PP1_BRANA
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 03-AUG-2022, entry version 89.
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 Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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
