P60487 (PLPP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyridoxal phosphate phosphatase
Short name=PLP phosphatase
EC=3.1.3.3
EC=3.1.3.74

Alternative name(s):
Chronophin

Gene names

Name:	Pdxp
Synonyms:	Cin, Plp, Plpp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. 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 similarity.
Catalytic activity	Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate. O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.
Cofactor	Divalent ions. Magnesium is the most effective By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm › cytosol By similarity. Cytoplasm › cytoskeleton By similarity. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection › lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell membrane; Peripheral membrane protein; 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.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Ligand	Magnesium Metal-binding Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	actin rod assembly Inferred from sequence orthology PubMed 19000834. Source: MGI cellular response to ATP Inferred from sequence orthology PubMed 19000834. Source: MGI positive regulation of actin filament depolymerization Inferred from sequence or structural similarity. Source: UniProtKB protein dephosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	actin cytoskeleton Inferred from electronic annotation. Source: Compara cleavage furrow Inferred from electronic annotation. Source: Compara contractile ring Inferred from electronic annotation. Source: Compara cytosol Inferred from sequence or structural similarity. Source: UniProtKB lamellipodium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: Compara ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heat shock protein binding Inferred from sequence orthology PubMed 19000834. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB phosphoserine phosphatase activity Inferred from electronic annotation. Source: EC pyridoxal phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 292	292	Pyridoxal phosphate phosphatase		PRO_0000068838
Regions
	Region	58 – 62	5	Substrate binding By similarity
Sites
	Active site	25	1	Nucleophile By similarity
	Active site	27	1	Proton donor By similarity
	Metal binding	25	1	Magnesium By similarity
	Metal binding	234	1	Magnesium By similarity
	Binding site	178	1	Substrate By similarity
	Binding site	209	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P60487 [UniParc]. Last modified March 1, 2004. Version 1. Checksum: B5F1B2C7E71A585D	FASTA	292	31,512
	10 20 30 40 50 60 MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLARA GKNTLFVSNN 70 80 90 100 110 120 SRRARPELAL RFARLGFAGL RAEQLFSSAL CAARLLRQRL SGPPDASGAV FVLGGEGLRA 130 140 150 160 170 180 ELRAAGLRLA GDPGEDPRVR AVLVGYDEQF SFSRLTEACA HLRDPDCLLV ATDRDPWHPL 190 200 210 220 230 240 SDGSRTPGTG SLAAAVETAS GRQALVVGKP SPYMFQCITE DFSVDPARTL MVGDRLETDI 250 260 270 280 290 LFGHRCGMTT VLTLTGVSSL EEAQAYLTAG QRDLVPHYYV ESIADLMEGL ED

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY366300 mRNA. Translation: AAR12209.1. BC058388 mRNA. Translation: AAH58388.1.
IPI	IPI00118654.
RefSeq	NP_064667.2. NM_020271.3.
UniGene	Mm.263169.
3D structure databases
ProteinModelPortal	P60487.
SMR	P60487. Positions 2-290.
ModBase	Search...
PTM databases
PhosphoSite	P60487.
2D gel databases
REPRODUCTION-2DPAGE	P60487.
Proteomic databases
PaxDb	P60487.
PRIDE	P60487.
Protocols and materials databases
DNASU	57028.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000089378; ENSMUSP00000086796; ENSMUSG00000068221.
GeneID	57028.
KEGG	mmu:57028.
UCSC	uc007wru.1. mouse.
Organism-specific databases
CTD	57026.
MGI	MGI:1919282. Pdxp.
Phylogenomic databases
eggNOG	COG0647.
GeneTree	ENSGT00510000047020.
HOGENOM	HOG000068104.
HOVERGEN	HBG049429.
InParanoid	P60487.
KO	K07758.
OMA	WNGERAV.
OrthoDB	EOG44F69M.
Enzyme and pathway databases
BRENDA	3.1.3.74. 3474.
Gene expression databases
ArrayExpress	P60487.
Bgee	P60487.
CleanEx	MM_PDXP.
Genevestigator	P60487.
GermOnline	ENSMUSG00000068221. Mus musculus.
Family and domain databases
Gene3D	3.40.50.1000. 2 hits. 3.40.50.10410. 1 hit.
InterPro	IPR023214. HAD-like_dom. IPR006357. HAD-SF_hydro_IIA. IPR023215. NPhePase-like_dom. IPR006349. PGP_euk. [Graphical view]
Pfam	PF13344. Hydrolase_6. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01460. HAD-SF-IIA. 1 hit. TIGR01452. PGP_euk. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PDXP. mouse.
NextBio	313473.
SOURCE	Search...

Entry information

Entry name

PLPP_MOUSE

Accession

Primary (citable) accession number: P60487

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2004
Last sequence update:	March 1, 2004
Last modified:	April 3, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program