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Entry version 129 (16 Jan 2019)
Sequence version 2 (19 Sep 2002)
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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 1

Gene

Enpp1

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

By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. 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. 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. Appears to modulate insulin sensitivity.By similarity

Caution

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

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

  • Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.By similarity EC:3.1.4.1

<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+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

<p>This subsection of the ‘Function’ 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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; catalyticBy similarity1
<p>This subsection of the ‘Function’ 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 intermediateBy similarity1
Metal bindingi238Zinc 1; catalyticBy similarity1
<p>This subsection of the ‘Function’ 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 sitei259SubstrateBy similarity1
Binding sitei277SubstrateBy similarity1
Binding sitei322SubstrateBy similarity1
Metal bindingi358Zinc 2; catalyticBy similarity1
Metal bindingi362Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi405Zinc 1; catalyticBy similarity1
Metal bindingi406Zinc 1; via tele nitrogen; catalyticBy similarity1
Metal bindingi517Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi781CalciumBy similarity1
Metal bindingi783CalciumBy similarity1
Metal bindingi785CalciumBy similarity1
Metal bindingi787Calcium; via carbonyl oxygenBy similarity1
Metal bindingi789CalciumBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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 5301
3.6.1.9 5301

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q924C3

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Short name:
E-NPP 1
Alternative name(s):
Phosphodiesterase I/nucleotide pyrophosphatase 1
Plasma-cell membrane glycoprotein PC-1
Including the following 2 domains:
Alkaline phosphodiesterase I (EC:3.1.4.1By similarity)
Nucleotide pyrophosphatase (EC:3.6.1.9By similarity)
Short name:
NPPase
Alternative name(s):
Nucleotide diphosphataseCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Enpp1
Synonyms:Npps, Pc1, Pdnp1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>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
628825 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_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 58CytoplasmicSequence analysisAdd BLAST58
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei59 – 79Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini80 – 906ExtracellularSequence analysisAdd BLAST827

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

<p>This section 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001885661 – 906Ectonucleotide pyrophosphatase/phosphodiesterase family member 1Add BLAST906

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 residuei25PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi90 ↔ 104PROSITE-ProRule annotation
Disulfide bondi94 ↔ 122PROSITE-ProRule annotation
Disulfide bondi102 ↔ 115PROSITE-ProRule annotation
Disulfide bondi108 ↔ 114PROSITE-ProRule annotation
Disulfide bondi131 ↔ 148PROSITE-ProRule annotation
Disulfide bondi136 ↔ 166PROSITE-ProRule annotation
Disulfide bondi146 ↔ 159PROSITE-ProRule annotation
Disulfide bondi152 ↔ 158PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi161N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi177 ↔ 223PROSITE-ProRule annotation
Disulfide bondi185 ↔ 397PROSITE-ProRule annotation
Modified residuei238PhosphothreonineCombined sources1
Glycosylationi267N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi323N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi413 ↔ 512PROSITE-ProRule annotation
Glycosylationi459N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi462 ↔ 849PROSITE-ProRule annotation
Glycosylationi567N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi596 ↔ 653PROSITE-ProRule annotation
Disulfide bondi607 ↔ 707PROSITE-ProRule annotation
Disulfide bondi609 ↔ 692PROSITE-ProRule annotation
Glycosylationi624N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi819 ↔ 829PROSITE-ProRule annotation

<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

A secreted form is produced through cleavage at Lys-85 by intracellular processing.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei84 – 85CleavageBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q924C3

PRoteomics IDEntifications database

More...
PRIDEi
Q924C3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q924C3

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

More...
PhosphoSitePlusi
Q924C3

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. The secreted form is monomeric. Interacts with INSR.By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000019519

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q924C3

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

More...
SMRi
Q924C3

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini86 – 126SMB 1PROSITE-ProRule annotationAdd BLAST41
Domaini127 – 170SMB 2PROSITE-ProRule annotationAdd BLAST44

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 – 573PhosphodiesteraseAdd BLAST401
Regioni579 – 628LinkerBy similarityAdd BLAST50
Regioni635 – 906NucleaseAdd 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 motif8

<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 epithelial cells, and for targeting to matrix vesicles derived from mineralizing cells.By similarity

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

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2645 Eukaryota
COG1524 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000037439

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG051484

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q924C3

KEGG Orthology (KO)

More...
KOi
K01513

Database of Orthologous Groups

More...
OrthoDBi
999163at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q924C3

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
IPR017849 Alkaline_Pase-like_a/b/a
IPR017850 Alkaline_phosphatase_core_sf
IPR001604 DNA/RNA_non-sp_Endonuclease
IPR020821 Extracellular_endonuc_su_A
IPR002591 Phosphodiest/P_Trfase
IPR036024 Somatomedin_B-like_dom_sf
IPR020436 Somatomedin_B_chordata
IPR001212 Somatomedin_B_dom

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00022 SOMATOMEDINB

Simple Modular Architecture Research Tool; a protein domain database

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

Superfamily database of structural and functional annotation

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

PROSITE; a protein domain and family database

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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

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 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 2 (identifier: Q924C3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MERDGEQAGQ GPRHGPAGNG RELESPAAAS LLAPMDLGEE PLEKAERART
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
DCKAHNDCCI NYSSVCQEKK SWVEEACETI DAPQCPAEFE SPPTLLFSLD
210 220 230 240 250
GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPVYPTKTFP NHYSIVTGLY
260 270 280 290 300
PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVRSG
310 320 330 340 350
TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSYERPHFY
360 370 380 390 400
TLYLEEPDSS GHSHGPVSSE VIKALQKVDH IVGMLMDGLK DLGLDKCLNL
410 420 430 440 450
ILISDHGMEQ GSCKKYVYLN KYLGDVNNVK VVYGPAARLR PTEVPETYYS
460 470 480 490 500
FNYEALAKNL SCRETNQHFR PYLKHFLPKR LHFAKNDRIE PLTFYLDPQW
510 520 530 540 550
QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG AEVDSFENIE
560 570 580 590 600
VYNLMCDLLG LIPAPNNESH GSLNHLLKKP IYTPSHPKEE SFLSQCPIKS
610 620 630 640 650
VSSDLGCTCD PSIVPIMDFE KQFNLTTDAV EDVYSMTVPN GRPRNLQKQH
660 670 680 690 700
RVCLLHQQQF LTGYSLDLLM PLWTSYTFLS NDQFSTDDFS NCLYQDLRIP
710 720 730 740 750
LSPMHKCSYY KSTSKLSYGF LTPPRLNRVS RQIYSEALLT SNIVPMYQSF
760 770 780 790 800
QVIWQYLHDT VLRRYAQERN GVNVVSGPVF DFDYDGRYDS SEILKQNTRV
810 820 830 840 850
IRSQENLIPT HFFIVLTSCK QLSESPLKCT ALESSAFLLP HRPDNIESCT
860 870 880 890 900
HGKQESAWVE ELLALHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP

IFSQED
Length:906
Mass (Da):102,942
Last modified:September 19, 2002 - 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:i71F56780B279A919
GO
Isoform 1 (identifier: Q924C3-2) [UniParc]FASTAAdd to basket

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

Show »
Length:905
Mass (Da):102,843
Checksum:i46EE88917B4BBCD3
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V7V4G3V7V4_RAT
Ectonucleotide pyrophosphatase/phos...
Enpp1
872Annotation 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>

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 varianti440 – 442RPT → NPP in strain: Wistar. 3
Natural varianti457A → T in strain: Lewis. 1
Natural varianti555M → I in strain: Lewis. 1
Natural varianti568E → G in strain: Wistar. 1
Natural varianti583T → I in strain: Lewis. 1
Natural varianti592F → V in strain: Lewis. 1
Natural varianti624N → K in strain: Lewis. 1
Natural varianti640N → H in strain: Lewis. 1
Natural varianti774V → I in strain: Lewis. 1
Natural varianti806N → I in strain: Lewis. 1
Natural varianti850T → I in strain: Lewis. 1
Natural varianti898H → Q in strain: Lewis. 1

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_006749630Missing in isoform 1. 1 Publication1

Sequence databases

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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
AF340185 mRNA Translation: AAK69653.1
AF340186 mRNA Translation: AAK69654.1
AF320054 mRNA Translation: AAL26912.1

NCBI Reference Sequences

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RefSeqi
NP_445987.1, NM_053535.1 [Q924C3-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Rn.1199

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
85496

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:85496

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
AF340185 mRNA Translation: AAK69653.1
AF340186 mRNA Translation: AAK69654.1
AF320054 mRNA Translation: AAL26912.1
RefSeqiNP_445987.1, NM_053535.1 [Q924C3-1]
UniGeneiRn.1199

3D structure databases

ProteinModelPortaliQ924C3
SMRiQ924C3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000019519

PTM databases

iPTMnetiQ924C3
PhosphoSitePlusiQ924C3

Proteomic databases

PaxDbiQ924C3
PRIDEiQ924C3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi85496
KEGGirno:85496

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5167
RGDi628825 Enpp1

Phylogenomic databases

eggNOGiKOG2645 Eukaryota
COG1524 LUCA
HOGENOMiHOG000037439
HOVERGENiHBG051484
InParanoidiQ924C3
KOiK01513
OrthoDBi999163at2759
PhylomeDBiQ924C3

Enzyme and pathway databases

BRENDAi3.1.4.1 5301
3.6.1.9 5301
SABIO-RKiQ924C3

Miscellaneous databases

Protein Ontology

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PROi
PR:Q924C3

Family and domain databases

Gene3Di3.40.720.10, 1 hit
InterProiView protein in InterPro
IPR017849 Alkaline_Pase-like_a/b/a
IPR017850 Alkaline_phosphatase_core_sf
IPR001604 DNA/RNA_non-sp_Endonuclease
IPR020821 Extracellular_endonuc_su_A
IPR002591 Phosphodiest/P_Trfase
IPR036024 Somatomedin_B-like_dom_sf
IPR020436 Somatomedin_B_chordata
IPR001212 Somatomedin_B_dom
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
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiENPP1_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: Q924C3
Secondary accession number(s): Q91XQ3, Q920C8
<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: September 19, 2002
Last modified: January 16, 2019
This is version 129 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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