EAK6_CAEEL
ID EAK6_CAEEL Reviewed; 405 AA.
AC G5EGU2; G5EEU5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type eak-6 {ECO:0000305};
DE EC=3.1.3.48 {ECO:0000305};
DE AltName: Full=Enhancer of akt-1 null 6 {ECO:0000312|WormBase:F10G8.4b};
GN Name=eak-6 {ECO:0000312|WormBase:F10G8.4b};
GN ORFNames=F10G8.4 {ECO:0000312|WormBase:F10G8.4b};
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:ABI83734.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, LACK OF IN VITRO
RP PHOSPHATASE ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Putative phosphatase which, together with eak-4 and sdf-9,
CC negatively regulates dauer larva formation downstream of insulin-like
CC receptor daf-2 and in parallel of age-1, pdk-1 and akt-1.
CC {ECO:0000269|PubMed:16839187}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16839187}. Cell
CC membrane {ECO:0000269|PubMed:16839187}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16839187}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:F10G8.4b}; Synonyms=EAK-6L
CC {ECO:0000303|PubMed:16839187};
CC IsoId=G5EGU2-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F10G8.4a}; Synonyms=EAK-6S
CC {ECO:0000303|PubMed:16839187};
CC IsoId=G5EGU2-2; Sequence=VSP_058227;
CC -!- TISSUE SPECIFICITY: Expressed in the 2 embryonic head hypodermal cells
CC XXXL/R. {ECO:0000269|PubMed:16839187}.
CC -!- DISRUPTION PHENOTYPE: Moderate increase in constitutive dauer larva
CC formation at 27 degrees Celsius. Increases constitutive dauer larva
CC formation at 25 degrees Celsius in akt-1 mg306, age-1 hx546 or pdk-1
CC sa709 mutant backgrounds. Normal lifespan.
CC {ECO:0000269|PubMed:16839187}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- CAUTION: Its phosphatase activity is uncertain. Lacks in vitro
CC phosphatase activity with p-nitrophenylphosphate, even if the catalytic
CC Cys is conserved. {ECO:0000269|PubMed:16839187}.
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DR EMBL; DQ907009; ABI83733.1; -; mRNA.
DR EMBL; DQ907010; ABI83734.1; -; mRNA.
DR EMBL; BX284601; CAP16268.1; -; Genomic_DNA.
DR EMBL; BX284601; CAP16269.1; -; Genomic_DNA.
DR RefSeq; NP_001122448.1; NM_001128976.1. [G5EGU2-2]
DR RefSeq; NP_001122449.1; NM_001128977.1. [G5EGU2-1]
DR AlphaFoldDB; G5EGU2; -.
DR SMR; G5EGU2; -.
DR STRING; 6239.F10G8.4b; -.
DR PaxDb; G5EGU2; -.
DR EnsemblMetazoa; F10G8.4a.1; F10G8.4a.1; WBGene00008663. [G5EGU2-2]
DR EnsemblMetazoa; F10G8.4b.1; F10G8.4b.1; WBGene00008663. [G5EGU2-1]
DR GeneID; 184324; -.
DR KEGG; cel:CELE_F10G8.4; -.
DR CTD; 184324; -.
DR WormBase; F10G8.4a; CE41631; WBGene00008663; eak-6. [G5EGU2-2]
DR WormBase; F10G8.4b; CE41632; WBGene00008663; eak-6. [G5EGU2-1]
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000165839; -.
DR InParanoid; G5EGU2; -.
DR OMA; DEWIENE; -.
DR OrthoDB; 144506at2759; -.
DR PhylomeDB; G5EGU2; -.
DR Reactome; R-CEL-388844; Receptor-type tyrosine-protein phosphatases.
DR PRO; PR:G5EGU2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008663; Expressed in larva.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0040024; P:dauer larval development; IMP:WormBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cytoplasm; Hydrolase; Membrane;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..405
FT /note="Tyrosine-protein phosphatase non-receptor type eak-
FT 6"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436048"
FT DOMAIN 30..309
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 248
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 377..393
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058227"
SQ SEQUENCE 405 AA; 48334 MW; FEE756942616926D CRC64;
MTNIREDENI FMFLCEKWIL INKNHIWNRI NQRINIIADF DRYQRARTIS EGQRTENIHR
NIYGAVPYDY NLVNLTSTQR NPLGYINASV AEFPEIGRHY IITGAAQDTQ IPFFWQMVFE
QKSPAIVMLL EDVELGIEKS DKYFPNNTRE ELKFGIYDIT CKEFVKRNIL EYRLLEVSVG
NETHQVHHYK FHGWTEFNLP KYEDFMAFYN TMKEVGVPLL AVMKNNCMSS FFKKYHHTPP
TNAPIIQCST GGARCGVFII IDILINLIDN RIKNSYSIEW WMLKVRSKRN HSALTNQQHS
FIYDIIIKYI RTRHNQLRHL EKYLEAHANT VRMIDSTNTE DVDKFIKPRD WIVDFDERDR
LIGKLQFRKR LKIEKDQVSE QKLVHLKSQL HLFQDTYKYE SYVLQ
