Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P60487

- PLPP_MOUSE

UniProt

P60487 - PLPP_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pyridoxal phosphate phosphatase

Gene

Pdxp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity). Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP.By similarity2 Publications

Catalytic activityi

Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.

Cofactori

Mg2+1 PublicationNote: Divalent metal ions. Mg(2+) is the most effective.1 Publication

Enzyme regulationi

Inhibited by beryllium trifluoride.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei25 – 251NucleophileBy similarity
Metal bindingi25 – 251Magnesium2 Publications
Active sitei27 – 271Proton donorBy similarity
Metal bindingi27 – 271Magnesium; via carbonyl oxygen2 Publications
Binding sitei178 – 1781SubstrateBy similarity
Binding sitei209 – 2091SubstrateBy similarity
Metal bindingi234 – 2341Magnesium2 Publications

GO - Molecular functioni

  1. heat shock protein binding Source: MGI
  2. magnesium ion binding Source: UniProtKB
  3. phosphoprotein phosphatase activity Source: UniProtKB
  4. phosphoserine phosphatase activity Source: UniProtKB-EC
  5. protein homodimerization activity Source: UniProtKB
  6. pyridoxal phosphatase activity Source: UniProtKB

GO - Biological processi

  1. actin rod assembly Source: MGI
  2. cellular response to ATP Source: MGI
  3. positive regulation of actin filament depolymerization Source: UniProtKB
  4. protein dephosphorylation Source: UniProtKB
  5. pyridoxal phosphate catabolic process Source: UniProtKB
  6. regulation of cytokinesis Source: UniProtKB
  7. regulation of mitosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi3.1.3.74. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal phosphate phosphatase (EC:3.1.3.3, EC:3.1.3.74)
Short name:
PLP phosphatase
Alternative name(s):
Chronophin
Gene namesi
Name:Pdxp
Synonyms:Cin, Plp, Plpp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1919282. Pdxp.

Subcellular locationi

Cytoplasmcytosol By similarity. Cytoplasmcytoskeleton By similarity. Cell projectionruffle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionlamellipodium membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
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 (By similarity).By similarity

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cell projection Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: UniProtKB
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1952AA → KK: Abolishes homodimerization. Strongly decreases affinity for pyridoxal phosphate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Pyridoxal phosphate phosphatasePRO_0000068838Add
BLAST

Proteomic databases

MaxQBiP60487.
PaxDbiP60487.
PRIDEiP60487.

2D gel databases

REPRODUCTION-2DPAGEP60487.

PTM databases

PhosphoSiteiP60487.

Expressioni

Tissue specificityi

Ubiquitous. highly expressed in brain (at protein level).1 Publication

Gene expression databases

BgeeiP60487.
CleanExiMM_PDXP.
ExpressionAtlasiP60487. baseline and differential.
GenevestigatoriP60487.

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810Combined sources
Beta strandi20 – 256Combined sources
Turni27 – 293Combined sources
Beta strandi30 – 323Combined sources
Helixi40 – 4910Combined sources
Beta strandi53 – 586Combined sources
Helixi65 – 7410Combined sources
Helixi82 – 843Combined sources
Beta strandi85 – 873Combined sources
Helixi88 – 9912Combined sources
Turni104 – 1063Combined sources
Beta strandi109 – 1146Combined sources
Helixi116 – 1249Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi139 – 1446Combined sources
Helixi152 – 16110Combined sources
Beta strandi167 – 1726Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi185 – 1873Combined sources
Helixi189 – 20012Combined sources
Helixi213 – 2219Combined sources
Helixi226 – 2283Combined sources
Beta strandi229 – 2346Combined sources
Turni236 – 2383Combined sources
Helixi239 – 2468Combined sources
Beta strandi249 – 2579Combined sources
Helixi260 – 2689Combined sources
Helixi272 – 2743Combined sources
Beta strandi277 – 2826Combined sources
Helixi283 – 2897Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BKMX-ray2.65A/B/C/D1-100[»]
A/B/C/D208-292[»]
4BX0X-ray1.75A1-292[»]
4BX2X-ray2.19A/B1-292[»]
4BX3X-ray2.19A/B1-292[»]
ProteinModelPortaliP60487.
SMRiP60487. Positions 1-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 625Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiCOG0647.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiP60487.
KOiK07758.
OMAiFECISSQ.
OrthoDBiEOG7XDBG1.
PhylomeDBiP60487.
TreeFamiTF314344.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

P60487-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLARA
60 70 80 90 100
GKNTLFVSNN SRRARPELAL RFARLGFAGL RAEQLFSSAL CAARLLRQRL
110 120 130 140 150
SGPPDASGAV FVLGGEGLRA ELRAAGLRLA GDPGEDPRVR AVLVGYDEQF
160 170 180 190 200
SFSRLTEACA HLRDPDCLLV ATDRDPWHPL SDGSRTPGTG SLAAAVETAS
210 220 230 240 250
GRQALVVGKP SPYMFQCITE DFSVDPARTL MVGDRLETDI LFGHRCGMTT
260 270 280 290
VLTLTGVSSL EEAQAYLTAG QRDLVPHYYV ESIADLMEGL ED
Length:292
Mass (Da):31,512
Last modified:March 1, 2004 - v1
Checksum:iB5F1B2C7E71A585D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY366300 mRNA. Translation: AAR12209.1.
BC058388 mRNA. Translation: AAH58388.1.
CCDSiCCDS27627.1.
RefSeqiNP_064667.2. NM_020271.3.
UniGeneiMm.263169.

Genome annotation databases

EnsembliENSMUST00000089378; ENSMUSP00000086796; ENSMUSG00000022436.
GeneIDi57028.
KEGGimmu:57028.
UCSCiuc007wru.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY366300 mRNA. Translation: AAR12209.1 .
BC058388 mRNA. Translation: AAH58388.1 .
CCDSi CCDS27627.1.
RefSeqi NP_064667.2. NM_020271.3.
UniGenei Mm.263169.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BKM X-ray 2.65 A/B/C/D 1-100 [» ]
A/B/C/D 208-292 [» ]
4BX0 X-ray 1.75 A 1-292 [» ]
4BX2 X-ray 2.19 A/B 1-292 [» ]
4BX3 X-ray 2.19 A/B 1-292 [» ]
ProteinModelPortali P60487.
SMRi P60487. Positions 1-291.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei P60487.

2D gel databases

REPRODUCTION-2DPAGE P60487.

Proteomic databases

MaxQBi P60487.
PaxDbi P60487.
PRIDEi P60487.

Protocols and materials databases

DNASUi 57028.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000089378 ; ENSMUSP00000086796 ; ENSMUSG00000022436 .
GeneIDi 57028.
KEGGi mmu:57028.
UCSCi uc007wru.1. mouse.

Organism-specific databases

CTDi 57026.
MGIi MGI:1919282. Pdxp.

Phylogenomic databases

eggNOGi COG0647.
GeneTreei ENSGT00760000118863.
HOGENOMi HOG000068104.
HOVERGENi HBG049429.
InParanoidi P60487.
KOi K07758.
OMAi FECISSQ.
OrthoDBi EOG7XDBG1.
PhylomeDBi P60487.
TreeFami TF314344.

Enzyme and pathway databases

BRENDAi 3.1.3.74. 3474.

Miscellaneous databases

NextBioi 313473.
PROi P60487.
SOURCEi Search...

Gene expression databases

Bgeei P60487.
CleanExi MM_PDXP.
ExpressionAtlasi P60487. baseline and differential.
Genevestigatori P60487.

Family and domain databases

Gene3Di 3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProi IPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view ]
Pfami PF13344. Hydrolase_6. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution."
    Jang Y.M., Kim D.W., Kang T.-C., Won M.H., Baek N.-I., Moon B.J., Choi S.Y., Kwon O.-S.
    J. Biol. Chem. 278:50040-50046(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Swiss.
    Tissue: Brain.
  2. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 100-119 AND 141-154, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-292.
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Evolutionary and structural analyses of the mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities."
    Seifried A., Knobloch G., Duraphe P.S., Segerer G., Manhard J., Schindelin H., Schultz J., Gohla A.
    J. Biol. Chem. 289:3416-3431(2014)
    Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-100 AND 208-233 IN COMPLEX WITH MAGNESIUM, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, FUNCTION.
  5. "Chronophin dimerization is required for proper positioning of its substrate specificity loop."
    Kestler C., Knobloch G., Tessmer I., Jeanclos E., Schindelin H., Gohla A.
    J. Biol. Chem. 289:3094-3103(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND BERYLLIUM TRIFLUORIDE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, MUTAGENESIS OF 194-ALA-ALA-195.

Entry informationi

Entry nameiPLPP_MOUSE
AccessioniPrimary (citable) accession number: P60487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: November 26, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3