EAK5_CAEEL
ID EAK5_CAEEL Reviewed; 345 AA.
AC G5EGA9;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Protein sdf-9 {ECO:0000305};
DE AltName: Full=Synthetic dauer formation 9 {ECO:0000312|WormBase:Y44A6D.4};
GN Name=sdf-9 {ECO:0000312|WormBase:Y44A6D.4};
GN Synonyms=eak-5 {ECO:0000312|WormBase:Y44A6D.4};
GN ORFNames=Y44A6D.4 {ECO:0000312|WormBase:Y44A6D.4};
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:BAC75705.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF PRO-175 AND ARG-264.
RX PubMed=12783794; DOI=10.1242/dev.00540;
RA Ohkura K., Suzuki N., Ishihara T., Katsura I.;
RT "SDF-9, a protein tyrosine phosphatase-like molecule, regulates the
RT L3/dauer developmental decision through hormonal signaling in C. elegans.";
RL Development 130:3237-3248(2003).
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ARG-264.
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).
CC -!- FUNCTION: Together with eak-4 and phosphatase eak-6, negatively
CC regulates dauer larva formation downstream of insulin-like receptor
CC daf-2 and in parallel of age-1, pdk-1 and akt-1.
CC {ECO:0000269|PubMed:12783794, ECO:0000269|PubMed:16839187}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12783794}. Cell
CC membrane {ECO:0000269|PubMed:16839187}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16839187}. Note=Localizes to dendrite-like
CC structure in XXXL/R cells. Membrane localization is daf-2/InsR-
CC independent. {ECO:0000269|PubMed:12783794}.
CC -!- TISSUE SPECIFICITY: Expressed in the 2 embryonic head hypodermal cells
CC XXXL/R. {ECO:0000269|PubMed:12783794, ECO:0000269|PubMed:16839187}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- CAUTION: Predicted to be inactive as the cysteine residue involved in
CC the catalytic reaction is a lysine at position 223.
CC {ECO:0000305|PubMed:12783794}.
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DR EMBL; AB108783; BAC75705.1; -; mRNA.
DR EMBL; BX284605; CAA19518.3; -; Genomic_DNA.
DR PIR; T26897; T26897.
DR RefSeq; NP_508013.2; NM_075612.3.
DR AlphaFoldDB; G5EGA9; -.
DR SMR; G5EGA9; -.
DR STRING; 6239.Y44A6D.4; -.
DR PaxDb; G5EGA9; -.
DR EnsemblMetazoa; Y44A6D.4.1; Y44A6D.4.1; WBGene00004748.
DR GeneID; 189901; -.
DR KEGG; cel:CELE_Y44A6D.4; -.
DR CTD; 189901; -.
DR WormBase; Y44A6D.4; CE35663; WBGene00004748; sdf-9.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000165839; -.
DR OrthoDB; 144506at2759; -.
DR PhylomeDB; G5EGA9; -.
DR Reactome; R-CEL-388844; Receptor-type tyrosine-protein phosphatases.
DR PRO; PR:G5EGA9; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004748; Expressed in larva.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
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 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; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..345
FT /note="Protein sdf-9"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436047"
FT DOMAIN 33..284
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT MUTAGEN 175
FT /note="P->L: In ut163; moderate increase in constitutive
FT dauer larva formation at 25 degrees Celsius. Constitutive
FT larva dauer formation is further increased in absence of
FT cholesterol. Lack of radial constriction in the pharynx of
FT constitutive dauer-like larvae."
FT /evidence="ECO:0000269|PubMed:12783794"
FT MUTAGEN 264
FT /note="R->K: In ut187 and ut157; moderate increase in
FT constitutive dauer formation at 25 degrees Celsius.
FT Constitutive dauer formation is further increased in
FT absence of cholesterol. Normal lifespan."
FT /evidence="ECO:0000269|PubMed:12783794,
FT ECO:0000269|PubMed:16839187"
SQ SEQUENCE 345 AA; 40338 MW; E44F5DFA08050F5D CRC64;
MEKYSIRSNI VHKLDDNQPL LSERVTARLE AVNRNRVVKI VPQHRYNVRL TPSMLNRDGY
INASLMEFSD VGQKYILTGI PSEDKVFAFW QMVLEQRSPT IIQFADNVEE KLEHYDKYFP
DKGDVWSYGH LQVERKSYAI HQGNFHTRNF ILRKGNETHR VLHFTVFGWT ETTTPIMQDF
LALRKVMKDT GALNMINPAS ALFRSTMRRY IHTPPSFAPI IQSARGSSRA GAFVVIDLLI
RMIDGKKTNL YSVEDLIVKC KHMRIHCVPV ALHHSFIYEA VLDYLLRRNP RFQDFKEPLI
AYSESCFVKW SSMDKEIEKF INTKTWFLNE SSRNKFLRSV MPPVV
