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Pyridoxal phosphate phosphatase (PLP phosphatase) (EC 3.1.3.3) (EC 3.1.3.74) (Chronophin)

 PLPP_MOUSE              Reviewed;         292 AA.
P60487;
01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2004, sequence version 1.
25-APR-2018, entry version 122.
RecName: Full=Pyridoxal phosphate phosphatase;
Short=PLP phosphatase;
EC=3.1.3.3 {ECO:0000269|PubMed:24338473};
EC=3.1.3.74 {ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687};
AltName: Full=Chronophin {ECO:0000303|PubMed:24338473};
Name=Pdxp; Synonyms=Cin, Plp, Plpp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=SWR/J; TISSUE=Brain;
PubMed=14522954; DOI=10.1074/jbc.M309619200;
Jang Y.M., Kim D.W., Kang T.-C., Won M.H., Baek N.-I., Moon B.J.,
Choi S.Y., Kwon O.-S.;
"Human pyridoxal phosphatase. Molecular cloning, functional
expression, and tissue distribution.";
J. Biol. Chem. 278:50040-50046(2003).
[2]
PROTEIN SEQUENCE OF 100-119 AND 141-154, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-292.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Liver, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-100 AND 208-233 IN COMPLEX
WITH MAGNESIUM, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR,
ENZYME REGULATION, AND FUNCTION.
PubMed=24338473; DOI=10.1074/jbc.M113.503359;
Seifried A., Knobloch G., Duraphe P.S., Segerer G., Manhard J.,
Schindelin H., Schultz J., Gohla A.;
"Evolutionary and structural analyses of the mammalian haloacid
dehalogenase-type phosphatases AUM and chronophin provide insight into
the basis of their different substrate specificities.";
J. Biol. Chem. 289:3416-3431(2014).
[6]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
BERYLLIUM TRIFLUORIDE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, AND
MUTAGENESIS OF 194-ALA-ALA-195.
PubMed=24338687; DOI=10.1074/jbc.M113.536482;
Kestler C., Knobloch G., Tessmer I., Jeanclos E., Schindelin H.,
Gohla A.;
"Chronophin dimerization is required for proper positioning of its
substrate specificity loop.";
J. Biol. Chem. 289:3094-3103(2014).
-!- FUNCTION: Protein serine phosphatase that dephosphorylates 'Ser-3'
in cofilin and probably also dephosphorylates phospho-serine
residues in DSTN. Regulates cofilin-dependent actin cytoskeleton
reorganization. Required for normal progress through mitosis and
normal cytokinesis. Does not dephosphorylate phospho-threonines in
LIMK1. Does not dephosphorylate peptides containing phospho-
tyrosine (By similarity). Pyridoxal phosphate (PLP) phosphatase,
which also catalyzes the dephosphorylation of pyridoxine 5'-
phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of
substrate preference PLP > PNP > PMP (By similarity)
(PubMed:24338473, PubMed:24338687). {ECO:0000250|UniProtKB:Q96GD0,
ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687}.
-!- CATALYTIC ACTIVITY: Pyridoxal 5'-phosphate + H(2)O = pyridoxal +
phosphate. {ECO:0000269|PubMed:24338473,
ECO:0000269|PubMed:24338687}.
-!- CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)-
serine + phosphate. {ECO:0000269|PubMed:24338473}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:24338473};
Note=Divalent metal ions. Mg(2+) is the most effective.
{ECO:0000269|PubMed:24338473};
-!- ENZYME REGULATION: Inhibited by beryllium trifluoride.
{ECO:0000269|PubMed:24338473}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24338473,
ECO:0000269|PubMed:24338687}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q96GD0}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
{ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium
membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane
protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q96GD0}. Cell membrane
{ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin
cytoskeleton in membrane ruffles and lamellipodia. Diffusely
distributed throughout the cytosol during pro-metaphase and
metaphase. Detected at the dynamic cell poles during telophase.
Detected at the cleavage furrow and contractile ring during
cytokinesis. Transiently detected at the plasma membrane in late
stages of cytokinesis. Detected at the midbody.
{ECO:0000250|UniProtKB:Q96GD0}.
-!- TISSUE SPECIFICITY: Ubiquitous. highly expressed in brain (at
protein level). {ECO:0000269|PubMed:24338473}.
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AY366300; AAR12209.1; -; mRNA.
EMBL; BC058388; AAH58388.1; -; mRNA.
CCDS; CCDS27627.1; -.
RefSeq; NP_064667.2; NM_020271.3.
UniGene; Mm.263169; -.
PDB; 4BKM; X-ray; 2.65 A; A/B/C/D=1-100, A/B/C/D=208-292.
PDB; 4BX0; X-ray; 1.75 A; A=1-292.
PDB; 4BX2; X-ray; 2.19 A; A/B=1-292.
PDB; 4BX3; X-ray; 2.19 A; A/B=1-292.
PDB; 5AES; X-ray; 2.75 A; A/B=1-292.
PDBsum; 4BKM; -.
PDBsum; 4BX0; -.
PDBsum; 4BX2; -.
PDBsum; 4BX3; -.
PDBsum; 5AES; -.
ProteinModelPortal; P60487; -.
SMR; P60487; -.
STRING; 10090.ENSMUSP00000086796; -.
BindingDB; P60487; -.
ChEMBL; CHEMBL3425392; -.
iPTMnet; P60487; -.
PhosphoSitePlus; P60487; -.
REPRODUCTION-2DPAGE; P60487; -.
EPD; P60487; -.
MaxQB; P60487; -.
PaxDb; P60487; -.
PeptideAtlas; P60487; -.
PRIDE; P60487; -.
DNASU; 57028; -.
Ensembl; ENSMUST00000089378; ENSMUSP00000086796; ENSMUSG00000022436.
GeneID; 57028; -.
KEGG; mmu:57028; -.
UCSC; uc007wru.1; mouse.
CTD; 57026; -.
MGI; MGI:1919282; Pdxp.
eggNOG; KOG2882; Eukaryota.
eggNOG; COG0647; LUCA.
GeneTree; ENSGT00760000118863; -.
HOGENOM; HOG000068104; -.
HOVERGEN; HBG049429; -.
InParanoid; P60487; -.
KO; K07758; -.
OMA; RFMFECI; -.
PhylomeDB; P60487; -.
TreeFam; TF314344; -.
BRENDA; 3.1.3.74; 3474.
ChiTaRS; Pdxp; mouse.
PRO; PR:P60487; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022436; -.
CleanEx; MM_PDXP; -.
ExpressionAtlas; P60487; baseline and differential.
Genevisible; P60487; MM.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0032154; C:cleavage furrow; IEA:Ensembl.
GO; GO:0070938; C:contractile ring; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0030496; C:midbody; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IBA:GO_Central.
GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
GO; GO:0004647; F:phosphoserine phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0033883; F:pyridoxal phosphatase activity; IDA:UniProtKB.
GO; GO:0031247; P:actin rod assembly; ISO:MGI.
GO; GO:0071318; P:cellular response to ATP; ISO:MGI.
GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0032361; P:pyridoxal phosphate catabolic process; IDA:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
Gene3D; 3.40.50.1000; -; 3.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006357; HAD-SF_hydro_IIA.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006349; PGP_euk.
Pfam; PF13344; Hydrolase_6; 1.
PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
TIGRFAMs; TIGR01452; PGP_euk; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Hydrolase;
Magnesium; Membrane; Metal-binding; Pyridoxal phosphate;
Reference proteome.
CHAIN 1 292 Pyridoxal phosphate phosphatase.
/FTId=PRO_0000068838.
REGION 58 62 Substrate binding. {ECO:0000250}.
ACT_SITE 25 25 Nucleophile. {ECO:0000250}.
ACT_SITE 27 27 Proton donor. {ECO:0000250}.
METAL 25 25 Magnesium. {ECO:0000269|PubMed:24338473,
ECO:0000269|PubMed:24338687}.
METAL 27 27 Magnesium; via carbonyl oxygen.
{ECO:0000269|PubMed:24338473,
ECO:0000269|PubMed:24338687}.
METAL 234 234 Magnesium. {ECO:0000269|PubMed:24338473,
ECO:0000269|PubMed:24338687}.
BINDING 178 178 Substrate. {ECO:0000250}.
BINDING 209 209 Substrate. {ECO:0000250}.
MUTAGEN 194 195 AA->KK: Abolishes homodimerization.
Strongly decreases affinity for pyridoxal
phosphate. {ECO:0000269|PubMed:24338687}.
HELIX 9 18 {ECO:0000244|PDB:4BX0}.
STRAND 20 25 {ECO:0000244|PDB:4BX0}.
TURN 27 29 {ECO:0000244|PDB:4BX0}.
STRAND 30 32 {ECO:0000244|PDB:4BX0}.
HELIX 40 49 {ECO:0000244|PDB:4BX0}.
STRAND 53 58 {ECO:0000244|PDB:4BX0}.
HELIX 65 74 {ECO:0000244|PDB:4BX0}.
HELIX 82 84 {ECO:0000244|PDB:4BX0}.
STRAND 85 87 {ECO:0000244|PDB:4BX0}.
HELIX 88 99 {ECO:0000244|PDB:4BX0}.
TURN 104 106 {ECO:0000244|PDB:4BX2}.
STRAND 109 114 {ECO:0000244|PDB:4BX0}.
HELIX 116 124 {ECO:0000244|PDB:4BX0}.
STRAND 132 134 {ECO:0000244|PDB:4BX0}.
STRAND 139 144 {ECO:0000244|PDB:4BX0}.
HELIX 152 161 {ECO:0000244|PDB:4BX0}.
STRAND 167 172 {ECO:0000244|PDB:4BX0}.
STRAND 176 179 {ECO:0000244|PDB:4BX0}.
STRAND 185 187 {ECO:0000244|PDB:4BX0}.
HELIX 189 200 {ECO:0000244|PDB:4BX0}.
HELIX 213 221 {ECO:0000244|PDB:4BX0}.
HELIX 226 228 {ECO:0000244|PDB:4BX0}.
STRAND 229 234 {ECO:0000244|PDB:4BX0}.
TURN 236 238 {ECO:0000244|PDB:4BX0}.
HELIX 239 246 {ECO:0000244|PDB:4BX0}.
STRAND 249 257 {ECO:0000244|PDB:4BX0}.
HELIX 260 268 {ECO:0000244|PDB:4BX0}.
HELIX 272 274 {ECO:0000244|PDB:4BX0}.
STRAND 277 282 {ECO:0000244|PDB:4BX0}.
HELIX 283 289 {ECO:0000244|PDB:4BX0}.
SEQUENCE 292 AA; 31512 MW; B5F1B2C7E71A585D CRC64;
MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLARA GKNTLFVSNN
SRRARPELAL RFARLGFAGL RAEQLFSSAL CAARLLRQRL SGPPDASGAV FVLGGEGLRA
ELRAAGLRLA GDPGEDPRVR AVLVGYDEQF SFSRLTEACA HLRDPDCLLV ATDRDPWHPL
SDGSRTPGTG SLAAAVETAS GRQALVVGKP SPYMFQCITE DFSVDPARTL MVGDRLETDI
LFGHRCGMTT VLTLTGVSSL EEAQAYLTAG QRDLVPHYYV ESIADLMEGL ED


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