PLPP_BOVIN
ID PLPP_BOVIN Reviewed; 296 AA.
AC Q3ZBF9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chronophin {ECO:0000303|PubMed:15580268};
DE EC=3.1.3.16 {ECO:0000269|PubMed:15580268};
DE EC=3.1.3.74 {ECO:0000250|UniProtKB:Q96GD0};
DE AltName: Full=Protein serine phosphatase {ECO:0000303|PubMed:15580268};
DE AltName: Full=Pyridoxal phosphate phosphatase {ECO:0000250|UniProtKB:Q96GD0};
DE Short=PLP phosphatase {ECO:0000250|UniProtKB:Q96GD0};
GN Name=PDXP {ECO:0000250|UniProtKB:Q96GD0};
GN Synonyms=CIN {ECO:0000303|PubMed:15580268};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15580268; DOI=10.1038/ncb1201;
RA Gohla A., Birkenfeld J., Bokoch G.M.;
RT "Chronophin, a novel HAD-type serine protein phosphatase, regulates
RT cofilin-dependent actin dynamics.";
RL Nat. Cell Biol. 7:21-29(2005).
CC -!- FUNCTION: Functions as a pyridoxal phosphate (PLP) phosphatase, which
CC also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP)
CC and pyridoxamine 5'-phosphate (PMP), with order of substrate preference
CC PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism (By
CC similarity). Also functions as a protein serine phosphatase that
CC specifically dephosphorylates 'Ser-3' in proteins of the actin-
CC depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby,
CC regulates cofilin-dependent actin cytoskeleton reorganization, being
CC required for normal progress through mitosis and normal cytokinesis.
CC Does not dephosphorylate phosphothreonines in LIMK1. Does not
CC dephosphorylate peptides containing phosphotyrosine (PubMed:15580268).
CC {ECO:0000250|UniProtKB:Q96GD0, ECO:0000269|PubMed:15580268}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20534;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pyridoxine 5'-phosphate = phosphate + pyridoxine;
CC Xref=Rhea:RHEA:25112, ChEBI:CHEBI:15377, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58589; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25113;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + pyridoxamine = H2O + pyridoxamine 5'-phosphate;
CC Xref=Rhea:RHEA:25135, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57761, ChEBI:CHEBI:58451; EC=3.1.3.74;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25137;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
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 Evidence={ECO:0000269|PubMed:15580268};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000269|PubMed:15580268};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96GD0};
CC Note=Divalent metal ions. Mg(2+) is the most effective.
CC {ECO:0000250|UniProtKB:Q96GD0};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96GD0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15580268}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96GD0}. Cell
CC projection, ruffle membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral
CC membrane protein {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0};
CC Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell projection,
CC lamellipodium membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin
CC cytoskeleton in membrane ruffles and lamellipodia. Diffusely
CC distributed throughout the cytosol during pro-metaphase and metaphase.
CC Detected at the dynamic cell poles during telophase. Detected at the
CC cleavage furrow and contractile ring during cytokinesis. Transiently
CC detected at the plasma membrane in late stages of cytokinesis. Detected
CC at the midbody. {ECO:0000250|UniProtKB:Q96GD0}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:15580268}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; BC103329; AAI03330.1; -; mRNA.
DR RefSeq; NP_001030207.1; NM_001035035.2.
DR AlphaFoldDB; Q3ZBF9; -.
DR SMR; Q3ZBF9; -.
DR STRING; 9913.ENSBTAP00000016505; -.
DR PaxDb; Q3ZBF9; -.
DR PeptideAtlas; Q3ZBF9; -.
DR GeneID; 506308; -.
DR KEGG; bta:506308; -.
DR CTD; 57026; -.
DR eggNOG; KOG2882; Eukaryota.
DR InParanoid; Q3ZBF9; -.
DR OrthoDB; 982374at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; ISS:UniProtKB.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0032361; P:pyridoxal phosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01452; PGP_euk; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Hydrolase;
KW Magnesium; Membrane; Metal-binding; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..296
FT /note="Chronophin"
FT /id="PRO_0000254016"
FT ACT_SITE 25
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT ACT_SITE 27
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 58..60
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q96GD0"
SQ SEQUENCE 296 AA; 31749 MW; A3F0B3AA9D5D1E19 CRC64;
MARCERLRGA ALRDVVGRAQ GVLFDCNGVL WNGERAVPGA PELLERLAQA GKATLFVSNN
SRRARPELAL RFARLGFGGL RSEQLFSSAL CAARLLRQRL LGPPDTQGAV FVLGGEGLRA
ELRAAGLRLA GDPSEDPGAA PRVRAVLVGY DEHFSFAKLS EACAHLRDPD CLLVATDRDP
WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITEHFSVDP GRTLMVGDRL
ETDILFGHRC GMTTVLTLTG VSSLEEAQAY LAAGQHDLVP HYYVESIADL MEGLED
