GLC7A_CAEBR
ID GLC7A_CAEBR Reviewed; 329 AA.
AC Q61JR3; A8X8I2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Serine/threonine-protein phosphatase PP1-alpha;
DE EC=3.1.3.16;
DE AltName: Full=Glc seven-like phosphatase 1;
GN Name=gsp-1; ORFNames=CBG09676;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Serine/threonine-protein phosphatase which antagonizes the
CC function of air-2 in the regulation of chromosome cohesion.
CC Dephosphorylates histone H3 at 'Ser-10'. Also involved in the
CC activation of chloride channel clh-3 during cell swelling and meiotic
CC maturation (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; HE600998; CAP28943.1; -; Genomic_DNA.
DR RefSeq; XP_002637166.1; XM_002637120.1.
DR AlphaFoldDB; Q61JR3; -.
DR SMR; Q61JR3; -.
DR STRING; 6238.CBG09676; -.
DR EnsemblMetazoa; CBG09676.1; CBG09676.1; WBGene00031226.
DR GeneID; 8579162; -.
DR KEGG; cbr:CBG_09676; -.
DR CTD; 8579162; -.
DR WormBase; CBG09676; CBP02415; WBGene00031226; Cbr-gsp-1.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; Q61JR3; -.
DR OMA; TVQMSEN; -.
DR OrthoDB; 766640at2759; -.
DR Proteomes; UP000008549; 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; IEA:EnsemblMetazoa.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
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_0000268636"
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
