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Entry version 203 (29 Sep 2021)
Sequence version 4 (19 Sep 2002)
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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Gene

Enpp1

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

Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (PubMed:9662402, PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:22510396, PubMed:25260930).

PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed:9662402, PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:19419305, PubMed:22510396, PubMed:25260930, PubMed:25479107, PubMed:26910915, PubMed:30111653).

Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed:11027689, PubMed:1647027, PubMed:23027977, PubMed:8223581).

May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling (PubMed:1647027).

Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (PubMed:30111653).

Appears to modulate insulin sensitivity (By similarity).

Also involved in melanogenesis (By similarity).

Also able to hydrolyze 2'-3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed:25344812).

2'-3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2'-3'-cGAMP hydrolysis is therefore unclear (By similarity).

Not able to hydrolyze the 2'-3'-cGAMP linkage isomer 3'-3'-cGAMP (By similarity).

By similarity15 Publications

Caution

It is uncertain whether Met-1 or Met-35 is the initiator.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+3 PublicationsNote: Binds 2 Zn2+ ions per subunit.3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

At low concentrations of ATP, a phosphorylated intermediate is formed which inhibits further hydrolysis.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=46 µM for ATP1 Publication
  2. KM=4.3 mM for UTP1 Publication
  3. KM=4.2 mM for GTP1 Publication
  4. KM=1.2 mM for CTP1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi200Zinc 1; catalytic3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei238AMP-threonine intermediate1 Publication1
Metal bindingi238Zinc 1; catalytic2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei259Substrate2 Publications1
Binding sitei277Substrate2 Publications1
Binding sitei308Substrate1 Publication1
Binding sitei322Substrate2 Publications1
Metal bindingi358Zinc 2; catalytic3 Publications1
Metal bindingi362Zinc 2; via tele nitrogen; catalytic3 Publications1
Binding sitei362Substrate 2'-3'-cGAMP1 Publication1
Metal bindingi405Zinc 1; catalytic3 Publications1
Metal bindingi406Zinc 1; via tele nitrogen; catalytic3 Publications1
Binding sitei514Substrate 2'-3'-cGAMP1 Publication1
Metal bindingi517Zinc 2; via tele nitrogen; catalytic3 Publications1
Metal bindingi781Calcium2 Publications1
Metal bindingi783Calcium2 Publications1
Metal bindingi785Calcium2 Publications1
Metal bindingi787Calcium; via carbonyl oxygen2 Publications1
Metal bindingi789Calcium2 Publications1
<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>Sitei896Essential for catalytic activityBy 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 functionHydrolase
Biological processBiomineralization
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.4.1, 3474
3.6.1.9, 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-196843, Vitamin B2 (riboflavin) metabolism

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P06802

<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_and_taxonomy_section">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:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Short name:
E-NPP 1
Alternative name(s):
Lymphocyte antigen 41
Short name:
Ly-41
Phosphodiesterase I/nucleotide pyrophosphatase 1
Plasma-cell membrane glycoprotein PC-11 Publication
Cleaved into the following chain:
Including the following 2 domains:
Alkaline phosphodiesterase I (EC:3.1.4.14 Publications)
Nucleotide pyrophosphatase (EC:3.6.1.94 Publications)
Short name:
NPPase
Alternative name(s):
Nucleotide diphosphataseCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Enpp11 PublicationImported
Synonyms:Npps1 Publication, Pc11 Publication, Pdnp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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: Unplaced

Organism-specific databases

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

More...
MGIi
MGI:97370, Enpp1

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 – 58CytoplasmicSequence analysisAdd BLAST58
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei59 – 79Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini80 – 906ExtracellularSequence analysisAdd BLAST827

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Defects in Enpp1 are the cause of the tiptoe walking (ttw) phenotype. Ttw mice exhibit ossification of the spinal ligaments (PubMed:9662402). Mice display increased bone formation process in joints and develop spontaneous osteoarthritis-like changes (PubMed:22510396).2 Publications
Defects in Enpp1 are the cause of spontaneous asj-2J mutant characterized by gait due to stiffening of the joints (PubMed:25479107). Defects are caused by a significant reduction in the plasma diphosphate (PPi) concentration, leading to extensive aberrant mineralization affecting the arterial vasculature, a number of internal organs and the dermal sheath of vibrissae (PubMed:25479107). Asj-2J mice are used as a model for arterial calcification of infancy disorder (GACI1) (PubMed:25479107). Mice also show ectopic mineralization of cartilage and collagen-rich tendons and ligaments (PubMed:26910915).2 Publications

<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

Mice show ectopic calcification of articular cartilage, the joint capsule and certain tendons (PubMed:25260930). Mice also display calcification of the joints and vertebrae as well as soft tissues including the whisker follicles, ear pinna and trachea (PubMed:25260930). This calcification worsened as the animals aged (PubMed:25260930). Bone mineralization in mice lacking both Enpp1 and Alpl is essentially normal, demonstrating that Enpp1 and Alpl are antagonist key regulators of bone mineralization by determining the normal steady-state levels of diphosphate (PPi) (PubMed:12082181).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi28A → G: No effect on basolateral sorting in epithelial cells. 1 Publication1
Mutagenesisi30S → A or D: Little change in baolateral sorting in epithelial cells. 1 Publication1
Mutagenesisi31L → A: 60% of ENPP1 redirected to apical surface in epithelial cells. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-32. 2 Publications1
Mutagenesisi32L → A: 70% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles. 75% of ENPP1 redirected to apical surface in epithelial cells; abrogation of increased NPP activity in oestoblastic matrix vesicles; when associated with A-31. 2 Publications1
Mutagenesisi42L → A: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication1
Mutagenesisi57Y → G: No change in increased NPP activity in oestoblastic matrix vesicles. 1 Publication1
Mutagenesisi200D → N: Decreases phosphodiesterase activity by 95%. Abolishes formation of nucleotidylated intermediate. 1 Publication1
Mutagenesisi237K → A: Decreases phosphodiesterase activity by 40%. Decreased formation of nucleotidylated intermediate. 1 Publication1
Mutagenesisi238T → A: Abolishes all phosphodiesterase activity. Abolishes formation of nucleotidylated intermediate. 2 Publications1
Mutagenesisi238T → S: Decreases phosphodiesterase activity by 95%. Accumulates nucleotidylated intermediate. 1 Publication1
Mutagenesisi239F → A: Decreases phosphodiesterase activity by 50%. Decreased formation of nucleotidylated intermediate. 2 Publications1
Mutagenesisi242H → L: Strongly decreased phosphodiesterase activity. 1 Publication1
Mutagenesisi304 – 323Missing : Nearly abolishes activity with nucleotide phosphates. Confers very low activity with lysophospholipids. 1 PublicationAdd BLAST20
Mutagenesisi308D → A: Decreased phosphodiesterase activity. 1 Publication1
Mutagenesisi322Y → A: Strongly decreased phosphodiesterase activity. 1 Publication1
Mutagenesisi358D → Q: Decreases phosphodiesterase activity by 90%. Accumulates nucleotidylated intermediate. 1 Publication1
Mutagenesisi362H → Q: Decreases phosphodiesterase activity by 95%. 65% activity can be restored by addition of Zn(2+) ions. Accumulates nucleotidylated intermediate. 1 Publication1
Mutagenesisi397C → S: Mice display a low bone mass density and show a striking joint disease and calcification of blood vessels. Probably affects protein stability. 1 Publication1
Mutagenesisi405D → N: Abolishes all phosphodiesterase activity. 10% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication1
Mutagenesisi406H → Q: Abolishes all phosphodiesterase activity. 15% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication1
Mutagenesisi514S → L: Abolished ability to hydrolyze 2'-3'-cGAMP without affecting ability to hydrolyze ATP. 1 Publication1
Mutagenesisi517H → Q: Abolishes all phosphodiesterase activity. 60% activity can be restored by addition of Zn(2+) ions. Abolishes formation of nucleotidylated intermediate. 1 Publication1

Keywords - Diseasei

Disease variant

<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_00001885651 – 906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1Add BLAST906
ChainiPRO_000044713485 – 906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form1 PublicationAdd BLAST822

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 residuei25PhosphoserineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi90 ↔ 104PROSITE-ProRule annotation
Disulfide bondi94 ↔ 122PROSITE-ProRule annotation
Disulfide bondi102 ↔ 115PROSITE-ProRule annotation
Disulfide bondi108 ↔ 114PROSITE-ProRule annotation
Disulfide bondi131 ↔ 148PROSITE-ProRule annotation
Disulfide bondi136 ↔ 166PROSITE-ProRule annotation
Disulfide bondi146 ↔ 159PROSITE-ProRule annotation
Disulfide bondi152 ↔ 158PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi161N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi177 ↔ 2232 Publications
Disulfide bondi185 ↔ 3972 Publications
Modified residuei238PhosphothreonineBy similarity1
Glycosylationi267N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi323N-linked (GlcNAc...) asparagine3 Publications1
Disulfide bondi413 ↔ 5122 Publications
Glycosylationi459N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi462 ↔ 8492 Publications
Glycosylationi567N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi596 ↔ 6532 Publications
Disulfide bondi607 ↔ 7072 Publications
Disulfide bondi609 ↔ 6922 Publications
Glycosylationi624N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi819 ↔ 8292 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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.5 Publications
The secreted form is produced through cleavage at Lys-85 by intracellular processing.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84 – 85Cleavage1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-4032

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P06802

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P06802

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

More...
PaxDbi
P06802

PRoteomics IDEntifications database

More...
PRIDEi
P06802

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
275869 [P06802-1]
275870 [P06802-2]

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2414, 1 N-Linked glycan (1 site) [P06802-2]

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P06802, 6 sites, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P06802

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

More...
PhosphoSitePlusi
P06802

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P06802

<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

Selectively expressed on the surface of antibody-secreting cells (PubMed:3104326). Expressed in osteocytes and osteoclasts (PubMed:25260930).2 Publications

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1: Homodimer (PubMed:23027977, PubMed:23041369). Ectonucleotide pyrophosphatase/phosphodiesterase family member 1:

Interacts with INSR; leading to inhibit INSR autophosphorylation and subsequent activation of INSR kinase activity (By similarity). Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form: Monomeric (PubMed:23041369).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

P06802
With#Exp.IntAct
itself2EBI-16016057,EBI-16016057

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
202097, 4 interactors

Database of interacting proteins

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DIPi
DIP-59981N

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000101159

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P06802, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1906
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P06802

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini86 – 126SMB 1PROSITE-ProRule annotationAdd BLAST41
Domaini127 – 171SMB 2PROSITE-ProRule annotationAdd BLAST45

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>Regioni1 – 22DisorderedSequence analysisAdd BLAST22
Regioni173 – 573Phosphodiesterase2 PublicationsAdd BLAST401
Regioni579 – 628Linker2 PublicationsAdd BLAST50
Regioni635 – 906Nuclease2 PublicationsAdd BLAST272

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>Motifi27 – 34Di-leucine motif2 Publications8

<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 di-leucine motif is required for basolateral targeting in polarized epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells.2 Publications

<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

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2645, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P06802

Database of Orthologous Groups

More...
OrthoDBi
999163at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P06802

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.720.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR017850, Alkaline_phosphatase_core_sf
IPR001604, DNA/RNA_non-sp_Endonuclease
IPR029890, ENPP1
IPR020821, Extracellular_endonuc_su_A
IPR002591, Phosphodiest/P_Trfase
IPR036024, Somatomedin_B-like_dom_sf
IPR020436, Somatomedin_B_chordata
IPR001212, Somatomedin_B_dom

The PANTHER Classification System

More...
PANTHERi
PTHR10151:SF77, PTHR10151:SF77, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01223, Endonuclease_NS, 1 hit
PF01663, Phosphodiest, 1 hit
PF01033, Somatomedin_B, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00022, SOMATOMEDINB

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00892, Endonuclease_NS, 1 hit
SM00477, NUC, 1 hit
SM00201, SO, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53649, SSF53649, 1 hit
SSF90188, SSF90188, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00524, SMB_1, 2 hits
PS50958, SMB_2, 2 hits

<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_length">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>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 2 (identifier: P06802-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MERDGDQAGH GPRHGSAGNG RELESPAAAS LLAPMDLGEE PLEKAERARP
60 70 80 90 100
AKDPNTYKVL SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS
110 120 130 140 150
NCRCDAACVS LGNCCLDFQE TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD
160 170 180 190 200
DCKTHNDCCI NYSSVCQDKK SWVEETCESI DTPECPAEFE SPPTLLFSLD
210 220 230 240 250
GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPMYPTKTFP NHYSIVTGLY
260 270 280 290 300
PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVKSG
310 320 330 340 350
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSHERPHFY
360 370 380 390 400
TLYLEEPDSS GHSHGPVSSE VIKALQKVDR LVGMLMDGLK DLGLDKCLNL
410 420 430 440 450
ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTDVPETYYS
460 470 480 490 500
FNYEALAKNL SCREPNQHFR PYLKPFLPKR LHFAKSDRIE PLTFYLDPQW
510 520 530 540 550
QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE
560 570 580 590 600
VYNLMCDLLG LIPAPNNGSH GSLNHLLKKP IYNPSHPKEE GFLSQCPIKS
610 620 630 640 650
TSNDLGCTCD PWIVPIKDFE KQLNLTTEDV DDIYHMTVPY GRPRILLKQH
660 670 680 690 700
HVCLLQQQQF LTGYSLDLLM PLWASYTFLR NDQFSRDDFS NCLYQDLRIP
710 720 730 740 750
LSPVHKCSYY KSNSKLSYGF LTPPRLNRVS NHIYSEALLT SNIVPMYQSF
760 770 780 790 800
QVIWHYLHDT LLQRYAHERN GINVVSGPVF DFDYDGRYDS LEILKQNSRV
810 820 830 840 850
IRSQEILIPT HFFIVLTSCK QLSETPLECS ALESSAYILP HRPDNIESCT
860 870 880 890 900
HGKRESSWVE ELLTLHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP

IFSQED
Length:906
Mass (Da):103,176
Last modified:September 19, 2002 - v4
<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:i068D45B0ED0F224D
GO
Isoform 1 (identifier: P06802-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     630-630: Missing.

Show »
Length:905
Mass (Da):103,076
Checksum:iFB6EEEA0FF659421
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3X9S2G3X9S2_MOUSE
Ectonucleotide pyrophosphatase/phos...
Enpp1
905Annotation score:

Annotation score:3 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>
A0A0R4J1Q7A0A0R4J1Q7_MOUSE
Ectonucleotide pyrophosphatase/phos...
Enpp1
906Annotation score:

Annotation score:3 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>
E9QQ26E9QQ26_MOUSE
Ectonucleotide pyrophosphatase/phos...
Enpp1
369Annotation score:

Annotation score:2 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti568 – 906Missing in ttw. 1 PublicationAdd BLAST339
Natural varianti651H → R in allele ENPP1b. 1 Publication1
Natural varianti680R → S in allele ENPP1b. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006748630Missing in isoform 1. 2 Publications1

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
J02700 mRNA Translation: AAA39893.2
AF339910 mRNA Translation: AAK84174.1
AK088857 mRNA Translation: BAC40616.1
L04516 Unassigned DNA No translation available.
M12552 mRNA Translation: AAA39892.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS35870.1 [P06802-2]
CCDS78802.1 [P06802-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A27410

NCBI Reference Sequences

More...
RefSeqi
NP_001295256.1, NM_001308327.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
18605

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:18605

Keywords - Coding sequence diversityi

Alternative splicing

<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
J02700 mRNA Translation: AAA39893.2
AF339910 mRNA Translation: AAK84174.1
AK088857 mRNA Translation: BAC40616.1
L04516 Unassigned DNA No translation available.
M12552 mRNA Translation: AAA39892.1
CCDSiCCDS35870.1 [P06802-2]
CCDS78802.1 [P06802-1]
PIRiA27410
RefSeqiNP_001295256.1, NM_001308327.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B56X-ray3.00A/B87-906[»]
4GTWX-ray2.70A/B92-906[»]
4GTXX-ray3.20A/B92-906[»]
4GTYX-ray3.19A/B92-906[»]
4GTZX-ray3.19A/B92-906[»]
6AEKX-ray1.80A170-906[»]
6AELX-ray1.90A170-906[»]
SMRiP06802
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi202097, 4 interactors
DIPiDIP-59981N
STRINGi10090.ENSMUSP00000101159

PTM databases

GlyConnecti2414, 1 N-Linked glycan (1 site) [P06802-2]
GlyGeniP06802, 6 sites, 1 N-linked glycan (1 site)
iPTMnetiP06802
PhosphoSitePlusiP06802
SwissPalmiP06802

Proteomic databases

CPTACinon-CPTAC-4032
jPOSTiP06802
MaxQBiP06802
PaxDbiP06802
PRIDEiP06802
ProteomicsDBi275869 [P06802-1]
275870 [P06802-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
18605

Genome annotation databases

GeneIDi18605
KEGGimmu:18605

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5167
MGIiMGI:97370, Enpp1

Phylogenomic databases

eggNOGiKOG2645, Eukaryota
InParanoidiP06802
OrthoDBi999163at2759
PhylomeDBiP06802

Enzyme and pathway databases

BRENDAi3.1.4.1, 3474
3.6.1.9, 3474
ReactomeiR-MMU-196843, Vitamin B2 (riboflavin) metabolism
SABIO-RKiP06802

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
18605, 1 hit in 61 CRISPR screens

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

More...
ChiTaRSi
Enpp1, mouse

Protein Ontology

More...
PROi
PR:P06802
RNActiP06802, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Family and domain databases

Gene3Di3.40.720.10, 1 hit
InterProiView protein in InterPro
IPR017850, Alkaline_phosphatase_core_sf
IPR001604, DNA/RNA_non-sp_Endonuclease
IPR029890, ENPP1
IPR020821, Extracellular_endonuc_su_A
IPR002591, Phosphodiest/P_Trfase
IPR036024, Somatomedin_B-like_dom_sf
IPR020436, Somatomedin_B_chordata
IPR001212, Somatomedin_B_dom
PANTHERiPTHR10151:SF77, PTHR10151:SF77, 1 hit
PfamiView protein in Pfam
PF01223, Endonuclease_NS, 1 hit
PF01663, Phosphodiest, 1 hit
PF01033, Somatomedin_B, 2 hits
PRINTSiPR00022, SOMATOMEDINB
SMARTiView protein in SMART
SM00892, Endonuclease_NS, 1 hit
SM00477, NUC, 1 hit
SM00201, SO, 2 hits
SUPFAMiSSF53649, SSF53649, 1 hit
SSF90188, SSF90188, 2 hits
PROSITEiView protein in PROSITE
PS00524, SMB_1, 2 hits
PS50958, SMB_2, 2 hits

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 nameiENPP1_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: P06802
Secondary accession number(s): Q542E9, Q924C4
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: September 19, 2002
Last modified: September 29, 2021
This is version 203 of the entry and version 4 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

3D-structure, 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
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