdf-9, negatively regulates dauer
CC larva formation downstream of the insulin-like receptor daf-2 and in
CC parallel with age-1, pdk-1 and akt-1 (PubMed:16839187).
CC {ECO:0000269|PubMed:16839187, ECO:0000269|PubMed:24385923}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16839187};
CC Lipid-anchor {ECO:0000305|PubMed:16839187}; Cytoplasmic side
CC {ECO:0000269|PubMed:16839187}.
CC -!- TISSUE SPECIFICITY: Expressed in the 2 embryonic head hypodermal cells
CC XXXL/R. {ECO:0000269|PubMed:16839187}.
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DR EMBL; DQ907008; ABI83732.1; -; mRNA.
DR EMBL; BX284604; CAA98128.1; -; Genomic_DNA.
DR PIR; T22535; T22535.
DR RefSeq; NP_502398.1; NM_069997.1.
DR AlphaFoldDB; G5EBR8; -.
DR SMR; G5EBR8; -.
DR STRING; 6239.F53B2.3; -.
DR iPTMnet; G5EBR8; -.
DR PaxDb; G5EBR8; -.
DR EnsemblMetazoa; F53B2.3.1; F53B2.3.1; WBGene00009955.
DR GeneID; 186150; -.
DR KEGG; cel:CELE_F53B2.3; -.
DR CTD; 186150; -.
DR WormBase; F53B2.3; CE05917; WBGene00009955; eak-4.
DR HOGENOM; CLU_1125402_0_0_1; -.
DR InParanoid; G5EBR8; -.
DR PhylomeDB; G5EBR8; -.
DR PRO; PR:G5EBR8; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00009955; Expressed in larva.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Myristate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:16839187"
FT CHAIN 2..247
FT /note="Protein eak-4"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436046"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:16839187"
FT MUTAGEN 2
FT /note="G->A: Probable loss of myristoylation. Loss of
FT membrane localization."
FT /evidence="ECO:0000269|PubMed:16839187"
FT MUTAGEN 85
FT /note="G->E: In mg348; wild-type lifespan. Moderate
FT increase in constitutive dauer larva formation at 27
FT degrees Celsius. Significant increase in dauer larva
FT formation in response to the AMP analog AICAR (5-amino-1-
FT (5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) at 25
FT degrees Celsius. This phenotype is abrogated in an aak-2
FT gt33 mutant background. Increases dauer formation in a hpd-
FT 1 ok1955 mutant background. Increases dauer formation and
FT increases aak-2 phosphorylation, but does not impair energy
FT production in a tatn-1 RNAi mutant background. Reduces
FT dauer formation in a tatn-1 RNAi or tatn-1 qd182 and aak-2
FT gt33 mutant background."
FT /evidence="ECO:0000269|PubMed:16839187,
FT ECO:0000269|PubMed:24385923"
FT MUTAGEN 96
FT /note="Y->N: In mg326; increases constitutive dauer larva
FT formation at 25 degrees Celsius in akt-1 mg306 mutant
FT background."
FT /evidence="ECO:0000269|PubMed:16839187"
SQ SEQUENCE 247 AA; 29087 MW; 10A5811179545F06 CRC64;
MGQCLAVHRR IMASQEFPNI PQPESQCHDA FIRYSPGRYE RRAARSQVDY YLLPQAPRLM
TEDLDKKEFQ RLYDARCELV ECPAGRRAMQ LDVQIYADRY EATLNKILET SQELDKGLED
IFQAYTKDDP LADKVMNCRL TVDEMGRVYE HFFRESAWNL DSFVEYRKNL ARDAYLLLAD
LKIAIQRLGM HFNPNFEDAQ VKVDFQIMQA EQIIFHFKRT YRDALKHNPD SITEFVEDEL
EDPGTPL
