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Reviewed, UniProtKB/Swiss-Prot P97675 (ENPP3_RAT)

Last modified November 25, 2008. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
      Short name=E-NPP 3
Alternative name(s):
    Phosphodiesterase I/nucleotide pyrophosphatase 3
    Phosphodiesterase I beta
      Short name=PD-Ibeta
    RB13-6 antigen
    B10
    CD_antigen=CD203c
Including the following 2 domains:
    1- Recommended name:
            Alkaline phosphodiesterase I
              EC=3.1.4.1
    2- Recommended name:
            Nucleotide pyrophosphatase
                Short name=NPPase
              EC=3.6.1.9
Gene names
Name: Enpp3
Synonyms: Pdnp3
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length875 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD By similarity.

Catalytic activity

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.

A dinucleotide + H(2)O = 2 mononucleotides.

Cofactor

Binds 2 divalent metal cations per subunit Probable.

Enzyme regulation

At low concentrations of ATP, a phosphorylated active site intermediate can be formed which inhibits further hydrolysis By similarity.

Subcellular location

Membrane; Single-pass type II membrane proteinPotential. SecretedBy similarity. Note= Located to the apical surface in intestinal and kidney epithelial cells. Located to the cell surface of basophils, and to the apical plasma membrane of bile duct cells. Secreted in serum, and in lumen of epithelial cells By similarity.

Tissue specificity

Highly expressed in intestinal epithelium. Also expressed in liver.

Post-translational modification

The N-terminal is blocked.

N-glycosylation is necessary for correct trafficking to the apical surface, but is not the apical targeting signal. No O-glycosylation.

It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Sequence similarities

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

Contains 2 SMB (somatomedin-B) domains.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 875875Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
PRO_0000188571

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3019Signal-anchor for type II membrane protein Potential
Topological domain31 – 875845Extracellular Potential
Domain51 – 9444SMB 1
Domain95 – 13945SMB 2
Region141 – 510370Phosphodiesterase
Region605 – 875271Nuclease
Motif79 – 813Cell attachment site Potential

Sites

Active site2061AMP-threonine intermediate By similarity
Metal binding1681Divalent metal cation 2 Probable
Metal binding3261Divalent metal cation 1 Probable
Metal binding3301Divalent metal cation 1 Probable
Metal binding3731Divalent metal cation 2 Probable
Metal binding3741Divalent metal cation 2 Probable
Metal binding4831Divalent metal cation 1 Probable

Amino acid modifications

Glycosylation2371N-linked (GlcNAc...) Potential
Glycosylation2801N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation5331N-linked (GlcNAc...) Potential
Glycosylation5741N-linked (GlcNAc...) Potential
Glycosylation5941N-linked (GlcNAc...) Potential
Glycosylation7021N-linked (GlcNAc...) Potential
Glycosylation7891N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 72Alternate By similarity
Disulfide bond55 ↔ 59Alternate By similarity
Disulfide bond59 ↔ 90Alternate By similarity
Disulfide bond70 ↔ 83Alternate By similarity
Disulfide bond70 ↔ 72Alternate By similarity
Disulfide bond76 ↔ 82 By similarity
Disulfide bond83 ↔ 90Alternate By similarity
Disulfide bond99 ↔ 116Alternate By similarity
Disulfide bond99 ↔ 104Alternate By similarity
Disulfide bond104 ↔ 134Alternate By similarity
Disulfide bond114 ↔ 127Alternate By similarity
Disulfide bond114 ↔ 116Alternate By similarity
Disulfide bond120 ↔ 126 By similarity
Disulfide bond127 ↔ 134Alternate By similarity

Natural variations

Natural variant1241K → E
Natural variant2011M → V
Natural variant596 – 5972SG → NR

Experimental info

Sequence conflict1111A → T in BAA06333. Ref.3
Sequence conflict2731P → L in CAA88029. Ref.1
Sequence conflict475 – 4762SS → VP in BAA06333. Ref.3
Sequence conflict8141N → KP in BAA06333. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
P97675-1 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 4205F263E8A933EA

FASTA87599,072
        10         20         30         40         50         60 
MDSRLALATE EPIKKDSLKR YKILCAVLLA LLVIVSLGLG LGLGLRKPEE HIGSCRKKCF 

        70         80         90        100        110        120 
DSSHRGLEGC RCDSGCTDRG DCCWDFEDTC VKSTQIWTCN SFRCGETRLE AALCSCADDC 

       130        140        150        160        170        180 
LQRKDCCTDY KAVCQGEVPW VTEACASSQE PQCPEGFDQP PVILFSMDGF RAEYLQTWST 

       190        200        210        220        230        240 
LLPNINKLKT CGLHSKYMRA MYPTKTFPNH YTIVTGLYPE SHGIIDNNMY DVYLNKNFSL 

       250        260        270        280        290        300 
SSVEKSNPAW WSGQPIWLTA MYQGLKAASY YWPGSDVAVN GSFPNIYRNY SNSVPYESRI 

       310        320        330        340        350        360 
ATLLQWLDLP KAERPSFYTI YVEEPDSAGH KSGPVSAGVI KALQLVDDAF GMLMEGLKQR 

       370        380        390        400        410        420 
NLHNCVNIIV LADHGMDQTS CDRVEYMTDY FPEINFYMYQ GPAPRIRTRN IPQDFFTFNS 

       430        440        450        460        470        480 
EEIVRDLSCR KSDQHFKPYL TPDLPKRLHY AKNVRIDKVH LMVDRQWLAY RNKGSSNCEG 

       490        500        510        520        530        540 
GTHGYNNEFK SMEAIFLAHG PSFKEKTVIE PFENIEVYNL LCDLLHIQPA PNNGSHGSLN 

       550        560        570        580        590        600 
HLLKAPFYQP SHAEELSKSA GCGFTTPLPK DSLNCSCLAL QTSGQEEQVN QRLNLSGGEV 

       610        620        630        640        650        660 
SATEKTNLPF GRPRVIQKNK DHCLLYHREY VSGFGKAMKM PMWSSYTVPK PGDTSSLPPT 

       670        680        690        700        710        720 
VPDCLRADVR VDPSESQKCS FYLADQNIDH GFLYPPAIKG NNESQYDALI TSNLVPMYKE 

       730        740        750        760        770        780 
FKKMWDYFHK VLLIKYAIER NGVNVVSGPI FDYNYDGHFD APDEITNYVA GTDVPVPTHY 

       790        800        810        820        830        840 
FVVLTSCKNK THTPDSCPGW LDVLPFVVPH RPTNVESCPE NKAEDLWVEE RFKAHIARVR 

       850        860        870 
DVELLTGLDF YQEKTQPVSE ILQLKTYLPT FETII

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References

« Hide 'large scale' references
[1]"Affinity purification and cDNA cloning of rat neural differentiation and tumor cell surface antigen gp130RB13-6 reveals relationship to human and murine PC-1."
Deissler H., Lottspeich F., Rajewsky M.F.
J. Biol. Chem. 270:9849-9855(1995) [PubMed: 7730366] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 331-339; 473-504; 544-558 AND 605-618, GLYCOSYLATION.
Strain: Sprague-Dawley.
Tissue: Fetal brain.
[2]"Biochemical and molecular identification of distinct forms of alkaline phosphodiesterase I expressed on the apical and basolateral plasma membrane surfaces of rat hepatocytes."
Scott L.J., Delautier D., Meerson N.R., Trugnan G., Goding J.W., Maurice M.
Hepatology 25:995-1002(1997) [PubMed: 9096610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 494-503 AND 726-746, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Intestine.
[3]"Molecular cloning of phosphodiesterase I cDNA from rat small intestine."
Sano K.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Small intestine.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]"Intracellular traffic of the ecto-nucleotide pyrophosphatase/phosphodiesterase NPP3 to the apical plasma membrane of MDCK and Caco-2 cells: apical targeting occurs in the absence of N-glycosylation."
Meerson N.R., Bello V., Delaunay J.-L., Slimane T.A., Delautier D., Lenoir C., Trugnan G., Maurice M.
J. Cell Sci. 113:4193-4202(2000) [PubMed: 11069764] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.

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Cross-references

Sequence databases

Z47987 mRNA. Translation: CAA88029.1.
U78787 mRNA. Translation: AAB61535.1.
U78788 mRNA. Translation: AAB61536.1.
D30649 mRNA. Translation: BAA06333.1.
BC097326 mRNA. Translation: AAH97326.1.
PIRA57080.
RefSeqNP_062243.2.
UniGeneRn.44

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000013791. Rattus norvegicus. [Contig view]
GeneID54410.
KEGGrno:54410.

Organism-specific databases

RGD708511. Enpp3.

Phylogenomic databases

HOVERGENP97675.

Gene expression databases

ArrayExpressP97675.
GermOnlineENSRNOG00000013791. Rattus norvegicus.

Family and domain databases

InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR001604. Endonuclease.
IPR002591. Phosphodiest/P_Trfase.
IPR001212. Somatomedin_B.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 1 hit.
G3DSA:3.40.570.10. Endonuclease. 1 hit.
PfamPF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
PRINTSPR00022. SOMATOMEDINB.
SMARTSM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
PROSITEPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio611055.

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Entry information

Entry nameENPP3_RAT
AccessionPrimary (citable) accession number: P97675
Secondary accession number(s): P70641 expand/collapse secondary AC list , P97676, Q4V8L6, Q63490
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: November 25, 2008
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents