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Entry version 146 (12 Aug 2020)
Sequence version 1 (01 Jun 2001)
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Protein

Phospholipid phosphatase 3

Gene

Plpp3

Organism
Mus musculus (Mouse)
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. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound. 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. 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 (By similarity). By maintaining the appropriate levels of this lipid in the cerebellum, also ensure its proper development and function (PubMed:21319224). 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 (By similarity).By similarity1 Publication
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:12925589, PubMed:27125875). Also plays a role in integrin-mediated cell-cell adhesion in angiogenesis (PubMed:16099422).3 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. Insensitive to N-ethylmaleimide.By similarity

<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.2 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 sitei200Proton donorsBy similarity1
Active sitei252NucleophileBy 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>Sitei256Stabilizes 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

GO - Biological processi

<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 functionDevelopmental protein, Hydrolase
Biological processLipid metabolism

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1660661, Sphingolipid de novo biosynthesis

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

More...
UniPathwayi
UPA00085

<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.-2 Publications, EC:3.1.3.41 Publication)
Alternative name(s):
Lipid phosphate phosphohydrolase 3
PAP2-beta
Phosphatidate phosphohydrolase type 2b
Phosphatidic acid phosphatase 2b
Short name:
PAP-2b
Short name:
PAP2b
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1915166, Plpp3

<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 – 123Cytoplasmic1 PublicationAdd BLAST17
Transmembranei124 – 144HelicalSequence analysisAdd BLAST21
Topological domaini145 – 194Extracellular1 PublicationAdd BLAST50
Transmembranei195 – 215HelicalSequence analysisAdd BLAST21
Topological domaini216 – 226Cytoplasmic1 PublicationAdd BLAST11
Transmembranei227 – 244HelicalSequence analysisAdd BLAST18
Topological domaini245 – 258Extracellular1 PublicationAdd BLAST14
Transmembranei259 – 279HelicalSequence analysisAdd BLAST21
Topological domaini280 – 312Cytoplasmic1 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

The homozygous knockout of Plpp3 is embryonic lethal (PubMed:12925589, PubMed:17610274, PubMed:19123136). It is characterized by a delay in development, absence of chorioallantoic fusion at the 6 somite stage, allantois compaction, impaired remodeling of the primary capillary plexus of the yolk sac and gastrulation defects with low penetrance. Persistence of open neural tube is also frequently observed (PubMed:12925589, PubMed:19123136). Conditional knockout of Plpp3 in the cerebellum is associated with defects in postnatal cerebellum development, modifications in the cytoarchitecture and arrangement of Bergmann glia with a mild non-progressive motor coordination defect (PubMed:21319224). Conditional knockout of Plpp3 in endothelial cells is associated with vascular leakage and hemorrhage that likely result in insufficient cardiovascular development and the observed embryonic lethality (PubMed:27125875). Conditional knockout of Plpp3 in adipocytes does not affect the development of the adipose tissue. However, mutant homozygous mice display lower accumulation of ceramide and sphingomyelin on high fat or Western diets compared to control animals (PubMed:29889835).6 Publications

<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_00002209131 – 312Phospholipid phosphatase 3Add BLAST312

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 residuei19PhosphoserineBy similarity1
<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>Glycosylationi171N-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. Contains high-mannose oligosaccharides.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q99JY8

MaxQB - The MaxQuant DataBase

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MaxQBi
Q99JY8

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

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PaxDbi
Q99JY8

PeptideAtlas

More...
PeptideAtlasi
Q99JY8

PRoteomics IDEntifications database

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PRIDEi
Q99JY8

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2585, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
Q99JY8, 1 site

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q99JY8

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

More...
PhosphoSitePlusi
Q99JY8

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q99JY8

<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

Detected in lung, cerebellum and heart atrium.2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Display a characteristic dynamic and changing pattern of expression throughout the life cycle of the mouse (PubMed:12925589). Expression during early stages of development is specific of structures where multiple inductive interactions occur such as the limb buds, mammary gland primordia, heart cushions and valves among others (PubMed:19123136). Detected in a few cells of the extra-embryonic ectoderm of E6.5 embryos. By E7.5, starts to be strongly expressed in the anterior visceral endoderm, as well as in the extra-embryonic membranes. By E8.0 expression extends to a highly localized region around the node and appears at the tip of the allantois. At E8.5 predominantly expressed in the allantois, the developing gut, the pericardio-peritoneal canal and somites. In E9.5 embryos persists in the umbilical cord, and is also found in the chorionic region. In later mid-gestation embryos, present at high levels in the apical ectodermal ridge and mesenchyme of the limb buds, in the peripheral nervous system, cranial nerves, and mammary gland primordia (PubMed:12925589).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000028517, Expressed in skin of back and 358 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q99JY8, MM

<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. Can also form heterooligomers with other PLPP2 and PLPP3.

Interacts with CTNND1; negatively regulates the PLPP3-mediated stabilization of beta-catenin/CTNNB1.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
212532, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q99JY8

Protein interaction database and analysis system

More...
IntActi
Q99JY8, 5 interactors

Molecular INTeraction database

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MINTi
Q99JY8

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000065719

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q99JY8, 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>Regioni149 – 157Phosphatase sequence motif IBy similarity9
Regioni197 – 200Phosphatase sequence motif IIBy similarity4
Regioni245 – 256Phosphatase sequence motif IIIBy similarityAdd BLAST12
Regioni276 – 312Mediates interaction with CTNND1By similarityAdd 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 motifBy similarity2
Motifi183 – 185Integrin-binding motif1 Publication3

<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.1 Publication
The dityrosine basolateral targeting motif mediates localization to the basolateral membrane in polarized cells.By similarity

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3030, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000156450

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_021458_3_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q99JY8

KEGG Orthology (KO)

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KOi
K01080

Identification of Orthologs from Complete Genome Data

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OMAi
FIMIAWY

Database of Orthologous Groups

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OrthoDBi
1621899at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q99JY8

TreeFam database of animal gene trees

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TreeFami
TF316040

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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

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PANTHERi
PTHR10165, PTHR10165, 1 hit
PTHR10165:SF79, PTHR10165:SF79, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01569, PAP2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00014, acidPPc, 1 hit

Superfamily database of structural and functional annotation

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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.

Q99JY8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP
60 70 80 90 100
FLIIETSTIK PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI
110 120 130 140 150
ITGEFYRIYY LKEKSRSTTQ NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV
160 170 180 190 200
SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY RCRGEDSKVQ EARKSFFSGH
210 220 230 240 250
ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF YTGLSRVSDY
260 270 280 290 300
KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV
310
DIIDRNNHHN MV
Length:312
Mass (Da):35,216
Last modified:June 1, 2001 - 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:iD782986E04B57D7D
GO

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 conflicti187S → C in BAE34848 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AK159136 mRNA Translation: BAE34848.1
AK160056 mRNA Translation: BAE35594.1
BC005558 mRNA Translation: AAH05558.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS18417.1

NCBI Reference Sequences

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RefSeqi
NP_542122.1, NM_080555.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517

Database of genes from NCBI RefSeq genomes

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GeneIDi
67916

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:67916

UCSC genome browser

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UCSCi
uc008tye.1, mouse

<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
AK159136 mRNA Translation: BAE34848.1
AK160056 mRNA Translation: BAE35594.1
BC005558 mRNA Translation: AAH05558.1
CCDSiCCDS18417.1
RefSeqiNP_542122.1, NM_080555.2

3D structure databases

Database of comparative protein structure models

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ModBasei
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SWISS-MODEL Interactive Workspace

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

Protein-protein interaction databases

BioGRIDi212532, 3 interactors
CORUMiQ99JY8
IntActiQ99JY8, 5 interactors
MINTiQ99JY8
STRINGi10090.ENSMUSP00000065719

PTM databases

GlyConnecti2585, 1 N-Linked glycan (1 site)
GlyGeniQ99JY8, 1 site
iPTMnetiQ99JY8
PhosphoSitePlusiQ99JY8
SwissPalmiQ99JY8

Proteomic databases

jPOSTiQ99JY8
MaxQBiQ99JY8
PaxDbiQ99JY8
PeptideAtlasiQ99JY8
PRIDEiQ99JY8

Genome annotation databases

EnsembliENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517
GeneIDi67916
KEGGimmu:67916
UCSCiuc008tye.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8613
MGIiMGI:1915166, Plpp3

Phylogenomic databases

eggNOGiKOG3030, Eukaryota
GeneTreeiENSGT00940000156450
HOGENOMiCLU_021458_3_0_1
InParanoidiQ99JY8
KOiK01080
OMAiFIMIAWY
OrthoDBi1621899at2759
PhylomeDBiQ99JY8
TreeFamiTF316040

Enzyme and pathway databases

UniPathwayiUPA00085
ReactomeiR-MMU-1660661, Sphingolipid de novo biosynthesis

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
67916, 0 hits in 18 CRISPR screens

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

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ChiTaRSi
Plpp3, mouse

Protein Ontology

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PROi
PR:Q99JY8
RNActiQ99JY8, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSMUSG00000028517, Expressed in skin of back and 358 other tissues
GenevisibleiQ99JY8, MM

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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_MOUSE
<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: Q99JY8
Secondary accession number(s): Q3TVM4, Q3TXR7, Q8BTB7
<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: June 1, 2001
Last modified: August 12, 2020
This is version 146 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

<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

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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