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UniProtKB - Q9R1E6 (ENPP2_MOUSE)

Entry version 180 (02 Dec 2020)
Sequence version 3 (10 Feb 2009)
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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

Enpp2

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

Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:17208043, PubMed:28414242, PubMed:27780639). Major substrate is lysophosphatidylcholine (PubMed:17208043, PubMed:27780639). Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:18175805). Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition (By similarity). Possible involvement in cell proliferation and adipose tissue development (Probable). Tumor cell motility-stimulating factor. Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (By similarity). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (By similarity).By similarity1 Publication5 Publications

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

<p>This subsection of the '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

Protein has several cofactor binding sites:

<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

Inhibited by EDTA and EGTA.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=12.9 mM for pNppp (isoform 1)1 Publication
  2. KM=4.4 mM for pNppp (isoform 2)1 Publication
  3. KM=11.8 mM for pNppp (isoform 3)1 Publication
  1. Vmax=1.9 nmol/min/µg enzyme with pNppp as substrate (isoform 1)1 Publication
  2. Vmax=0.35 nmol/min/µg enzyme with pNppp as substrate (isoform 2)1 Publication
  3. Vmax=1.8 nmol/min/µg enzyme with pNppp as substrate (isoform 3)1 Publication

pH dependencei

Optimum pH is 8.0 for isoforms 1, 2 and 3.1 Publication

Temperature dependencei

Isoforms 1 and 3 have maximum activity from 45 to 55 degrees Celsius.1 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 bindingi171Zinc 1; catalyticCombined sources2 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 sitei209Nucleophile1 Publication1
Metal bindingi209Zinc 1; catalyticCombined sources2 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 sitei230SubstrateCombined sources1 Publication1
Binding sitei306SubstrateCombined sources1 Publication1
Metal bindingi311Zinc 2; catalyticCombined sources2 Publications1
Metal bindingi315Zinc 2; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi358Zinc 1; catalyticCombined sources2 Publications1
Metal bindingi359Zinc 1; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi474Zinc 2; via tele nitrogen; catalyticCombined sources2 Publications1
Metal bindingi739CalciumCombined sources3 Publications1
Metal bindingi741CalciumCombined sources3 Publications1
Metal bindingi743CalciumCombined sources3 Publications1
Metal bindingi745Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi747CalciumCombined sources3 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>Sitei852Essential for catalytic activity1 Publication1

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionHydrolase
Biological processChemotaxis, Lipid degradation, Lipid metabolism
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.4.39, 3474

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9R1E6

<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 2 (EC:3.1.4.395 Publications)
Short name:
E-NPP 2
Alternative name(s):
Autotaxin1 Publication
Extracellular lysophospholipase D
Short name:
LysoPLD
<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:Enpp2
Synonyms:Npps2, Pdnp21 Publication
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 15

Organism-specific databases

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

More...MGIi		MGI:1321390, Enpp2

<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

Keywords - Cellular componenti

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

May contribute to obesity (PubMed:15700135).1 Publication

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>Mutagenesisi12 – 27Missing : Complete inhibition of secretion. 1 PublicationAdd BLAST16
Mutagenesisi12 – 22Missing : Complete inhibition of secretion. 1 PublicationAdd BLAST11
Mutagenesisi23 – 27Missing : No effect on secretion. 1 Publication5
Mutagenesisi23Missing : No effect on secretion. 1
Mutagenesisi25Missing : No effect on secretion. 1 Publication1
Mutagenesisi27 – 35Missing : No effect on secretion nor lysophospholipase activity. 1 Publication9
Mutagenesisi27 – 30Missing : No effect on secretion. 1 Publication4
Mutagenesisi27Missing : No effect on secretion. 1 Publication1
Mutagenesisi30 – 41Missing : No effect on secretion nor lysophospholipase activity. 1 PublicationAdd BLAST12
Mutagenesisi30 – 33Missing : No effect on secretion nor lysophospholipase activity. 1 Publication4
Mutagenesisi32 – 35Missing : No effect on secretion nor lysophospholipase activity. 1 Publication4
Mutagenesisi36 – 40Missing : No effect on secretion nor lysophospholipase activity. 1 Publication5
Mutagenesisi53Missing : No effect on secretion; slightly decreases lysophospholipase activity. Almost complete loss of lysophospholipase activity; when associated with N-410 del. 1 Publication1
Mutagenesisi210F → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi213L → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi230N → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi243L → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi247E → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi249F → A: Reduced lysophospholipase activity. 1 Publication1
Mutagenesisi410Missing : No effect on secretion; greatly inhibits lysoPLD activity. Inhibits secretion. Almost complete loss of lysoPLD activity; when associated with N-53 del. 1 Publication1
Mutagenesisi512M → A: Reduced lysophospholipase activity. 1
Mutagenesisi851 – 853LKT → AAA, RRR or SSS: No catalytic activity. 1 Publication3
Mutagenesisi851L → A: No effect. 1 Publication1
Mutagenesisi852K → A or R: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi853T → A: No effect. 1 Publication1

Keywords - Diseasei

Obesity

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3826871

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2901

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 27By similarityAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000028165028 – 35Removed by furinBy similarity8
<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_000018856836 – 862Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi53N-linked (GlcNAc...) asparagineCombined sources2 Publications1
<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 bondi58 ↔ 75Combined sources4 Publications
Disulfide bondi62 ↔ 93Combined sources4 Publications
Disulfide bondi73 ↔ 86Combined sources4 Publications
Disulfide bondi79 ↔ 85Combined sources4 Publications
Disulfide bondi102 ↔ 119Combined sources4 Publications
Disulfide bondi107 ↔ 137Combined sources4 Publications
Disulfide bondi117 ↔ 130Combined sources4 Publications
Disulfide bondi123 ↔ 129Combined sources4 Publications
Disulfide bondi148 ↔ 194Combined sources4 Publications
Disulfide bondi156 ↔ 350Combined sources3 Publications
Disulfide bondi366 ↔ 468Combined sources3 Publications
Glycosylationi410N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Disulfide bondi413 ↔ 805Combined sources4 Publications
Glycosylationi524N-linked (GlcNAc...) asparagineCombined sources3 Publications1
Disulfide bondi566 ↔ 666Combined sources4 Publications
Disulfide bondi568 ↔ 651Combined sources4 Publications
Disulfide bondi774 ↔ 784Combined sources4 Publications
Glycosylationi806N-linked (GlcNAc...) asparagineSequence analysis1

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

N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity. Secretion requires simultaneous glycosylation on Asn-53 and Asn-410, while probable glycosylation of Asn-410 has a preferential role on lysoPLD activity. Not O-glycosylated.3 Publications
The interdomain disulfide bond between Cys-413 and Cys-805 is essential for catalytic activity.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PeptideAtlas

More...PeptideAtlasi		Q9R1E6

PRoteomics IDEntifications database

More...PRIDEi		Q9R1E6

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		2275, 5 N-Linked glycans (2 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q9R1E6, 4 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9R1E6

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

More...PhosphoSitePlusi		Q9R1E6

<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

Expressed in brain and adipose tissue.1 Publication

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

Up-regulated in adipocytes of obese-diabetic db/db mice.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000022425, Expressed in choroid plexus epithelium and 417 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9R1E6, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9R1E6, MM

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

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000132640

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9R1E6

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9R1E6, 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

1862
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		Q9R1E6

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9R1E6

<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>Domaini54 – 97SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini98 – 142SMB 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>Regioni144 – 501PhosphodiesteraseAdd BLAST358
Regioni210 – 213Substrate bindingCombined sources1 Publication4
Regioni243 – 254Substrate binding1 PublicationAdd BLAST12
Regioni597 – 862NucleaseAdd BLAST266
Regioni829 – 850Required for secretionAdd BLAST22

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>Motifi126 – 128Cell attachment siteSequence analysis3

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

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2645, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155778

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_012256_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9R1E6

Identification of Orthologs from Complete Genome Data

More...OMAi		CHDFDEH

Database of Orthologous Groups

More...OrthoDBi		999163at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9R1E6

TreeFam database of animal gene trees

More...TreeFami		TF330032

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
IPR029881, ENPP2
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:SF21, PTHR10151:SF21, 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 (3+)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 3 <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 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9R1E6-1) [UniParc]FASTAAdd to basket
Also known as: Beta

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
MARQGCFGSY QVISLFTFAI GVNLCLGFTA SRIKRAEWDE GPPTVLSDSP 
        60         70         80         90        100
WTNTSGSCKG RCFELQEVGP PDCRCDNLCK SYSSCCHDFD ELCLKTARGW 
       110        120        130        140        150
ECTKDRCGEV RNEENACHCS EDCLSRGDCC TNYQVVCKGE SHWVDDDCEE 
       160        170        180        190        200
IRVPECPAGF VRPPLIIFSV DGFRASYMKK GSKVMPNIEK LRSCGTHAPY 
       210        220        230        240        250
MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAT FHLRGREKFN 
       260        270        280        290        300
HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP 
       310        320        330        340        350
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLKLHRC 
       360        370        380        390        400
VNVIFVGDHG MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRPKIPNNL 
       410        420        430        440        450
KYDPKAIIAN LTCKKPDQHF KPYMKQHLPK RLHYANNRRI EDLHLLVERR 
       460        470        480        490        500
WHVARKPLDV YKKPSGKCFF QGDHGFDNKV NSMQTVFVGY GPTFKYRTKV 
       510        520        530        540        550
PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR PTLPEEVSRP 
       560        570        580        590        600
NYPGIMYLQS DFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEERHLLYGR 
       610        620        630        640        650
PAVLYRTSYD ILYHTDFESG YSEIFLMPLW TSYTISKQAE VSSIPEHLTN 
       660        670        680        690        700
CVRPDVRVSP GFSQNCLAYK NDKQMSYGFL FPPYLSSSPE AKYDAFLVTN 
       710        720        730        740        750
MVPMYPAFKR VWTYFQRVLV KKYASERNGV NVISGPIFDY NYNGLRDIED 
       760        770        780        790        800
EIKQYVEGSS IPVPTHYYSI ITSCLDFTQP ADKCDGPLSV SSFILPHRPD 
       810        820        830        840        850
NDESCNSSED ESKWVEELMK MHTARVRDIE HLTGLDFYRK TSRSYSEILT 
       860 
LKTYLHTYES EI
Length:862
Mass (Da):98,885
Last modified:February 10, 2009 - v3
<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:i343D44DEAA8FA352
GO
Isoform 2 (identifier: Q9R1E6-2) [UniParc]FASTAAdd to basket
Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     323-323: E → EESSYGSPLTPAKRPKRKVAPKRRQERPVAPPKKRRRKLHRMDHYTAETRQDK

Show »
Length:914
Mass (Da):105,089
Checksum:iE36A577AB858AF02
GO
Isoform 3 (identifier: Q9R1E6-3) [UniParc]FASTAAdd to basket
Also known as: Gamma

The sequence of this isoform differs from the canonical sequence as follows:
     592-592: E → EAETGKFRGSKHENKKSLNGNVEPRK

Show »
Length:887
Mass (Da):101,680
Checksum:i599952429BBFBD6B
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
G3UXY9G3UXY9_MOUSE
Ectonucleotide pyrophosphatase/phos...
Enpp2
910Annotation 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>
A0A2I3BR60A0A2I3BR60_MOUSE
Ectonucleotide pyrophosphatase/phos...
Enpp2
62Annotation score:

Annotation score:1 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>
A0A2I3BS26A0A2I3BS26_MOUSE
Ectonucleotide pyrophosphatase/phos...
Enpp2
118Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti103T → I in ACD12866 (Ref. 3) Curated1
Sequence conflicti517G → S in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti550P → T in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti573E → K in AAD46480 (PubMed:10702660).Curated1
Sequence conflicti743N → D in ACD12866 (Ref. 3) Curated1
Sequence conflicti743N → D in AAH03264 (PubMed:15489334).Curated1

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_036396323E → EESSYGSPLTPAKRPKRKVA PKRRQERPVAPPKKRRRKLH RMDHYTAETRQDK in isoform 2. 1 Publication1
Alternative sequenceiVSP_036397