ID PPP6_CAEEL Reviewed; 331 AA. AC Q09496; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 17-JAN-2003, sequence version 2. DT 27-MAR-2024, entry version 157. DE RecName: Full=Serine/threonine-protein phosphatase 6 catalytic subunit {ECO:0000305}; DE EC=3.1.3.16 {ECO:0000250|UniProtKB:O00743}; DE AltName: Full=Protein phosphatase pph-6 {ECO:0000303|PubMed:20040490}; GN Name=pph-6 {ECO:0000303|PubMed:20040490, GN ECO:0000312|WormBase:C34C12.3}; GN ORFNames=C34C12.3 {ECO:0000312|WormBase:C34C12.3}; 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; 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, IDENTIFICATION IN A COMPLEX WITH SAPS-1, SUBCELLULAR LOCATION, RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE. RX PubMed=20040490; DOI=10.1242/dev.042754; RA Afshar K., Werner M.E., Tse Y.C., Glotzer M., Goenczy P.; RT "Regulation of cortical contractility and spindle positioning by the RT protein phosphatase 6 PPH-6 in one-cell stage C. elegans embryos."; RL Development 137:237-247(2010). RN [3] RP ERRATUM OF PUBMED:20040490. RX PubMed=27436042; DOI=10.1242/dev.141515; RA Afshar K., Werner M.E., Tse Y.C., Glotzer M., Goenczy P.; RL Development 143:2689-2689(2016). CC -!- FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6) (By CC similarity). In complex with saps-1, promotes actomyosin contractility CC during cytokinesis by regulating the organization of cortical non- CC muscle myosin II nmy-2 and thus contributing to correct spindle CC positioning (PubMed:20040490). Also required for the proper generation CC of pulling forces on spindle poles during anaphase by regulating the CC cortical localization of gpr-1, gpr-2 and lin-5 (PubMed:20040490). CC {ECO:0000250|UniProtKB:O00743, ECO:0000269|PubMed:20040490}. 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:O00743}; 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:O00743}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P36873}; CC Note=Binds 2 manganese ions per subunit. CC {ECO:0000250|UniProtKB:P36873}; CC -!- SUBUNIT: Forms a complex composed of catalytic subunit pph-6 and CC regulatory subunit saps-1; the interaction increases pph-6 and saps-1 CC protein stability. {ECO:0000269|PubMed:20040490}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20040490}. CC Cytoplasm, cell cortex {ECO:0000269|PubMed:20040490}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:20040490}. Cytoplasm, cytoskeleton, CC spindle pole {ECO:0000269|PubMed:20040490}. Note=In embryos, localizes CC mainly to the cytoplasm and to a lesser extent with microtubule asters. CC {ECO:0000269|PubMed:20040490}. CC -!- DEVELOPMENTAL STAGE: Expressed in embryos. CC {ECO:0000269|PubMed:20040490}. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes lethality in 17 CC percent of animals. In the 1-cell embryo, cortical contractions are CC severely reduced and the pseudocleavage furrow is absent. Positioning CC of the spindle is abnormal due to reduced pulling forces that prevent CC oscillatory movements of the posterior spindle pole during anaphase. In CC 15 percent of animals, causes defects in chromosome segregation CC resulting in daughter cells with multiple nuclei. CC {ECO:0000269|PubMed:20040490}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V) CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284603; CAA87100.2; -; Genomic_DNA. DR PIR; T19701; T19701. DR RefSeq; NP_497714.2; NM_065313.5. DR AlphaFoldDB; Q09496; -. DR SMR; Q09496; -. DR BioGRID; 48030; 5. DR ComplexPortal; CPX-4025; pph-6-saps-1 phosphatase complex. DR IntAct; Q09496; 1. DR STRING; 6239.C34C12.3.1; -. DR EPD; Q09496; -. DR PaxDb; 6239-C34C12-3; -. DR PeptideAtlas; Q09496; -. DR EnsemblMetazoa; C34C12.3.1; C34C12.3.1; WBGene00007922. DR GeneID; 183199; -. DR KEGG; cel:CELE_C34C12.3; -. DR UCSC; C34C12.3; c. elegans. DR AGR; WB:WBGene00007922; -. DR WormBase; C34C12.3; CE31433; WBGene00007922; pph-6. DR eggNOG; KOG0373; Eukaryota. DR GeneTree; ENSGT00550000074961; -. DR HOGENOM; CLU_004962_8_1_1; -. DR InParanoid; Q09496; -. DR OMA; MEGFKYH; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; Q09496; -. DR PRO; PR:Q09496; -. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00007922; Expressed in embryo and 4 other cell types or tissues. DR GO; GO:0000235; C:astral microtubule; IDA:WormBase. DR GO; GO:0005938; C:cell cortex; IDA:WormBase. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:1903293; C:phosphatase complex; IPI:ComplexPortal. DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell. 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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central. DR GO; GO:0000916; P:actomyosin contractile ring contraction; NAS:ComplexPortal. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:WormBase. DR GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase. DR GO; GO:0030590; P:first cell cycle pseudocleavage; IMP:WormBase. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central. DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0051653; P:spindle localization; NAS:ComplexPortal. DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR047129; PPA2-like. DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase. DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1. DR PANTHER; PTHR45619:SF10; SERINE_THREONINE-PROTEIN PHOSPHATASE 6 CATALYTIC SUBUNIT; 1. DR Pfam; PF00149; Metallophos; 1. DR PRINTS; PR00114; STPHPHTASE. DR SMART; SM00156; PP2Ac; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1. PE 1: Evidence at protein level; KW Cell cycle; Cytoplasm; Cytoskeleton; Hydrolase; Manganese; Metal-binding; KW Protein phosphatase; Reference proteome. FT CHAIN 1..331 FT /note="Serine/threonine-protein phosphatase 6 catalytic FT subunit" FT /id="PRO_0000058917" FT ACT_SITE 140 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 79 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 81 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 107 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 107 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 139 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 189 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" FT BINDING 264 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P36873" SQ SEQUENCE 331 AA; 37388 MW; ACE68C04772E9262 CRC64; MIDTNLLRVT VCDEGELEKS TTHFIGSRKI EPEQWITWAS ECKYLPESDA VALCATLIDR LSLEANVVPV SSPVTICGDI HGQFYDLLEL FKTGGTVPNT KYVFMGDYVD RGHYSLETVT LLFCLLLKYP NQITLLRGNH ESRRISNVYG FYDECQNKYG HGNVHKWFCK VFDVLPIGAL IDESVLCVHG GLSPDIRTID SLMLLDRAQE VPNKGPLCDI MWSDPDDDVE DWVISQRGAG FVFGAKVTEE FLMNNDLSLL CRSHQLVDEG FKYMFNEKLA TVWSAPNYCY RCGNAAAVFE IDGNNRSTKY FNAVPDGSRE KPDRVVAPYF L //