ID GLC7B_CAEEL Reviewed; 333 AA. AC P48727; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Serine/threonine-protein phosphatase PP1-beta; DE EC=3.1.3.16 {ECO:0000305|PubMed:30921322}; DE AltName: Full=CeGLC-7-beta; DE AltName: Full=Glc seven-like phosphatase 2; GN Name=gsp-2 {ECO:0000312|WormBase:F56C9.1}; GN Synonyms=Ce-glc-7beta {ECO:0000312|WormBase:F56C9.1}, CeGLC-7beta GN {ECO:0000312|WormBase:F56C9.1}, glc-7 {ECO:0000312|WormBase:F56C9.1}; GN ORFNames=F56C9.1 {ECO:0000312|WormBase:F56C9.1}; 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. RX PubMed=10975519; DOI=10.1016/s0092-8674(00)00034-9; RA Hsu J.-Y., Sun Z.-W., Li X., Reuben M., Tatchell K., Bishop D.K., RA Grushcow J.M., Brame C.J., Caldwell J.A., Hunt D.F., Lin R., Smith M.M., RA Allis C.D.; RT "Mitotic phosphorylation of histone H3 is governed by Ipl1/aurora kinase RT and Glc7/PP1 phosphatase in budding yeast and nematodes."; RL Cell 102:279-291(2000). RN [3] RP FUNCTION. RX PubMed=11940606; DOI=10.1083/jcb.200110045; RA Rogers E., Bishop J.D., Waddle J.A., Schumacher J.M., Lin R.; RT "The aurora kinase AIR-2 functions in the release of chromosome cohesion in RT Caenorhabditis elegans meiosis."; RL J. Cell Biol. 157:219-229(2002). RN [4] RP FUNCTION. RX PubMed=12163466; DOI=10.1083/jcb.200204142; RA Rutledge E., Denton J., Strange K.; RT "Cell cycle- and swelling-induced activation of a Caenorhabditis elegans RT ClC channel is mediated by CeGLC-7alpha/beta phosphatases."; RL J. Cell Biol. 158:435-444(2002). RN [5] RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP SUBCELLULAR LOCATION. RX PubMed=12837290; DOI=10.1016/s0014-4827(03)00157-5; RA Sassa T., Ueda-Ohba H., Kitamura K., Harada S., Hosono R.; RT "Role of Caenorhabditis elegans protein phosphatase type 1, CeGLC-7 beta, RT in metaphase to anaphase transition during embryonic development."; RL Exp. Cell Res. 287:350-360(2003). RN [6] RP FUNCTION. RX PubMed=14622138; DOI=10.1046/j.1365-2443.2003.00682.x; RA Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A.; RT "Caenorhabditis elegans RBX1 is essential for meiosis, mitotic chromosomal RT condensation and segregation, and cytokinesis."; RL Genes Cells 8:857-872(2003). RN [7] RP FUNCTION. RX PubMed=18923084; DOI=10.1101/gad.1691208; RA de Carvalho C.E., Zaaijer S., Smolikov S., Gu Y., Schumacher J.M., RA Colaiacovo M.P.; RT "LAB-1 antagonizes the Aurora B kinase in C. elegans."; RL Genes Dev. 22:2869-2885(2008). RN [8] RP INTERACTION WITH LAB-1. RX PubMed=22927794; DOI=10.1371/journal.pbio.1001378; RA Tzur Y.B., Egydio de Carvalho C., Nadarajan S., Van Bostelen I., Gu Y., RA Chu D.S., Cheeseman I.M., Colaiacovo M.P.; RT "LAB-1 targets PP1 and restricts Aurora B kinase upon entrance into meiosis RT to promote sister chromatid cohesion."; RL PLoS Biol. 10:E1001378-E1001378(2012). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP ASP-252. RX PubMed=30921322; DOI=10.1371/journal.pgen.1008004; RA Billmyre K.K., Doebley A.L., Spichal M., Heestand B., Belicard T., RA Sato-Carlton A., Flibotte S., Simon M., Gnazzo M., Skop A., Moerman D., RA Carlton P.M., Sarkies P., Ahmed S.; RT "The meiotic phosphatase GSP-2/PP1 promotes germline immortality and small RT RNA-mediated genome silencing."; RL PLoS Genet. 15:E1008004-E1008004(2019). CC -!- FUNCTION: Serine/threonine-protein phosphatase essential for CC chromosomal dynamics during meiosis and mitosis. During meiosis, CC promotes chromosomal cohesion and germline immortality via a small RNA- CC mediated genome silencing pathway (PubMed:30921322). Antagonizes the CC function of air-2 kinase during meiosis I and mitosis to promote CC chromatid cohesion and spindle attachment (PubMed:18923084). CC Dephosphorylates histone H3 at 'Ser-10' (Probable). Dephosphorylates CC histone H3 at 'Thr-3' (Probable). Also involved in the activation of CC chloride channel clh-3 during cell swelling and meiotic maturation. CC Promotes small RNA-mediated genome silencing over multiple generations CC (PubMed:30921322). Essential for embryogenesis. CC {ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:11940606, CC ECO:0000269|PubMed:12163466, ECO:0000269|PubMed:12837290, CC ECO:0000269|PubMed:14622138, ECO:0000269|PubMed:18923084, CC ECO:0000269|PubMed:30921322, ECO:0000305|PubMed:30921322}. 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:0000305|PubMed:30921322}; 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:0000305|PubMed:30921322}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- ACTIVITY REGULATION: Inhibited by okadaic acid. CC {ECO:0000269|PubMed:12837290}. CC -!- SUBUNIT: Interacts with lab-1; the interaction is direct. CC {ECO:0000269|PubMed:22927794}. CC -!- INTERACTION: CC P48727; Q17604: lab-1; NbExp=2; IntAct=EBI-2418500, EBI-16011794; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12837290}. Nucleus CC {ECO:0000269|PubMed:12837290, ECO:0000269|PubMed:30921322}. CC Note=Localizes to nuclei in the mid-pachytene to diplotene phase of CC meiosis. {ECO:0000269|PubMed:30921322}. CC -!- TISSUE SPECIFICITY: Expressed in gonads, nervous system, intestine and CC muscles. {ECO:0000269|PubMed:12837290}. CC -!- DEVELOPMENTAL STAGE: Expressed at early embryonic stages. CC {ECO:0000269|PubMed:12837290}. CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily. CC {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; CCD61828.1; -; Genomic_DNA. DR PIR; T16476; T16476. DR RefSeq; NP_001022616.1; NM_001027445.4. DR AlphaFoldDB; P48727; -. DR SMR; P48727; -. DR BioGRID; 532125; 30. DR DIP; DIP-25119N; -. DR IntAct; P48727; 4. DR STRING; 6239.F56C9.1.1; -. DR EPD; P48727; -. DR PaxDb; 6239-F56C9-1; -. DR PeptideAtlas; P48727; -. DR EnsemblMetazoa; F56C9.1.1; F56C9.1.1; WBGene00001748. DR GeneID; 3564807; -. DR KEGG; cel:CELE_F56C9.1; -. DR UCSC; F56C9.1; c. elegans. DR AGR; WB:WBGene00001748; -. DR WormBase; F56C9.1; CE01319; WBGene00001748; gsp-2. DR eggNOG; KOG0374; Eukaryota. DR GeneTree; ENSGT00940000169490; -. DR HOGENOM; CLU_004962_0_0_1; -. DR InParanoid; P48727; -. DR OMA; SDDKMNI; -. DR OrthoDB; 19833at2759; -. DR PhylomeDB; P48727; -. DR Reactome; R-CEL-5673000; RAF activation. DR PRO; PR:P48727; -. DR Proteomes; UP000001940; Chromosome III. DR GO; GO:0005694; C:chromosome; IDA:WormBase. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0031965; C:nuclear membrane; IDA:WormBase. DR GO; GO:0005634; C:nucleus; IDA:WormBase. 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; IDA:WormBase. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR CDD; cd07414; MPP_PP1_PPKL; 1. 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 InterPro; IPR031675; STPPase_N. DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR11668:SF498; SERINE_THREONINE-PROTEIN PHOSPHATASE-RELATED; 1. DR Pfam; PF00149; Metallophos; 1. DR Pfam; PF16891; STPPase_N; 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; Cell division; Chromatin regulator; Cytoplasm; KW Developmental protein; Hydrolase; Manganese; Meiosis; Metal-binding; KW Mitosis; Nucleus; Protein phosphatase; Reference proteome. FT CHAIN 1..333 FT /note="Serine/threonine-protein phosphatase PP1-beta" FT /id="PRO_0000058913" FT REGION 306..333 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 124 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 63 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 65 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 91 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 123 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 172 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 247 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250" FT MUTAGEN 252 FT /note="D->N: In yp14; temperature-sensitive. Embryonic FT lethality in 6% of animals at 20 degrees Celsius and in FT 41.6% of animals at 25 degrees Celsius. Fertile at 20 FT degrees Celsius, but sterile at 25 Degrees Celsius. In FT sterile mutants at 25 degrees Celsius, 40% of oocytes FT contain unpaired chromosomes. Defective germ cell FT immortality at 20 degrees Celsius, which is more prominent FT at 25 degrees Celsius. The germ cell immortality defect is FT due to an X chromosome segregation defect, which results in FT a high proportion of male progeny (Him phenotype). FT Disrupted inheritance of small RNA-mediated genome FT silencing over multiple generations. Decreased levels of FT total 22GRNAs and miRNAs. Increased phosphorylation of FT histone H3 at 'Ser-10' and 'Thr-3' in oocytes at 25 degrees FT Celsius. Reduced di- and trimethylation of 'Lys-9' of FT histone H3 in the diakinesis phase of prophase I in meiotic FT oocytes at 25 degrees Celsius. Double knockout with the FT lab-1 tm1791, hrde-1 tm1200 or rsd-6 yp11 mutant increases FT the incidence of sterility at 25 degrees Celsius as FT compared to the single mutants." FT /evidence="ECO:0000269|PubMed:30921322" SQ SEQUENCE 333 AA; 37792 MW; A73CE460AC78054E CRC64; MDVEKLNLDN IISRLLEVRG SKPGKNVQLT ESEIKGLCQK SREIFLSQPI LLELEAPLKI CGDVHGQYYD LLRLFEYGGF PPESNYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPV AAIIDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDQGLL CDLLWSDPDK DVTGWGENDR GVSFTFGPEV VAKFLHKHDL DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGS MMTVDETLMC SFQILKPADK KKYPYGAGGV GSNRPVTPPR NAPAAQPKKG AKK //