2A51_CAEEL
ID 2A51_CAEEL Reviewed; 542 AA.
AC O18178;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit pptr-1 {ECO:0000305};
DE AltName: Full=Serine/threonine-protein phosphatase 2A 56kDa regulatory subunit pptr-1 {ECO:0000305};
DE AltName: Full=Serine/threonine-protein phosphatase 2A regulatory subunit B' pptr-1 {ECO:0000305};
GN Name=pptr-1 {ECO:0000312|WormBase:W08G11.4};
GN ORFNames=W08G11.4 {ECO:0000312|WormBase:W08G11.4};
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|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 [2] {ECO:0000305}
RP FUNCTION, INTERACTION WITH AKT-1 AND SGK-1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, 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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21127218; DOI=10.1126/science.1193697;
RA Gallo C.M., Wang J.T., Motegi F., Seydoux G.;
RT "Cytoplasmic partitioning of P granule components is not required to
RT specify the germline in C. elegans.";
RL Science 330:1685-1689(2010).
RN [4]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH MEG-1; MEG-3 AND MEG-4.
RX PubMed=25535836; DOI=10.7554/elife.04591;
RA Wang J.T., Smith J., Chen B.C., Schmidt H., Rasoloson D., Paix A.,
RA Lambrus B.G., Calidas D., Betzig E., Seydoux G.;
RT "Regulation of RNA granule dynamics by phosphorylation of serine-rich,
RT intrinsically disordered proteins in C. elegans.";
RL Elife 3:e04591-e04591(2014).
CC -!- FUNCTION: Probable regulatory subunit of serine/threonine-protein
CC phosphatase let-92 which negatively regulates the insulin receptor
CC signaling cascade composed of daf-2, age-1, akt-1, akt-2 and sgk-1 by
CC promoting the dephosphorylation of akt-1 on 'Thr-350'
CC (PubMed:19249087). Negatively regulates several functions controlled by
CC the insulin pathway including dauer formation, lifespan, fat storage
CC and stress resistance (PubMed:19249087). Plays a role in the asymmetric
CC segregation of the P granule components during embryonic cell divisions
CC but does not play an essential role in specifying germ cell fate
CC (PubMed:21127218). Within a PP2A phosphatase complex, acts redundantly
CC with pptr-2, to dephosphorylate P granule components including meg-1
CC and meg-3 to promote the assembly and accumulation of zygotic P
CC granules in the posterior cytoplasm during zygote polarization, and
CC thus maintain P granule distribution and segregation in early stage
CC embryos following meiosis (PubMed:25535836). In adults, required to
CC promote germ cell proliferation and differentiation when exposed to
CC thermic stress (PubMed:21127218). {ECO:0000269|PubMed:19249087,
CC ECO:0000269|PubMed:21127218, ECO:0000269|PubMed:25535836}.
CC -!- SUBUNIT: Part of a complex consisting of a common heterodimeric core
CC enzyme, composed of catalytic subunit let-92 and constant regulatory
CC subunit paa-1, that associates with a variety of regulatory subunits
CC which confer distinct properties to the holoenzyme (Probable).
CC Interacts with akt-1 but not akt-2 (PubMed:19249087). Interacts with
CC sgk-1 (PubMed:19249087). Interacts with P granule components meg-1,
CC meg-3 and meg-4 (PubMed:25535836). {ECO:0000269|PubMed:19249087,
CC ECO:0000269|PubMed:25535836, ECO:0000305, ECO:0000305|PubMed:25535836}.
CC -!- INTERACTION:
CC O18178; Q17941: akt-1; NbExp=3; IntAct=EBI-2298122, EBI-1770718;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19249087}.
CC -!- TISSUE SPECIFICITY: Expressed in pharynx, vulva and spermatheca.
CC {ECO:0000269|PubMed:19249087}.
CC -!- DISRUPTION PHENOTYPE: Mutants have small gonads and the number of
CC progeny is reduced (PubMed:21127218). At higher temperatures, 20
CC percent of mutants are sterile with no gametes (PubMed:21127218).
CC Mutant embryos display several defects in P granule partitioning during
CC the first cell divisions. Unlike in wild-type, plg-1-positive granules
CC becomes unstable during mitosis resulting in their disassembly and in
CC the loss of asymmetric segregation of plg-1 between somatic and
CC germline blastomeres (PubMed:21127218). plg-1-positive granules reform
CC during interphase but are fewer and smaller (PubMed:21127218). By the
CC 100-cell stage, only small granules remain, and these are not enriched
CC in Z2/Z3 primordial germ cells compared to wild-type. In addition,
CC asymmetric segregation of cey-2 and nos-2 mRNAs, 2 components of P
CC granules, is lost without affecting their degradation in the somatic
CC lineage after cell division (PubMed:21127218). RNAi-mediated knockdown
CC suppresses constitutive dauer formation, and, increases lifespan, fat
CC storage and thermotolerance and reduces daf-16 nuclear localization in
CC a daf-2 (e1370) mutant background (PubMed:19249087).
CC {ECO:0000269|PubMed:19249087, ECO:0000269|PubMed:21127218}.
CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC family. {ECO:0000305}.
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DR EMBL; BX284605; CAB07297.4; -; Genomic_DNA.
DR RefSeq; NP_507133.4; NM_074732.5.
DR AlphaFoldDB; O18178; -.
DR SMR; O18178; -.
DR ComplexPortal; CPX-1367; PP2A-PPTR-1 phosphatase complex.
DR IntAct; O18178; 3.
DR STRING; 6239.W08G11.4; -.
DR EPD; O18178; -.
DR PaxDb; O18178; -.
DR PeptideAtlas; O18178; -.
DR EnsemblMetazoa; W08G11.4.1; W08G11.4.1; WBGene00012348.
DR GeneID; 180100; -.
DR KEGG; cel:CELE_W08G11.4; -.
DR UCSC; W08G11.4; c. elegans.
DR CTD; 180100; -.
DR WormBase; W08G11.4; CE32003; WBGene00012348; pptr-1.
DR eggNOG; KOG2085; Eukaryota.
DR GeneTree; ENSGT01030000234620; -.
DR HOGENOM; CLU_012437_4_0_1; -.
DR InParanoid; O18178; -.
DR OMA; NHEDQER; -.
DR OrthoDB; 890437at2759; -.
DR PhylomeDB; O18178; -.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-CEL-389513; CTLA4 inhibitory signaling.
DR Reactome; R-CEL-432142; Platelet sensitization by LDL.
DR Reactome; R-CEL-5673000; RAF activation.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR SignaLink; O18178; -.
DR PRO; PR:O18178; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012348; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0072542; F:protein phosphatase activator activity; IMP:WormBase.
DR GO; GO:0040024; P:dauer larval development; IGI:WormBase.
DR GO; GO:0008340; P:determination of adult lifespan; IGI:WormBase.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IGI:WormBase.
DR GO; GO:1903863; P:P granule assembly; IMP:WormBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:WormBase.
DR GO; GO:0010883; P:regulation of lipid storage; IGI:WormBase.
DR GO; GO:0009408; P:response to heat; IGI:WormBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002554; PP2A_B56.
DR PANTHER; PTHR10257; PTHR10257; 1.
DR Pfam; PF01603; B56; 1.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..542
FT /note="Serine/threonine-protein phosphatase 2A regulatory
FT subunit pptr-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437754"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 61835 MW; 4AA532BACB97CA92 CRC64;
MHGSGHSLTG APHQIPPPRT QGAATGGQQL SATANQFVDK IDPFHNKRGT SRRLRINNSS
RYNVDSAQEL VQLALIKDTA ANEQPALVIE KLVQCQHVFD FYDPVAQLKC KEIKRAALNE
LIDHITSTKG AIVETIYPAV IKMVAKNIFR VLPPSENCEF DPEEDEPTLE VSWPHLQLVY
ELFLRFLESP DFQASIGKKY IDQRFVLKLL DLFDSEDPRE RDFLKTVLHR IYGKFLGLRA
FIRKHINNMF LRFVYETDSF NGVGELLEIL GSIINGFALP LKQEHKVFLV KVLLPLHKPK
CLSLYHAQLA YCVVQFIEKD SSLTPQVFEA LLKFWPRTCS SKEVMFLGEV EEILDIIEPE
QFKKIIDPLF RQLAKCVSSP HFQVAERALY FWNNEYILSL IEDTSSLVMP IMFPALYRIS
KEHWNQTIVA LVYNVLKTFM EMNGKLFDEL TSTYKGERLR EKQREKDRDA FWKKMEALEL
NPPAEGKEVT PSLFPEKLTD YLKKDGPNMT PLPVATAGGG DKSPSVVKKS STGSETTTPA
KK
