PP1_BRAOL
ID PP1_BRAOL Reviewed; 316 AA.
AC P48487;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Serine/threonine-protein phosphatase PP1;
DE EC=3.1.3.16;
GN Name=PP1;
OS Brassica oleracea (Wild cabbage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3712;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Flower;
RX PubMed=1330067; DOI=10.1007/bf00040596;
RA Rundle S.J., Nasrallah J.B.;
RT "Molecular characterization of type 1 serine/threonine phosphatases from
RT Brassica oleracea.";
RL Plant Mol. Biol. 20:367-375(1992).
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; X63558; CAA45119.1; -; mRNA.
DR PIR; S26225; S26225.
DR AlphaFoldDB; P48487; -.
DR SMR; P48487; -.
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 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 2: Evidence at transcript level;
KW Hydrolase; Manganese; Metal-binding; Protein phosphatase.
FT CHAIN 1..316
FT /note="Serine/threonine-protein phosphatase PP1"
FT /id="PRO_0000058806"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 316 AA; 35902 MW; 66D5131A3ECA4DF0 CRC64;
MAEKPAPEQE QEQTRAMEPA VLDDIIRRLV EFRNTRPGSG KQVHLSEGEI RQLCAVSKDI
FLQQPILLEL EAPIKICGDI HGQYSDLLRL FEYGGFPPDA NYLFLGDYVD RGKQSLETIC
FLLAYKIKYP ENFFLLRGNH ECASINRIYG FYDECKRRFN VRLWKIFTDC FNCLPVAALI
DRILCMHGGI SPELMSLDQI RSISRPLDIP DSGLVCDLLW SDPSGDVKGW GANDRGVSYT
FGADTVAEFL QKNDMDLICR AHQVVEDGYE FFAERQVVTV FSAPNYCGEF DNAGAMMSID
ESLMCSFQIL KPSEKK
