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Entry version 199 (02 Dec 2020)
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%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 '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%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

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%5Fsection">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%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 sitei238AMP-threonine intermediate1 Publication1
    Metal bindingi238Zinc 1; catalytic2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%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:
    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%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:Enpp11 PublicationImported
    Synonyms:Npps1 Publication, Pc11 Publication, Pdnp1
    <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: 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

    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 – 58CytoplasmicSequence analysisAdd BLAST58
    <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>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%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>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 mutation

    <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%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>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%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.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

    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

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    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%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

    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%5Fsection">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, 2 interactors

    Database of interacting proteins

    More...
    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

    More...
    SMRi
    P06802

    Database of comparative protein structure models

    More...
    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%5Fand%5Fdomains%5Fsection">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>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%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>Sequences (2+)i

    <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.

    <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 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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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
    A0A0R4J1Q7A0A0R4J1Q7_MOUSE
    Ectonucleotide pyrophosphatase/phos...
    Enpp1
    906Annotation score:

    Annotation score:4 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>
    G3X9S2G3X9S2_MOUSE
    Ectonucleotide pyrophosphatase/phos...
    Enpp1
    905Annotation 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>
    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, Polymorphism

    <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, 2 interactors
    DIPiDIP-59981N
    STRINGi10090.ENSMUSP00000101159

    PTM databases

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

    Proteomic databases

    CPTACinon-CPTAC-4032
    jPOSTiP06802
    MaxQBiP06802
    PaxDbiP06802
    PRIDEiP06802

    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 17 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

    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 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%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: January 1, 1988
    Last sequence update: September 19, 2002
    Last modified: December 2, 2020
    This is version 199 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
    UniProt is an ELIXIR core data resource
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