GLC7A_CAEEL
ID GLC7A_CAEEL Reviewed; 329 AA.
AC Q27497;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1999, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-alpha;
DE EC=3.1.3.16;
DE AltName: Full=CeGLC-7-alpha;
DE AltName: Full=Glc seven-like phosphatase 1;
GN Name=gsp-1 {ECO:0000312|WormBase:F29F11.6};
GN ORFNames=F29F11.6 {ECO:0000312|WormBase:F29F11.6};
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.
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=22719267; DOI=10.1371/journal.pgen.1002760;
RA Baker B.M., Nargund A.M., Sun T., Haynes C.M.;
RT "Protective coupling of mitochondrial function and protein synthesis via
RT the eIF2alpha kinase GCN-2.";
RL PLoS Genet. 8:E1002760-E1002760(2012).
CC -!- FUNCTION: Serine/threonine-protein phosphatase which antagonizes the
CC function of air-2 in the regulation of chromosome cohesion
CC (PubMed:11940606, PubMed:14622138). Dephosphorylates histone H3 at
CC 'Ser-10' (PubMed:10975519). Dephosphorylates translation initiation
CC factor eIF2alpha (PubMed:22719267). Involved in the activation of
CC chloride channel clh-3 during cell swelling and meiotic maturation
CC (PubMed:12163466). {ECO:0000269|PubMed:10975519,
CC ECO:0000269|PubMed:11940606, ECO:0000269|PubMed:12163466,
CC ECO:0000269|PubMed:14622138, ECO:0000269|PubMed:22719267}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with lab-1; the interaction is direct.
CC {ECO:0000269|PubMed:22927794}.
CC -!- INTERACTION:
CC Q27497; Q17604: lab-1; NbExp=3; IntAct=EBI-2416859, EBI-16011794;
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284605; CAA98273.1; -; Genomic_DNA.
DR PIR; T21553; T21553.
DR RefSeq; NP_001256249.1; NM_001269320.1.
DR RefSeq; NP_001256250.1; NM_001269321.1.
DR AlphaFoldDB; Q27497; -.
DR SMR; Q27497; -.
DR BioGRID; 44515; 10.
DR DIP; DIP-55373N; -.
DR IntAct; Q27497; 4.
DR STRING; 6239.F29F11.6a; -.
DR iPTMnet; Q27497; -.
DR EPD; Q27497; -.
DR PaxDb; Q27497; -.
DR EnsemblMetazoa; F29F11.6.1; F29F11.6.1; WBGene00001747.
DR GeneID; 179486; -.
DR KEGG; cel:CELE_F29F11.6; -.
DR UCSC; F29F11.6; c. elegans.
DR CTD; 179486; -.
DR WormBase; F29F11.6; CE20735; WBGene00001747; gsp-1.
DR eggNOG; KOG0374; Eukaryota.
DR GeneTree; ENSGT00940000154644; -.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; Q27497; -.
DR OMA; TVQMSEN; -.
DR OrthoDB; 766640at2759; -.
DR PhylomeDB; Q27497; -.
DR Reactome; R-CEL-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-CEL-5625740; RHO GTPases activate PKNs.
DR Reactome; R-CEL-5627123; RHO GTPases activate PAKs.
DR Reactome; R-CEL-5673000; RAF activation.
DR PRO; PR:Q27497; -.
DR Proteomes; UP000001940; Chromosome V.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:UniProtKB.
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; Hydrolase; Manganese;
KW Meiosis; Metal-binding; Mitosis; Protein phosphatase; Reference proteome.
FT CHAIN 1..329
FT /note="Serine/threonine-protein phosphatase PP1-alpha"
FT /id="PRO_0000268637"
FT REGION 309..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 37205 MW; 500145324CA16D1B CRC64;
MSNDGDLNID NLITRLLEVR GCRPGKPVTM SEAEIRALCH KSREIFLSQP ILLELEAPLK
ICGDIHGQYN DLLRLFEYGG FPPEANYLFL GDYVDRGKQS LETICLLLAY KVKYPENFFL
LRGNHECASI NRIYGFYDEC KRRFSIKLWK TFTDCFNCLP IAALIDEKIF CCHGGLSPDL
QNMEQIRRVM RPTDVPDTGL LCDLLWSDPD KDVTGWGEND RGVSFTFGPD VVAKFLNRHD
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG GMMSVDETLM CSFQILKPSE
KKAKYQYQGM NSGRPAVGGG RPGTTAGKK
