ID   PP11_ACEPE              Reviewed;         319 AA.
AC   P48480;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 90.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1 isozyme 1;
DE            EC=3.1.3.16;
OS   Acetabularia peniculus (Green alga) (Polyphysa peniculus).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Ulvophyceae;
OC   TCBD clade; Dasycladales; Polyphysaceae; Acetabularia.
OX   NCBI_TaxID=35862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7664759;
RA   Menzel D., Vugrek O., Frank S., Elsner-Menzel C.;
RT   "Protein phosphatase 2A, a potential regulator of actin dynamics and actin-
RT   based organelle motility in the green alga Acetabularia.";
RL   Eur. J. Cell Biol. 67:179-187(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = 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=O-phospho-L-threonyl-[protein] + H2O = 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; Z28627; CAA82263.1; -; Genomic_DNA.
DR   AlphaFoldDB; P48480; -.
DR   SMR; P48480; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   FunFam; 3.60.21.10:FF:000004; Serine/threonine-protein phosphatase; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR050341; PP1_catalytic_subunit.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF300; SERINE_THREONINE-PROTEIN PHOSPHATASE; 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   3: Inferred from homology;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase.
FT   CHAIN           1..319
FT                   /note="Serine/threonine-protein phosphatase PP1 isozyme 1"
FT                   /id="PRO_0000058795"
FT   REGION          299..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        122
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         61
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
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         89
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         89
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   319 AA;  36313 MW;  80696B708B768E22 CRC64;
     MDESTVDDVI ERLLEVRNNR PGKQVQLTES EIRLLCLTSK EILSEQPNLL ELEAPIKICG
     DIHGQYTDLL RLFEYGGFPP EANYLFLGDY VDRGKQSLET ICLLLAFKIK YPENFFILRG
     NHECASINRI YGFYDECKRR YNIRLWKTFT DCFNCLPVAA IVDEKILCMH GGLSPELKTL
     EQIRRIPRPT DVPDTGLLCD LLWADPDKDV QGWGENDRGV SYTFGPDTVT EFLQRHDLDL
     VCRAHQVVED GYEFFAKRQL VTLFSAPNYC GEFDNAGALM SVDDTLMCSF QILKPSEKKG
     KFMQGGNSLA GAGRGTPRR
//