GLC7B_CAEEL
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 03-AUG-2022, entry version 151.
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},
GN CeGLC-7beta {ECO:0000312|WormBase:F56C9.1},
GN 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; 28.
DR DIP; DIP-25119N; -.
DR IntAct; P48727; 4.
DR STRING; 6239.F56C9.1; -.
DR EPD; P48727; -.
DR PaxDb; P48727; -.
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 CTD; 3564807; -.
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; GDHECAR; -.
DR OrthoDB; 766640at2759; -.
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 GO; GO:0070262; P:peptidyl-serine dephosphorylation; IDA:WormBase.
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 Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 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; 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 22G RNAs 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
