ID   PP1_BRANA               Reviewed;         255 AA.
AC   P23777;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1;
DE            EC=3.1.3.16;
DE   Flags: Fragment;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2176161; DOI=10.1016/0014-5793(90)80531-m;
RA   Mackintosh R.W., Haycox G., Hardie D.G., Cohen P.T.W.;
RT   "Identification by molecular cloning of two cDNA sequences from the plant
RT   Brassica napus which are very similar to mammalian protein phosphatases-1
RT   and -2A.";
RL   FEBS Lett. 276:156-160(1990).
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; X57438; CAA40686.1; -; mRNA.
DR   PIR; S12985; S12985.
DR   AlphaFoldDB; P23777; -.
DR   SMR; P23777; -.
DR   EnsemblPlants; CDX80617; CDX80617; GSBRNA2T00133753001.
DR   Gramene; CDX80617; CDX80617; GSBRNA2T00133753001.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF432; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 8; 1.
DR   Pfam; PF00149; Metallophos; 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   2: Evidence at transcript level;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase.
FT   CHAIN           <1..255
FT                   /note="Serine/threonine-protein phosphatase PP1"
FT                   /id="PRO_0000058805"
FT   ACT_SITE        63
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         2
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         4
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         111
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   255 AA;  28850 MW;  7BA2A62C12221D05 CRC64;
     GDIHGQYQDL LRLFEYGGYP PSANFLFLGD YVDRGKQSLE TICLLLAYKI RYPSKIYLLR
     GNHEDAKINR IYGFYDECKR RFNVRLWKIF TDCFNCLPVA ALIDDKILCM HGGLSPELDN
     LNQIREIQRP TEIPDSGLLC DLLWSDPDQK IEGWADSDRG ISCTFGADKV AEFLDKNDLD
     LICRGHQVVE DGYEFFAKRR LVTIFSAPNY GGEFDNAGAL LSVDESLVCS FEIMKPALAS
     SSGHPLKKVP KMGKS
//