PTEN_CAEEL
ID PTEN_CAEEL Reviewed; 962 AA.
AC G5EE01;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase daf-18 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000250|UniProtKB:P60484};
DE EC=3.1.3.48 {ECO:0000269|PubMed:19853560};
DE EC=3.1.3.67 {ECO:0000305|PubMed:15637588};
DE AltName: Full=Abnormal dauer formation protein 18 {ECO:0000312|WormBase:T07A9.6};
GN Name=daf-18 {ECO:0000312|WormBase:T07A9.6};
GN ORFNames=T07A9.6 {ECO:0000312|WormBase:T07A9.6};
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:AAD03420.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9885576; DOI=10.1016/s1097-2765(00)80303-2;
RA Ogg S., Ruvkun G.;
RT "The C. elegans PTEN homolog, DAF-18, acts in the insulin receptor-like
RT metabolic signaling pathway.";
RL Mol. Cell 2:887-893(1998).
RN [2] {ECO:0000312|EMBL:CAA10315.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10209098; DOI=10.1016/s0960-9822(99)80143-2;
RA Rouault J.P., Kuwabara P.E., Sinilnikova O.M., Duret L., Thierry-Mieg D.,
RA Billaud M.;
RT "Regulation of dauer larva development in Caenorhabditis elegans by daf-18,
RT a homologue of the tumour suppressor PTEN.";
RL Curr. Biol. 9:329-332(1999).
RN [3] {ECO:0000312|EMBL:AAD21620.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10077613; DOI=10.1073/pnas.96.6.2925;
RA Gil E.B., Malone Link E., Liu L.X., Johnson C.D., Lees J.A.;
RT "Regulation of the insulin-like developmental pathway of Caenorhabditis
RT elegans by a homolog of the PTEN tumor suppressor gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2925-2930(1999).
RN [4] {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 [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10377431; DOI=10.1073/pnas.96.13.7427;
RA Mihaylova V.T., Borland C.Z., Manjarrez L., Stern M.J., Sun H.;
RT "The PTEN tumor suppressor homolog in Caenorhabditis elegans regulates
RT longevity and dauer formation in an insulin receptor-like signaling
RT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:7427-7432(1999).
RN [6] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLY-174.
RX PubMed=15637588; DOI=10.1038/sj.onc.1207978;
RA Solari F., Bourbon-Piffaut A., Masse I., Payrastre B., Chan A.M.,
RA Billaud M.;
RT "The human tumour suppressor PTEN regulates longevity and dauer formation
RT in Caenorhabditis elegans.";
RL Oncogene 24:20-27(2005).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16631584; DOI=10.1016/j.cub.2006.02.073;
RA Fukuyama M., Rougvie A.E., Rothman J.H.;
RT "C. elegans DAF-18/PTEN mediates nutrient-dependent arrest of cell cycle
RT and growth in the germline.";
RL Curr. Biol. 16:773-779(2006).
RN [8] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=16481471; DOI=10.1101/gad.1378906;
RA Suzuki Y., Han M.;
RT "Genetic redundancy masks diverse functions of the tumor suppressor gene
RT PTEN during C. elegans development.";
RL Genes Dev. 20:423-428(2006).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=16950159; DOI=10.1016/j.neuron.2006.07.024;
RA Tomioka M., Adachi T., Suzuki H., Kunitomo H., Schafer W.R., Iino Y.;
RT "The insulin/PI 3-kinase pathway regulates salt chemotaxis learning in
RT Caenorhabditis elegans.";
RL Neuron 51:613-625(2006).
RN [10]
RP FUNCTION.
RX PubMed=18436204; DOI=10.1016/j.ydbio.2008.03.019;
RA Dixon S.J., Alexander M., Chan K.K., Roy P.J.;
RT "Insulin-like signaling negatively regulates muscle arm extension through
RT DAF-12 in Caenorhabditis elegans.";
RL Dev. Biol. 318:153-161(2008).
RN [11] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH VAB-1, TISSUE SPECIFICITY,
RP PHOSPHORYLATION, ACTIVE SITE, AND MUTAGENESIS OF ASP-137 AND CYS-169.
RX PubMed=19853560; DOI=10.1016/j.devcel.2009.08.009;
RA Brisbin S., Liu J., Boudreau J., Peng J., Evangelista M., Chin-Sang I.;
RT "A role for C. elegans Eph RTK signaling in PTEN regulation.";
RL Dev. Cell 17:459-469(2009).
RN [12] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19249087; DOI=10.1016/j.cell.2009.01.025;
RA Padmanabhan S., Mukhopadhyay A., Narasimhan S.D., Tesz G., Czech M.P.,
RA Tissenbaum H.A.;
RT "A PP2A regulatory subunit regulates C. elegans insulin/IGF-1 signaling by
RT modulating AKT-1 phosphorylation.";
RL Cell 136:939-951(2009).
RN [13] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ARR-1 AND MPZ-1, AND DISRUPTION PHENOTYPE.
RX PubMed=20207731; DOI=10.1074/jbc.m110.104612;
RA Palmitessa A., Benovic J.L.;
RT "Arrestin and the multi-PDZ domain-containing protein MPZ-1 interact with
RT phosphatase and tensin homolog (PTEN) and regulate Caenorhabditis elegans
RT longevity.";
RL J. Biol. Chem. 285:15187-15200(2010).
RN [14] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22069193; DOI=10.1242/dev.069062;
RA Christensen R., de la Torre-Ubieta L., Bonni A., Colon-Ramos D.A.;
RT "A conserved PTEN/FOXO pathway regulates neuronal morphology during C.
RT elegans development.";
RL Development 138:5257-5267(2011).
RN [15] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP GLY-174.
RX PubMed=22916028; DOI=10.1371/journal.pgen.1002881;
RA Nakdimon I., Walser M., Froehli E., Hajnal A.;
RT "PTEN negatively regulates MAPK signaling during Caenorhabditis elegans
RT vulval development.";
RL PLoS Genet. 8:E1002881-E1002881(2012).
RN [16]
RP FUNCTION.
RX PubMed=25383666; DOI=10.1038/nsmb.2915;
RA Nakagawa A., Sullivan K.D., Xue D.;
RT "Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by
RT inhibiting the AKT pathway.";
RL Nat. Struct. Mol. Biol. 21:1082-1090(2014).
RN [17]
RP FUNCTION, INTERACTION WITH DAF-2, AND DISRUPTION PHENOTYPE.
RX PubMed=23995781; DOI=10.1038/onc.2013.347;
RA Liu J., Visser-Grieve S., Boudreau J., Yeung B., Lo S., Chamberlain G.,
RA Yu F., Sun T., Papanicolaou T., Lam A., Yang X., Chin-Sang I.;
RT "Insulin activates the insulin receptor to downregulate the PTEN tumour
RT suppressor.";
RL Oncogene 33:3878-3885(2014).
RN [18]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26552888; DOI=10.1242/dev.130252;
RA Narbonne P., Maddox P.S., Labbe J.C.;
RT "DAF-18/PTEN locally antagonizes insulin signalling to couple germline stem
RT cell proliferation to oocyte needs in C. elegans.";
RL Development 142:4230-4241(2015).
CC -!- FUNCTION: Acts as a dual-specificity protein phosphatase,
CC dephosphorylating tyrosine-, serine- and threonine-phosphorylated
CC proteins (By similarity). Also acts as a lipid phosphatase, removing
CC the phosphate in the D3 position of the inositol ring from
CC phosphatidylinositol 3,4,5-trisphosphate (PubMed:15637588). By
CC dephosphorylating PtdIns(3,4,5)P3 antagonizes PtdIns(3,4,5)P3
CC production by age-1/PI3K and thus, negatively regulates daf-2-mediated
CC processes including dauer formation, longevity, fat metabolism,
CC chemotaxis towards salt, thermotolerance and axon guidance
CC (PubMed:9885576, PubMed:10209098, PubMed:10377431, PubMed:16950159,
CC PubMed:19249087, PubMed:23995781, PubMed:10077613, PubMed:20207731).
CC Similarly, promotes apoptosis during embryonic development by
CC suppressing the recruitment of the prosurvival kinases akt-1/2 to the
CC plasma membrane (PubMed:25383666). In addition, regulates Z2/Z3
CC germline precursor cell cycle by maintaining them arrested at the G2
CC stage and by controlling their growth during L1 diapause
CC (PubMed:16631584). After sperm depletion in larvae and adult
CC hermaphrodites, promotes germline stem cell quiescence and oocyte
CC accumulation (PubMed:26552888). By dephosphorylating ephrin-like
CC receptor vab-1 on tyrosine residues, negatively regulates oocyte
CC maturation downstream of vab-1 and upstream of mpk-1, independently of
CC daf-2 (PubMed:19853560). Plays a role in postembryonic muscle arm
CC extensions (PubMed:18436204). Required for neurite outgrowth during AIY
CC interneuron embryonic development (PubMed:22069193). Mainly
CC independently of daf-2, negatively regulates vulva induction probably
CC by inhibiting mpk-1 phosphorylation (PubMed:22916028). Both lipid and
CC protein phosphatase activities are required for the regulation of vulva
CC induction (PubMed:22916028). {ECO:0000250|UniProtKB:P60484,
CC ECO:0000269|PubMed:10077613, ECO:0000269|PubMed:10209098,
CC ECO:0000269|PubMed:10377431, ECO:0000269|PubMed:16631584,
CC ECO:0000269|PubMed:16950159, ECO:0000269|PubMed:18436204,
CC ECO:0000269|PubMed:19249087, ECO:0000269|PubMed:19853560,
CC ECO:0000269|PubMed:20207731, ECO:0000269|PubMed:22069193,
CC ECO:0000269|PubMed:22916028, ECO:0000269|PubMed:23995781,
CC ECO:0000269|PubMed:25383666, ECO:0000269|PubMed:26552888,
CC ECO:0000269|PubMed:9885576, ECO:0000303|PubMed:15637588}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836,
CC ChEBI:CHEBI:58456; EC=3.1.3.67;
CC Evidence={ECO:0000305|PubMed:15637588};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P60484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000250|UniProtKB:P60484};
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;
CC Evidence={ECO:0000269|PubMed:19853560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-
CC trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416,
CC ChEBI:CHEBI:83419; Evidence={ECO:0000250|UniProtKB:P60484};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-
CC 3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-
CC (1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43560,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420,
CC ChEBI:CHEBI:83423; Evidence={ECO:0000250|UniProtKB:P60484};
CC -!- SUBUNIT: Interacts (via C-terminus) with vab-1 (via kinase domain); the
CC interaction is independent of vab-1 kinase activity (PubMed:19853560).
CC Interacts with arr-1 and mpz-1; the interaction may inhibit daf-18
CC (PubMed:20207731). Interacts (via C-terminus) with daf-2 (via kinase
CC domain) (PubMed:23995781). {ECO:0000269|PubMed:19853560,
CC ECO:0000269|PubMed:20207731, ECO:0000269|PubMed:23995781}.
CC -!- INTERACTION:
CC G5EE01; O61460: vab-1; NbExp=3; IntAct=EBI-2914422, EBI-1788319;
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:22069193}. Cell
CC membrane {ECO:0000269|PubMed:22916028}; Peripheral membrane protein
CC {ECO:0000269|PubMed:22916028}. Cell projection, axon
CC {ECO:0000269|PubMed:22069193}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22069193}. Cytoplasm {ECO:0000269|PubMed:22916028}.
CC Nucleus {ECO:0000269|PubMed:22916028}. Note=During vulva development,
CC localizes to the cytoplasm and the nucleus of vulva precursor cells and
CC of vulva cells at the Pn.p stage of L2 larvae. From the Pn.px to Pn.pxx
CC stage of L3/L4 larvae, localization increases at the plasma membrane
CC and becomes maximal at the Pn.pxxx stage of L4 larvae.
CC {ECO:0000269|PubMed:22916028}.
CC -!- TISSUE SPECIFICITY: Expressed in embryo, larvae and in adult germline
CC (at protein level) (PubMed:16481471, PubMed:22916028, PubMed:19853560).
CC Expressed at equal levels in the 6 vulva precursor cells (VPCs) of L2
CC larvae and in the descendant cells of the induced VPCs (at protein
CC level) (PubMed:22916028). Expressed in the uterus (at protein level)
CC (PubMed:22916028). Expressed in the Z2/Z3 germline precursors, oocytes,
CC several amphid neurons and weakly in the nerve cord (at protein level)
CC (PubMed:19853560). {ECO:0000269|PubMed:16481471,
CC ECO:0000269|PubMed:19853560, ECO:0000269|PubMed:22916028}.
CC -!- PTM: Phosphorylated by vab-1 on tyrosine residues which may promote
CC daf-18 degradation. {ECO:0000269|PubMed:19853560}.
CC -!- DISRUPTION PHENOTYPE: Mutants are viable but with a shorter lifespan.
CC They also fail to enter dauer stage under starvation conditions and 17
CC percent of mutants display vulval bursting (PubMed:10209098,
CC PubMed:10377431, PubMed:20207731). Unlike in wild-type animals,
CC germline stem cell proliferation continues following sperm depletion
CC and Z2/Z3 germline precursors continue to proliferate during L1
CC diapause (PubMed:16631584, PubMed:26552888). The number of unfertilized
CC eggs laid after sperm depletion is also increased (PubMed:26552888).
CC Prevents constitutive dauer entry and pharynx remodeling and restores
CC normal brood size in a daf-2 mutant background (PubMed:10209098,
CC PubMed:10377431). Prevents increase in lifespan in an arr-1 (ok401)
CC mutant background or in mpz-1 RNAi-mediated knockdown animals
CC (PubMed:20207731). Suppresses the increase in ovulation rate and mpk-1
CC phosphorylation in distal oocytes in a vab-1 (dx31) mutant background.
CC Restores normal axon extension of PLM neurons in a daf-2 (e1370) mutant
CC background (PubMed:23995781). RNAi-mediated knockdown prevents arrest
CC at the dauer larval stage in a daf-2 or age-1 mutant background
CC (PubMed:9885576, PubMed:10077613). In addition, suppresses increased
CC thermotolerance and fat storage and reduces daf-16 nuclear localization
CC in a daf-2 mutant background (PubMed:19249087).
CC {ECO:0000269|PubMed:10077613, ECO:0000269|PubMed:10209098,
CC ECO:0000269|PubMed:10377431, ECO:0000269|PubMed:16631584,
CC ECO:0000269|PubMed:19249087, ECO:0000269|PubMed:20207731,
CC ECO:0000269|PubMed:23995781, ECO:0000269|PubMed:26552888,
CC ECO:0000269|PubMed:9885576}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
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DR EMBL; AJ131181; CAA10315.1; -; mRNA.
DR EMBL; AF098286; AAD03420.1; -; mRNA.
DR EMBL; AF126286; AAD21620.1; -; mRNA.
DR EMBL; BX284604; CCD73977.1; -; Genomic_DNA.
DR PIR; T51924; T51924.
DR RefSeq; NP_499926.1; NM_067525.5.
DR AlphaFoldDB; G5EE01; -.
DR SMR; G5EE01; -.
DR ComplexPortal; CPX-3881; arr-1-mpz-1-daf-18 complex.
DR IntAct; G5EE01; 3.
DR STRING; 6239.T07A9.6; -.
DR EPD; G5EE01; -.
DR PaxDb; G5EE01; -.
DR PeptideAtlas; G5EE01; -.
DR EnsemblMetazoa; T07A9.6.1; T07A9.6.1; WBGene00000913.
DR GeneID; 176869; -.
DR KEGG; cel:CELE_T07A9.6; -.
DR CTD; 176869; -.
DR WormBase; T07A9.6; CE26385; WBGene00000913; daf-18.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000163053; -.
DR HOGENOM; CLU_307414_0_0_1; -.
DR InParanoid; G5EE01; -.
DR OMA; LIYPEQL; -.
DR OrthoDB; 1195490at2759; -.
DR Reactome; R-CEL-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-CEL-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR Reactome; R-CEL-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-CEL-202424; Downstream TCR signaling.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-5689896; Ovarian tumor domain proteases.
DR Reactome; R-CEL-8948747; Regulation of PTEN localization.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR SignaLink; G5EE01; -.
DR PRO; PR:G5EE01; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000913; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0062049; C:protein phosphatase inhibitor complex; IC:ComplexPortal.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; ISS:WormBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:WormBase.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR GO; GO:0007635; P:chemosensory behavior; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0007611; P:learning or memory; IMP:WormBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISS:WormBase.
DR GO; GO:0061066; P:positive regulation of dauer larval development; IMP:WormBase.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; IMP:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IMP:WormBase.
DR GO; GO:0006606; P:protein import into nucleus; IGI:WormBase.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:WormBase.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IGI:WormBase.
DR GO; GO:1902074; P:response to salt; IMP:UniProtKB.
DR CDD; cd14509; PTP_PTEN; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR045101; PTP_PTEN.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Hydrolase; Lipid metabolism;
KW Lipid-binding; Membrane; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..962
FT /note="Phosphatidylinositol 3,4,5-trisphosphate 3-
FT phosphatase and dual-specificity protein phosphatase daf-
FT 18"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437872"
FT DOMAIN 58..230
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 234..530
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 169
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590,
FT ECO:0000269|PubMed:19853560"
FT MUTAGEN 137
FT /note="D->A: Probable loss of phosphatase activity.
FT Stabilizes the interaction with vab-1."
FT /evidence="ECO:0000269|PubMed:19853560"
FT MUTAGEN 169
FT /note="C->S: Loss of tyrosine phosphatase activity."
FT /evidence="ECO:0000269|PubMed:19853560"
FT MUTAGEN 174
FT /note="G->E: Probable loss of lipid phosphatase activity
FT without affecting protein phosphatase activity. Fails to
FT prevent both constitutive dauer formation and increased
FT lifespan in a daf-2 (e1370) mutant background. Partially
FT increases the percentage of animals lacking a vulva in a
FT let-23 mutant background and partially reduces the number
FT of animals with multiple vulva in a gain-of-function let-60
FT mutant background."
FT /evidence="ECO:0000269|PubMed:15637588,
FT ECO:0000269|PubMed:22916028"
SQ SEQUENCE 962 AA; 110329 MW; 79212EF05C959837 CRC64;
MVTPPPDVPS TSTRSMARDL QENPNRQPGE PRVSEPYHNS IVERIRHIFR TAVSSNRCRT
EYQNIDLDCA YITDRIIAIG YPATGIEANF RNSKVQTQQF LTRRHGKGNV KVFNLRGGYY
YDADNFDGNV ICFDMTDHHP PSLELMAPFC REAKEWLEAD DKHVIAVHCK AGKGRTGVMI
CALLIYINFY PSPRQILDYY SIIRTKNNKG VTIPSQRRYI YYYHKLRERE LNYLPLRMQL
IGVYVERPPK TWGGGSKIKV EVGNGSTILF KPDPLIISKS NHQRERATWL NNCDTPNEFD
TGEQKYHGFV SKRAYCFMVP EDAPVFVEGD VRIDIREIGF LKKFSDGKIG HVWFNTMFAC
DGGLNGGHFE YVDKTQPYIG DDTSIGRKNG MRRNETPMRK IDPETGNEFE SPWQIVNPPG
LEKHITEEQA MENYTNYGMI PPRYTISKIL HEKHEKGIVK DDYNDRKLPM GDKSYTESGK
SGDIRGVGGP FEIPYKAEEH VLTFPVYEMD RALKSKDLNN GMKLHVVLRC VDTRDSKMME
KSEVFGNLAF HNESTRRLQA LTQMNPKWRP EPCAFGSKGA EMHYPPSVRY SSNDGKYNGA
CSENLVSDFF EHRNIAVLNR YCRYFYKQRS TSRSRYPRKF RYCPLIKKHF YIPADTDDVD
ENGQPFFHSP EHYIKEQEKI DAEKAAKGIE NTGPSTSGSS APGTIKKTEA SQSDKVKPAT
EDELPPARLP DNVRRFPVVG VDFENPEEES CEHKTVESIA GFEPLEHLFH ESYHPNTAGN
MLRQDYHTDS EVKIAEQEAK AFVDQLLNGQ GVLQEFMKQF KVPSDNSFAD YVTGQAEVFK
AQIALLEQSE DFQRVQANAE EVDLEHTLGE AFERFGHVVE ESNGSSKNPK ALKTREQMVK
ETGKDTQKTR NHVLLHLEAN HRVQIERRET CPELHPEDKI PRIAHFSENS FSDSNFDQAI
YL
