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UniProtKB - O14495 (PLPP3_HUMAN)

Entry version 171 (17 Jun 2020)
Sequence version 1 (01 Jan 1998)
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Protein

Phospholipid phosphatase 3

Gene

PLPP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:9705349, PubMed:9607309, PubMed:27694435). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). Has both an extracellular and an intracellular phosphatase activity, allowing the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (PubMed:9607309, PubMed:23591818, PubMed:27694435). Through the dephosphorylation of extracellular sphingosine-1-phosphate and the regulation of its extra- and intracellular availability, plays a role in vascular homeostasis, regulating endothelial cell migration, adhesion, survival, proliferation and the production of pro-inflammatory cytokines (PubMed:27694435). By maintaining the appropriate levels of this lipid in the cerebellum, also ensure its proper development and function (By similarity). Through its intracellular lipid phosphatase activity may act in early compartments of the secretory pathway, regulating the formation of Golgi to endoplasmic reticulum retrograde transport carriers (PubMed:23591818).By similarity4 Publications
Independently of this phosphatase activity may also function in the Wnt signaling pathway and the stabilization of beta-catenin/CTNNB1, thereby regulating cell proliferation, migration and differentiation in angiogenesis or yet in tumor growth (PubMed:20123964, PubMed:21569306). Also plays a role in integrin-mediated cell-cell adhesion in angiogenesis (PubMed:12660161, PubMed:16099422).4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Magnesium-independent phospholipid phosphatase (PubMed:9705349). Insensitive to N-ethylmaleimide (PubMed:9705349). Inhibited by sphingosine, zinc ions and modestly by propanolol (PubMed:9705349).1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=100 µM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate1 Publication
  2. KM=110 µM for (9Z)-octadecenoyl-sn-glycero-3-phosphate1 Publication
  3. KM=56 µM for N-oleoyl ethanolamine phosphatidic acid1 Publication
  1. Vmax=0.27 nmol/min/mg enzyme with 1,2-dihexadecanoyl-sn-glycero-3-phosphate as substrate1 Publication
  2. Vmax=0.46 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate1 Publication
  3. Vmax=0.36 nmol/min/mg enzyme with N-(octanoyl)-sphing-4-enine-1-phosphate as substrate1 Publication
  4. Vmax=0.24 nmol/min/mg enzyme with sphing-4-enine 1-phosphate as substrate1 Publication
  5. Vmax=13 nmol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate as substrate1 Publication
  6. Vmax=15 nmol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate1 Publication
  7. Vmax=29 nmol/min/mg enzyme with N-(9Z-octadecenoyl)-ethanolamine phosphate as substrate1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: phospholipid metabolism

This protein is involved in the pathway phospholipid metabolism, which is part of Lipid metabolism.3 Publications
View all proteins of this organism that are known to be involved in the pathway phospholipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei199Proton donorsBy similarity1
Active sitei251NucleophileBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei255Stabilizes the active site histidine for nucleophilic attackBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1660661 Sphingolipid de novo biosynthesis

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		O14495

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00085

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001642

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Phospholipid phosphatase 3Curated (EC:3.1.3.-1 Publication, EC:3.1.3.42 Publications)
Alternative name(s):
Lipid phosphate phosphohydrolase 3
PAP2-beta
Phosphatidate phosphohydrolase type 2b
Phosphatidic acid phosphatase 2b
Short name:
PAP-2b
Short name:
PAP2b
Vascular endothelial growth factor and type I collagen-inducible protein1 Publication
Short name:
VCIP1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PLPP3Imported
Synonyms:LPP3, PPAP2B
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000162407.8

Human Gene Nomenclature Database

More...HGNCi		HGNC:9229 PLPP3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		607125 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O14495

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 33Cytoplasmic1 PublicationAdd BLAST33
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei34 – 54HelicalSequence analysisAdd BLAST21
Topological domaini55 – 85Extracellular1 PublicationAdd BLAST31
Transmembranei86 – 106HelicalSequence analysisAdd BLAST21
Topological domaini107 – 122Cytoplasmic1 PublicationAdd BLAST16
Transmembranei123 – 143HelicalSequence analysisAdd BLAST21
Topological domaini144 – 193Extracellular1 PublicationAdd BLAST50
Transmembranei194 – 214HelicalSequence analysisAdd BLAST21
Topological domaini215 – 225Cytoplasmic1 PublicationAdd BLAST11
Transmembranei226 – 243HelicalSequence analysisAdd BLAST18
Topological domaini244 – 257Extracellular1 PublicationAdd BLAST14
Transmembranei258 – 278HelicalSequence analysisAdd BLAST21
Topological domaini279 – 311Cytoplasmic1 PublicationAdd BLAST33

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi106Y → A: No effect on basolateral localization in polarized cells. 1 Publication1
Mutagenesisi109Y → A: Loss of basolateral localization in polarized cells. 1 Publication1
Mutagenesisi110Y → A: Loss of basolateral localization in polarized cells. 1 Publication1
Mutagenesisi184D → E: Loss of binding to integrin. Loss of function in integrin-mediated cell-cell interaction. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		8613

Open Targets

More...OpenTargetsi		ENSG00000162407

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33553

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		O14495 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PLPP3

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002209121 – 311Phospholipid phosphatase 3Add BLAST311

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi170N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated (PubMed:9705349). Contains high-mannose oligosaccharides (PubMed:9705349).1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O14495

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O14495

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		O14495

MaxQB - The MaxQuant DataBase

More...MaxQBi		O14495

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		O14495

PeptideAtlas

More...PeptideAtlasi		O14495

PRoteomics IDEntifications database

More...PRIDEi		O14495

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		48039

PTM databases

DEPOD human dephosphorylation database

More...DEPODi		O14495

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O14495

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		O14495

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed (PubMed:9305923, PubMed:12660161). Highly expressed in heart and placenta (PubMed:9305923).2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By EGF, VEGF, FGF2 and phorbol myristate acetate (PMA).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000162407 Expressed in metanephric glomerulus and 238 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O14495 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000162407 Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms functional homodimers and homooligomers that are not required for substrate recognition and catalytic activity (PubMed:14725715). Can also form heterooligomers with other PLPP2 and PLPP3 (PubMed:18215144).

Interacts with CTNND1; negatively regulates the PLPP3-mediated stabilization of beta-catenin/CTNNB1 (PubMed:20123964).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		114171, 12 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O14495

Protein interaction database and analysis system

More...IntActi		O14495, 4 interactors

Molecular INTeraction database

More...MINTi		O14495

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000360296

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O14495 protein

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni148 – 156Phosphatase sequence motif IBy similarity9
Regioni196 – 199Phosphatase sequence motif IIBy similarity4
Regioni244 – 255Phosphatase sequence motif IIIBy similarityAdd BLAST12
Regioni275 – 311Mediates interaction with CTNND11 PublicationAdd BLAST37

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi109 – 110Dityrosine basolateral targeting motif1 Publication2
Motifi182 – 184Integrin-binding motif2 Publications3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The integrin-binding motif mediates the binding to integrin alpha-5/beta-1 (ITGA5:ITGB1) and integrin alpha-V/beta-3 (ITGAV:ITGB3) and is required for the function in integrin-mediated cell-cell adhesion.2 Publications
The dityrosine basolateral targeting motif mediates localization to the basolateral membrane in polarized cells.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the PA-phosphatase related phosphoesterase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3030 Eukaryota
COG0671 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156450

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_021458_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O14495

KEGG Orthology (KO)

More...KOi		K01080

Identification of Orthologs from Complete Genome Data

More...OMAi		FIMIAWY

Database of Orthologous Groups

More...OrthoDBi		1621899at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O14495

TreeFam database of animal gene trees

More...TreeFami		TF316040

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028675 LPP3
IPR036938 P_Acid_Pase_2/haloperoxi_sf
IPR000326 P_Acid_Pase_2/haloperoxidase
IPR043216 PLPP

The PANTHER Classification System

More...PANTHERi		PTHR10165 PTHR10165, 1 hit
PTHR10165:SF79 PTHR10165:SF79, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01569 PAP2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00014 acidPPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48317 SSF48317, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

O14495-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQNYKYDKAI VPESKNGGSP ALNNNPRRSG SKRVLLICLD LFCLFMAGLP 
        60         70         80         90        100
FLIIETSTIK PYHRGFYCND ESIKYPLKTG ETINDAVLCA VGIVIAILAI 
       110        120        130        140        150
ITGEFYRIYY LKKSRSTIQN PYVAALYKQV GCFLFGCAIS QSFTDIAKVS 
       160        170        180        190        200
IGRLRPHFLS VCNPDFSQIN CSEGYIQNYR CRGDDSKVQE ARKSFFSGHA 
       210        220        230        240        250
SFSMYTMLYL VLYLQARFTW RGARLLRPLL QFTLIMMAFY TGLSRVSDHK 
       260        270        280        290        300
HHPSDVLAGF AQGALVACCI VFFVSDLFKT KTTLSLPAPA IRKEILSPVD 
       310 
IIDRNNHHNM M
Length:311
Mass (Da):35,116
Last modified:January 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCB3F60189044DA31
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB50222 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti32K → M in AAV38396 (Ref. 7) Curated1
Sequence conflicti282T → M in AAH09196 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AB000889 mRNA Translation: BAA22594.1
AF017786 mRNA Translation: AAC63433.1
AF480883 mRNA Translation: AAO84481.1
AF043329 mRNA Translation: AAD02271.1
U79294 mRNA Translation: AAB50222.1 Frameshift.
AK312439 mRNA Translation: BAG35348.1
BT019589 mRNA Translation: AAV38396.1
CH471059 Genomic DNA Translation: EAX06651.1
CH471059 Genomic DNA Translation: EAX06652.1
CH471059 Genomic DNA Translation: EAX06653.1
BC009196 mRNA Translation: AAH09196.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS604.1

NCBI Reference Sequences

More...RefSeqi		NP_003704.3, NM_003713.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000371250; ENSP00000360296; ENSG00000162407

Database of genes from NCBI RefSeq genomes

More...GeneIDi		8613

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:8613

UCSC genome browser

More...UCSCi		uc001cyj.3 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB000889 mRNA Translation: BAA22594.1
AF017786 mRNA Translation: AAC63433.1
AF480883 mRNA Translation: AAO84481.1
AF043329 mRNA Translation: AAD02271.1
U79294 mRNA Translation: AAB50222.1 Frameshift.
AK312439 mRNA Translation: BAG35348.1
BT019589 mRNA Translation: AAV38396.1
CH471059 Genomic DNA Translation: EAX06651.1
CH471059 Genomic DNA Translation: EAX06652.1
CH471059 Genomic DNA Translation: EAX06653.1
BC009196 mRNA Translation: AAH09196.1
CCDSiCCDS604.1
RefSeqiNP_003704.3, NM_003713.4

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi114171, 12 interactors
CORUMiO14495
IntActiO14495, 4 interactors
MINTiO14495
STRINGi9606.ENSP00000360296

Chemistry databases

SwissLipidsiSLP:000001642

PTM databases

DEPODiO14495
iPTMnetiO14495
PhosphoSitePlusiO14495

Polymorphism and mutation databases

BioMutaiPLPP3

Proteomic databases

EPDiO14495
jPOSTiO14495
MassIVEiO14495
MaxQBiO14495
PaxDbiO14495
PeptideAtlasiO14495
PRIDEiO14495
ProteomicsDBi48039

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		33239 126 antibodies

The DNASU plasmid repository

More...DNASUi		8613

Genome annotation databases

EnsembliENST00000371250; ENSP00000360296; ENSG00000162407
GeneIDi8613
KEGGihsa:8613
UCSCiuc001cyj.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8613
DisGeNETi8613
EuPathDBiHostDB:ENSG00000162407.8

GeneCards: human genes, protein and diseases

More...GeneCardsi		PLPP3
HGNCiHGNC:9229 PLPP3
HPAiENSG00000162407 Low tissue specificity
MIMi607125 gene
neXtProtiNX_O14495
OpenTargetsiENSG00000162407
PharmGKBiPA33553

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3030 Eukaryota
COG0671 LUCA
GeneTreeiENSGT00940000156450
HOGENOMiCLU_021458_3_0_1
InParanoidiO14495
KOiK01080
OMAiFIMIAWY
OrthoDBi1621899at2759
PhylomeDBiO14495
TreeFamiTF316040

Enzyme and pathway databases

UniPathwayiUPA00085
ReactomeiR-HSA-1660661 Sphingolipid de novo biosynthesis
SignaLinkiO14495

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		8613 0 hits in 786 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PLPP3 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PPAP2B

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		8613
PharosiO14495 Tbio

Protein Ontology

More...PROi		PR:O14495
RNActiO14495 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000162407 Expressed in metanephric glomerulus and 238 other tissues
GenevisibleiO14495 HS

Family and domain databases

InterProiView protein in InterPro
IPR028675 LPP3
IPR036938 P_Acid_Pase_2/haloperoxi_sf
IPR000326 P_Acid_Pase_2/haloperoxidase
IPR043216 PLPP
PANTHERiPTHR10165 PTHR10165, 1 hit
PTHR10165:SF79 PTHR10165:SF79, 1 hit
PfamiView protein in Pfam
PF01569 PAP2, 1 hit
SMARTiView protein in SMART
SM00014 acidPPc, 1 hit
SUPFAMiSSF48317 SSF48317, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPLPP3_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O14495
Secondary accession number(s): B2R651
, D3DQ52, Q5U0F7, Q96GW0, Q99782
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: June 17, 2020
This is version 171 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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