PPP5_CAEEL
ID PPP5_CAEEL Reviewed; 496 AA.
AC Q9NES8;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Serine/threonine-protein phosphatase 5 {ECO:0000250|UniProtKB:P53041};
DE EC=3.1.3.16 {ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:26593036};
GN Name=pph-5 {ECO:0000312|WormBase:Y39B6A.2a};
GN ORFNames=Y39B6A.2 {ECO:0000312|WormBase:Y39B6A.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
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]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF PRO-375.
RX PubMed=21878498; DOI=10.1242/jcs.073379;
RA Richie C.T., Bembenek J.N., Chestnut B., Furuta T., Schumacher J.M.,
RA Wallenfang M., Golden A.;
RT "Protein phosphatase 5 is a negative regulator of separase function during
RT cortical granule exocytosis in C. elegans.";
RL J. Cell Sci. 124:2903-2913(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=23569206; DOI=10.1074/jbc.m112.439257;
RA Eckl J.M., Rutz D.A., Haslbeck V., Zierer B.K., Reinstein J., Richter K.;
RT "Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90)
RT motility by interaction with N-terminal and middle domain binding sites.";
RL J. Biol. Chem. 288:16032-16042(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH
RP DAF-21.
RX PubMed=26593036; DOI=10.1038/srep17058;
RA Haslbeck V., Eckl J.M., Drazic A., Rutz D.A., Lorenz O.R., Zimmermann K.,
RA Kriehuber T., Lindemann C., Madl T., Richter K.;
RT "The activity of protein phosphatase 5 towards native clients is modulated
RT by the middle- and C-terminal domains of Hsp90.";
RL Sci. Rep. 5:17058-17058(2015).
CC -!- FUNCTION: Serine/threonine-protein phosphatase (PubMed:23569206,
CC PubMed:26593036). Dephosphorylates cdc-37 (PubMed:23569206). Probably
CC by dephosphorylating separase sep-1, may be involved in sep-1-mediated
CC exocytosis of cortical granules during meiotic anaphase and mitotic
CC cytokinesis (PubMed:21878498). {ECO:0000269|PubMed:21878498,
CC ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:26593036}.
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:0000269|PubMed:23569206, ECO:0000269|PubMed:26593036};
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:0000269|PubMed:23569206, ECO:0000269|PubMed:26593036};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53042};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P53042};
CC Note=Binds 2 Mg(2+) or Mn(2+) cations per subunit.
CC {ECO:0000250|UniProtKB:P53042};
CC -!- ACTIVITY REGULATION: Autoinhibited. In the autoinhibited state, the TPR
CC domain interacts with the catalytic region and prevents substrate
CC access to the catalytic pocket (By similarity). daf-21/Hsp90 probably
CC releases the autoinhibition by the TPR repeat (PubMed:26593036,
CC PubMed:23569206). {ECO:0000250|UniProtKB:P53042,
CC ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:26593036}.
CC -!- SUBUNIT: Interacts (via catalytic region) with daf-21/Hsp90 (via TPR
CC repeat-binding and central region); the interaction promotes pph-5
CC phosphatase activity. {ECO:0000269|PubMed:26593036}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21878498}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21878498}.
CC Note=Cytoplasmic localization during interphase, enriched at the
CC mitotic spindle matrix during metaphase and released from the spindle
CC during anaphase. {ECO:0000269|PubMed:21878498}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic and germline tissues.
CC {ECO:0000269|PubMed:21878498}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes no visible
CC phenotype. {ECO:0000269|PubMed:21878498}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-5 (PP-T)
CC subfamily. {ECO:0000305}.
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DR EMBL; BX284605; CAC51076.2; -; Genomic_DNA.
DR PIR; T45058; T45058.
DR RefSeq; NP_001256849.1; NM_001269920.1.
DR AlphaFoldDB; Q9NES8; -.
DR SMR; Q9NES8; -.
DR ComplexPortal; CPX-3983; Hsp90-cdc-37-pph-5 phosphatase complex.
DR DIP; DIP-25900N; -.
DR IntAct; Q9NES8; 3.
DR STRING; 6239.Y39B6A.2a; -.
DR EPD; Q9NES8; -.
DR PaxDb; Q9NES8; -.
DR PeptideAtlas; Q9NES8; -.
DR PRIDE; Q9NES8; -.
DR EnsemblMetazoa; Y39B6A.2a.1; Y39B6A.2a.1; WBGene00012665.
DR UCSC; Y39B6A.2; c. elegans.
DR WormBase; Y39B6A.2a; CE36619; WBGene00012665; pph-5.
DR eggNOG; KOG0376; Eukaryota.
DR GeneTree; ENSGT00940000158785; -.
DR HOGENOM; CLU_004962_5_2_1; -.
DR InParanoid; Q9NES8; -.
DR OMA; NHFFMSR; -.
DR OrthoDB; 671536at2759; -.
DR PhylomeDB; Q9NES8; -.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-CEL-8939211; ESR-mediated signaling.
DR PRO; PR:Q9NES8; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00012665; Expressed in adult organism and 4 other tissues.
DR ExpressionAtlas; Q9NES8; baseline and differential.
DR GO; GO:0101031; C:chaperone complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008287; C:protein serine/threonine phosphatase complex; IC:ComplexPortal.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0045920; P:negative regulation of exocytosis; IGI:WormBase.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0033365; P:protein localization to organelle; IMP:WormBase.
DR GO; GO:0045859; P:regulation of protein kinase activity; IC:ComplexPortal.
DR CDD; cd07417; MPP_PP5_C; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041753; PP5_C.
DR InterPro; IPR013235; PPP_dom.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR011236; Ser/Thr_PPase_5.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR45668:SF5; PTHR45668:SF5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF08321; PPP5; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Protein phosphatase; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..496
FT /note="Serine/threonine-protein phosphatase 5"
FT /evidence="ECO:0000305"
FT /id="PRO_0000437870"
FT REPEAT 29..62
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 63..95
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 96..129
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REGION 184..496
FT /note="Catalytic"
FT /evidence="ECO:0000305"
FT ACT_SITE 303
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 241
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 270
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 302..303
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 302
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 351
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT BINDING 426
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53041"
FT MUTAGEN 375
FT /note="P->E: In av101; no obvious defects. Restores
FT exocytosis of cortical granules, chromosome segregation,
FT cytokinesis and polar body extrusion in a sep-1 (ax110)
FT mutant background."
FT /evidence="ECO:0000269|PubMed:21878498"
SQ SEQUENCE 496 AA; 56462 MW; 2C872FF1700384EE CRC64;
MAATITDDIV ATVLESIEEK SYEDEKEKAG MIKDEANQFF KDQVYDVAAD LYSVAIEIHP
TAVLYGNRAQ AYLKKELYGS ALEDADNAIA IDPSYVKGFY RRATANMALG RFKKALTDYQ
AVVKVCPNDK DARAKFDECS KIVRRQKFEA AISTDHDKKT VAETLDINAM AIEDSYDGPR
LEDKITKEFV LQLIKTFKNQ QKLHKKYAFK MLLEFYNYVK SLPTMVEITV PTGKKFTICG
DVHGQFYDLC NIFEINGYPS ETNPYLFNGD FVDRGSFSVE TIFTMIGFKL LYPNHFFMSR
GNHESDVMNK MYGFEGEVKA KYTQQMCDMF TETFCWLPLC HLINEKIFVC HGGLFKEDGV
TLEDIRKTDR NRQPPDEGIM CDLLWSDPQP INGRSPSKRG VGCQFGPDVT SKWCETNGIE
YVVRSHEVKP EGYEMHHNGQ CFTVFSAPNY CDQMNNKGAF ITITGDNLTP RFTPFDAVPH
PKLPPMAYAN SLFGFN
