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Entry version 151 (18 Sep 2019)
Sequence version 2 (20 Mar 2007)
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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 2

Gene

Enpp2

Organism
Rattus norvegicus (Rat)
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:12633853, PubMed:29259743, PubMed:27660691, PubMed:27268273, PubMed:27075612). Major substrate is lysophosphatidylcholine (PubMed:12119361, PubMed:27660691, PubMed:27268273, PubMed:27075612). Also can act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility (PubMed:12119361). Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:12633853, PubMed:27268273). 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. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor (By similarity).By similarity7 Publications

<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

Protein has several cofactor binding sites:

<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

Inhibited by vanadate (PubMed:27268273). Inhibited by micromolar levels of bile salts, such as tauroursodeoxycholate. Not inhibited by taurodeoxycholate. Not inhibited by hydroxysterols, such as 7-hydroxycholesterol, testosterone, dexamethasone and prednisolone (PubMed:27075612).2 Publications

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 bindingi171Zinc 1; catalyticCombined sources4 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 sitei209Nucleophile2 Publications1
Metal bindingi209Zinc 1; catalyticCombined sources4 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 sitei230SubstrateCombined sources1 Publication1
Binding sitei306SubstrateCombined sources1 Publication1
Metal bindingi311Zinc 2; catalyticCombined sources4 Publications1
Metal bindingi315Zinc 2; via tele nitrogen; catalyticCombined sources4 Publications1
Metal bindingi358Zinc 1; catalyticCombined sources4 Publications1
Metal bindingi359Zinc 1; via tele nitrogen; catalyticCombined sources4 Publications1
Metal bindingi474Zinc 2; via tele nitrogen; catalyticCombined sources4 Publications1
Metal bindingi764CalciumCombined sources3 Publications1
Metal bindingi766CalciumCombined sources3 Publications1
Metal bindingi768CalciumCombined sources3 Publications1
Metal bindingi770Calcium; via carbonyl oxygenCombined sources3 Publications1
Metal bindingi772CalciumCombined 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>Sitei877Essential 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 processChemotaxis, Lipid degradation, Lipid metabolism
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.4.39 5301

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q64610

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000394

<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 2 (EC:3.1.4.397 Publications)
Short name:
E-NPP 2
Alternative name(s):
Autotaxin1 Publication
Extracellular lysophospholipase D
Short name:
LysoPLD1 Publication
<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:Enpp2
Synonyms:Atx, Npps2
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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

Rat genome database

More...
RGDi
69298 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

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>Mutagenesisi13I → L: No effect on secretion. 1 Publication1
Mutagenesisi16 – 18FTF → VLS: No effect on secretion. 1 Publication3
Mutagenesisi18 – 21FAIS → SVCV: No effect on secretion. 1 Publication4
Mutagenesisi21 – 24SVNI → VLTT: No effect on secretion. 1 Publication4
Mutagenesisi24 – 25IC → TI: No effect on secretion. 1 Publication2
Mutagenesisi28 – 30FTA → CIF: No effect on secretion. 1 Publication3
Mutagenesisi171D → N: Abolishes lysophospholipase D activity. 1 Publication1
Mutagenesisi209T → A: Abolishes lysophospholipase D activity. 1 Publication1
Mutagenesisi209T → S: 15% of wild-type lysophospholipase D activity. 1 Publication1
Mutagenesisi311D → N: Abolishes lysophospholipase D activity. 1 Publication1
Mutagenesisi315H → Q: 20% of wild-type lysophospholipase D activity. 1 Publication1
Mutagenesisi430K → A: Impaired secretion. No effect on lysophospholipase activity. 1 Publication1
Mutagenesisi764 – 768DYNYD → SYAYS: Abolishes secretion. Strongly reduced lysophospholipase activity. 1 Publication5

Keywords - Diseasei

Obesity

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3826870

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 – 272 PublicationsAdd BLAST27
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_000028165128 – 35Removed by furin2 Publications8
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000018856936 – 887Ectonucleotide pyrophosphatase/phosphodiesterase family member 2Add BLAST852

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
<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 ↔ 75PROSITE-ProRule annotation1 Publication
Disulfide bondi62 ↔ 93PROSITE-ProRule annotation1 Publication
Disulfide bondi73 ↔ 86PROSITE-ProRule annotation1 Publication
Disulfide bondi79 ↔ 85PROSITE-ProRule annotation1 Publication
Disulfide bondi102 ↔ 119PROSITE-ProRule annotation1 Publication
Disulfide bondi107 ↔ 137PROSITE-ProRule annotation1 Publication
Disulfide bondi117 ↔ 130PROSITE-ProRule annotation1 Publication
Disulfide bondi123 ↔ 129PROSITE-ProRule annotation1 Publication
Disulfide bondi148 ↔ 194PROSITE-ProRule annotation1 Publication
Disulfide bondi156 ↔ 350PROSITE-ProRule annotation1 Publication
Disulfide bondi366 ↔ 468PROSITE-ProRule annotation1 Publication
Glycosylationi398N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi410N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi413 ↔ 830PROSITE-ProRule annotation1 Publication
Glycosylationi524N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi566 ↔ 691PROSITE-ProRule annotation1 Publication
Disulfide bondi568 ↔ 676PROSITE-ProRule annotation1 Publication
Glycosylationi610N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi799 ↔ 809PROSITE-ProRule annotation1 Publication
Glycosylationi831N-linked (GlcNAc...) asparagineSequence analysis1

<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-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q64610

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q64610

<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

Abundantly expressed in cerebrum and cerebellum. Localized in secretory epithelial cells in the brain and the eye including choroid plexus epithelial cells, ciliary epithelial cells, iris pigment epithelial cells, and retinal pigment cells.2 Publications

<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

1887
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
Q64610

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
Q64610

<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>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>Regioni210 – 213Substrate bindingBy similarity4
Regioni243 – 254Substrate bindingBy similarityAdd BLAST12
Regioni854 – 875Required for secretionBy similarityAdd 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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000037439

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q64610

KEGG Orthology (KO)

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KOi
K01122

Database of Orthologous Groups

More...
OrthoDBi
999163at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q64610

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

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PANTHERi
PTHR10151:SF21 PTHR10151:SF21, 1 hit

Pfam protein domain database

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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 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q64610-1) [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
MARQGCLGSF QVISLFTFAI SVNICLGFTA 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
IKVPECPAGF VRPPLIIFSV DGFRASYMKK GSKVMPNIEK LRSCGTHAPY
210 220 230 240 250
MRPVYPTKTF PNLYTLATGL YPESHGIVGN SMYDPVFDAS FHLRGREKFN
260 270 280 290 300
HRWWGGQPLW ITATKQGVRA GTFFWSVSIP HERRILTILQ WLSLPDNERP
310 320 330 340 350
SVYAFYSEQP DFSGHKYGPF GPEMTNPLRE IDKTVGQLMD GLKQLRLHRC
360 370 380 390 400
VNVIFVGDHG MEDVTCDRTE FLSNYLTNVD DITLVPGTLG RIRAKSINNS
410 420 430 440 450
KYDPKTIIAN LTCKKPDQHF KPYMKQHLPK RLHYANNRRI EDIHLLVDRR
460 470 480 490 500
WHVARKPLDV YKKPSGKCFF QGDHGFDNKV NSMQTVFVGY GPTFKYRTKV
510 520 530 540 550
PPFENIELYN VMCDLLGLKP APNNGTHGSL NHLLRTNTFR PTMPDEVSRP
560 570 580 590 600
NYPGIMYLQS EFDLGCTCDD KVEPKNKLEE LNKRLHTKGS TEAETGKFRG
610 620 630 640 650
SKHENKKNLN GSVEPRKERH LLYGRPAVLY RTSYDILYHT DFESGYSEIF
660 670 680 690 700
LMPLWTSYTI SKQAEVSSIP EHLTNCVRPD VRVSPGFSQN CLAYKNDKQM
710 720 730 740 750
SYGFLFPPYL SSSPEAKYDA FLVTNMVPMY PAFKRVWAYF QRVLVKKYAS
760 770 780 790 800
ERNGVNVISG PIFDYNYDGL RDTEDEIKQY VEGSSIPVPT HYYSIITSCL
810 820 830 840 850
DFTQPADKCD GPLSVSSFIL PHRPDNDESC NSSEDESKWV EELMKMHTAR
860 870 880
VRDIEHLTGL DFYRKTSRSY SEILTLKTYL HTYESEI
Length:887
Mass (Da):101,576
Last modified:March 20, 2007 - v2
<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:i40AD1C957F833869
GO
Isoform 2 (identifier: Q64610-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     591-615: Missing.

Note: No experimental confirmation available.
Show »
Length:862
Mass (Da):98,836
Checksum:i2A530389DBA57952
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LSF4F1LSF4_RAT
Ectonucleotide pyrophosphatase/phos...
Enpp2
883Annotation 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>
D3ZES5D3ZES5_RAT
Ectonucleotide pyrophosphatase/phos...
Enpp2
858Annotation 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>

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 conflicti97A → V in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti107C → S in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti120S → P in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti147 – 162DCEEI…AGFVR → AARNQSSECLQVCP in BAA05910 (PubMed:7961762).CuratedAdd BLAST16
Sequence conflicti198A → V in BAA05910 (PubMed:7961762).Curated1
Sequence conflicti201M → T in BAA05910 (PubMed:7961762).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_024018591 – 615Missing in isoform 2. 1 PublicationAdd BLAST25

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D28560 mRNA Translation: BAA05910.1
DQ131564 mRNA Translation: AAZ99725.1
BC081747 mRNA Translation: AAH81747.1

Protein sequence database of the Protein Information Resource

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PIRi
A55453

NCBI Reference Sequences

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RefSeqi
NP_476445.2, NM_057104.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
84050

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:84050

UCSC genome browser

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UCSCi
RGD:69298 rat [Q64610-1]

Keywords - Coding sequence diversityi

Alternative splicing

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28560 mRNA Translation: BAA05910.1
DQ131564 mRNA Translation: AAZ99725.1
BC081747 mRNA Translation: AAH81747.1
PIRiA55453
RefSeqiNP_476445.2, NM_057104.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2XR9X-ray2.05A36-887[»]
2XRGX-ray3.20A1-887[»]
5DLTX-ray1.60A36-887[»]
5DLVX-ray2.00A/B36-887[»]
5DLWX-ray1.80A36-887[»]
5IJQX-ray2.05A36-887[»]
5IJSX-ray2.20A36-887[»]
5L0BX-ray2.41A/B1-887[»]
5L0EX-ray3.06A/B1-887[»]
5L0KX-ray2.73A/B51-884[»]
5LQQX-ray2.40A36-887[»]
5M0DX-ray2.40A36-887[»]
5M0EX-ray1.95A36-887[»]
5M0MX-ray2.10A36-887[»]
5M0SX-ray2.10A36-887[»]
SMRiQ64610
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

ChEMBLiCHEMBL3826870
GuidetoPHARMACOLOGYi2901
SwissLipidsiSLP:000000394

PTM databases

iPTMnetiQ64610

Proteomic databases

PRIDEiQ64610

Genome annotation databases

GeneIDi84050
KEGGirno:84050
UCSCiRGD:69298 rat [Q64610-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5168
RGDi69298 Enpp2

Phylogenomic databases

HOGENOMiHOG000037439
InParanoidiQ64610
KOiK01122
OrthoDBi999163at2759
PhylomeDBiQ64610

Enzyme and pathway databases

BRENDAi3.1.4.39 5301
SABIO-RKiQ64610

Miscellaneous databases

EvolutionaryTraceiQ64610

Protein Ontology

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PROi
PR:Q64610

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
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
PANTHERiPTHR10151:SF21 PTHR10151:SF21, 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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiENPP2_RAT
<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: Q64610
Secondary accession number(s): Q66HQ0
<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: September 19, 2002
Last sequence update: March 20, 2007
Last modified: September 18, 2019
This is version 151 of the entry and version 2 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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