PPP6_CAEEL
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 03-AUG-2022, entry version 150.
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, 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}.
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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; -.
DR EPD; Q09496; -.
DR PaxDb; Q09496; -.
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 CTD; 183199; -.
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; CQNKYGN; -.
DR OrthoDB; 808922at2759; -.
DR PhylomeDB; Q09496; -.
DR PRO; PR:Q09496; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00007922; Expressed in embryo and 4 other 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; IC: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; IC:ComplexPortal.
DR GO; GO:0051653; P:spindle localization; IC:ComplexPortal.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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
