UniProtKB - Q8VD52 (PLPP_RAT)
Chronophin
Pdxp
Functioni
Functions as a 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 and therefore plays a role in vitamin B6 metabolism. Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine.
By similarityCatalytic activityi
- EC:3.1.3.74By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:3.1.3.74By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:3.1.3.74By similarityThis reaction proceeds in the backwardBy similarity direction.
- EC:3.1.3.16By similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 25 | NucleophileBy similarity | 1 | |
Metal bindingi | 25 | MagnesiumBy similarity | 1 | |
Active sitei | 27 | Proton donorBy similarity | 1 | |
Metal bindingi | 27 | Magnesium; via carbonyl oxygenBy similarity | 1 | |
Binding sitei | 178 | SubstrateBy similarity | 1 | |
Binding sitei | 209 | SubstrateBy similarity | 1 | |
Metal bindingi | 234 | MagnesiumBy similarity | 1 |
GO - Molecular functioni
- glycerol-3-phosphatase activity Source: GO_Central
- growth factor binding Source: RGD
- heat shock protein binding Source: RGD
- magnesium ion binding Source: UniProtKB
- phosphatase activity Source: GO_Central
- phosphoprotein phosphatase activity Source: UniProtKB
- protein homodimerization activity Source: RGD
- protein serine/threonine phosphatase activity Source: UniProtKB-EC
- pyridoxal phosphatase activity Source: UniProtKB
GO - Biological processi
- actin rod assembly Source: RGD
- cellular response to ATP Source: RGD
- dephosphorylation Source: RGD
- positive regulation of actin filament depolymerization Source: UniProtKB
- protein dephosphorylation Source: UniProtKB
- pyridoxal phosphate catabolic process Source: UniProtKB
- regulation of cytokinesis Source: UniProtKB
- regulation of mitotic nuclear division Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Ligand | Magnesium, Metal-binding, Pyridoxal phosphate |
Names & Taxonomyi
Protein namesi | |
Gene namesi | |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 1586212, Pdxp |
Subcellular locationi
Cytoplasm and Cytosol
- cytosol By similarity
Plasma membrane
- ruffle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
- lamellipodium 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
Cytoskeleton
- cytoskeleton 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
Cytoskeleton
- cytoskeleton Source: UniProtKB-SubCell
Cytosol
- cytosol Source: UniProtKB
Plasma Membrane
- lamellipodium membrane Source: UniProtKB-SubCell
- ruffle membrane Source: UniProtKB-SubCell
Other locations
- cell-cell junction Source: RGD
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000068839 | 1 – 309 | ChronophinAdd BLAST | 309 |
Proteomic databases
jPOSTi | Q8VD52 |
PaxDbi | Q8VD52 |
Interactioni
Subunit structurei
Homodimer.
By similarityGO - Molecular functioni
- growth factor binding Source: RGD
- heat shock protein binding Source: RGD
- protein homodimerization activity Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000064092 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 58 – 60 | Substrate bindingBy similarity | 3 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2882, Eukaryota |
InParanoidi | Q8VD52 |
PhylomeDBi | Q8VD52 |
Family and domain databases
Gene3Di | 3.40.50.1000, 2 hits |
InterProi | View protein in InterPro IPR036412, HAD-like_sf IPR006357, HAD-SF_hydro_IIA IPR023214, HAD_sf IPR006349, PGP_euk |
Pfami | View protein in Pfam PF13344, Hydrolase_6, 1 hit |
PIRSFi | PIRSF000915, PGP-type_phosphatase, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR01460, HAD-SF-IIA, 1 hit TIGR01452, PGP_euk, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
10 20 30 40 50
MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLAQA
60 70 80 90 100
GKATLFVSNN SRRARPELAL RFARLGFTGL RAEELFSSAV CAARLLRQRL
110 120 130 140 150
PGPPDAPGAV FVLGGEGLRA ELRAAGLRLA GDPGDDPRVR AVLVGYDEHF
160 170 180 190 200
SFAKLTEACA HLRDPDCLLV ATDRDPWHPL TDGSRTPGTG SLAAAVETAS
210 220 230 240 250
GRQALVVGKP SPYMFQCITE DFSVDPARML MVGDRLETDI LFGHRCGMTT
260 270 280 290 300
VLTLTGVSSL EEAQAYLAAG QHDLVPHYYV ESIADLMEGL GGLSPPPQFP
DPVDGGYRP
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketB2GV79 | B2GV79_RAT | Chronophin | Pdxp | 292 | Annotation score: | ||
A0A8I6AIF9 | A0A8I6AIF9_RAT | Chronophin | Pdxp rCG_59788 | 105 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 106 – 108 | APG → GTR in AAL37168 (Ref. 2) Curated | 3 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AABR03056024 Genomic DNA No translation available. AF318578 mRNA Translation: AAL37168.1 |
Genome annotation databases
UCSCi | RGD:1586212, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AABR03056024 Genomic DNA No translation available. AF318578 mRNA Translation: AAL37168.1 |
3D structure databases
AlphaFoldDBi | Q8VD52 |
SMRi | Q8VD52 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000064092 |
Proteomic databases
jPOSTi | Q8VD52 |
PaxDbi | Q8VD52 |
Genome annotation databases
UCSCi | RGD:1586212, rat |
Organism-specific databases
RGDi | 1586212, Pdxp |
Phylogenomic databases
eggNOGi | KOG2882, Eukaryota |
InParanoidi | Q8VD52 |
PhylomeDBi | Q8VD52 |
Miscellaneous databases
PROi | PR:Q8VD52 |
Family and domain databases
Gene3Di | 3.40.50.1000, 2 hits |
InterProi | View protein in InterPro IPR036412, HAD-like_sf IPR006357, HAD-SF_hydro_IIA IPR023214, HAD_sf IPR006349, PGP_euk |
Pfami | View protein in Pfam PF13344, Hydrolase_6, 1 hit |
PIRSFi | PIRSF000915, PGP-type_phosphatase, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR01460, HAD-SF-IIA, 1 hit TIGR01452, PGP_euk, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PLPP_RAT | |
Accessioni | Q8VD52Primary (citable) accession number: Q8VD52 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 1, 2004 |
Last sequence update: | January 10, 2006 | |
Last modified: | May 25, 2022 | |
This is version 120 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families