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Q6DYE8 (ENPP3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Short name=E-NPP 3
Alternative name(s):
Phosphodiesterase I beta
Short name=PD-Ibeta
Phosphodiesterase I/nucleotide pyrophosphatase 3
CD_antigen=CD203c

Including the following 2 domains:

  1. Alkaline phosphodiesterase I
    EC=3.1.4.1
  2. Nucleotide pyrophosphatase
    Short name=NPPase
    EC=3.6.1.9
Gene names
Name:Enpp3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length874 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 + H2O = 2 mononucleotides.

Cofactor

Binds 2 divalent metal cations per subunit Probable.

Enzyme regulation

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

Subcellular location

Membrane; Single-pass type II membrane protein Potential. Secreted By 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.

Post-translational modification

N-glycosylation is necessary for correct trafficking to the apical surface, but is not the apical targeting signal By similarity.

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

Contains 2 SMB (somatomedin-B) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 874874Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
PRO_0000281652

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3019Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 874844Extracellular Potential
Domain51 – 9343SMB 1
Domain94 – 13845SMB 2
Region140 – 509370Phosphodiesterase
Region605 – 874270Nuclease
Motif78 – 803Cell attachment site Potential

Sites

Active site2051AMP-threonine intermediate By similarity
Metal binding1671Divalent metal cation 2 Probable
Metal binding3251Divalent metal cation 1 Probable
Metal binding3291Divalent metal cation 1 Probable
Metal binding3721Divalent metal cation 2 Probable
Metal binding3731Divalent metal cation 2 Probable
Metal binding4821Divalent metal cation 1 Probable

Amino acid modifications

Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation2881N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential
Glycosylation5321N-linked (GlcNAc...) Potential
Glycosylation5941N-linked (GlcNAc...) Ref.3
Glycosylation6871N-linked (GlcNAc...) Potential
Glycosylation7011N-linked (GlcNAc...) Potential
Glycosylation8201N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 71Alternate By similarity
Disulfide bond54 ↔ 58Alternate By similarity
Disulfide bond58 ↔ 89Alternate By similarity
Disulfide bond69 ↔ 82Alternate By similarity
Disulfide bond69 ↔ 71Alternate By similarity
Disulfide bond75 ↔ 81 By similarity
Disulfide bond82 ↔ 89Alternate By similarity
Disulfide bond98 ↔ 115Alternate By similarity
Disulfide bond98 ↔ 103Alternate By similarity
Disulfide bond103 ↔ 133Alternate By similarity
Disulfide bond113 ↔ 126Alternate By similarity
Disulfide bond113 ↔ 115Alternate By similarity
Disulfide bond119 ↔ 125 By similarity
Disulfide bond126 ↔ 133Alternate By similarity

Experimental info

Sequence conflict2121I → S in AAT64421. Ref.1
Sequence conflict5601D → V in AAT64421. Ref.1
Sequence conflict8351A → V in AAT64421. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6DYE8 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 6CFF970ECC830D08

FASTA87498,662
        10         20         30         40         50         60 
MDSRLALATE EPIKKDSLKK YKILCVVLLA LLVIVSLGLG LGLGLRKPEE QGSCRKKCFD 

        70         80         90        100        110        120 
SSHRGLEGCR CDSGCTGRGD CCWDFEDTCV KSTQIWTCNL FRCGENRLET ALCSCADDCL 

       130        140        150        160        170        180 
QRKDCCADYK TVCQGESPWV TEACASSQEP QCPPGFDLPP VILFSMDGFR AEYLQTWSTL 

       190        200        210        220        230        240 
LPNINKLKTC GIHSKYMRAM YPTKTFPNHY TIVTGLYPES HGIIDNNMYD VHLNKNFSLS 

       250        260        270        280        290        300 
SVEKSNPAWW SGQPIWLTAM YQGLKAACYY WPGSDVAVNG SFPTIYRNYS NSVPYERRIT 

       310        320        330        340        350        360 
TLLQWLDLPK ADRPSFYTIY VEEPDSAGHS SGPVSAGVIK ALQSVDNAFG MLMEGLKQRN 

       370        380        390        400        410        420 
LHNCVNIIVL ADHGMDQTSC DRVEYMTDYF PKINFYMYQG PAPRIRTRNI PQDFFTFNSE 

       430        440        450        460        470        480 
EIVRNLSCRK PDQHFKPYLT PDLPKRLHYA KNVRIDKAHL MVDRQWLAFR SKGSSNCGGG 

       490        500        510        520        530        540 
THGYNNEFKS MEAIFLAHGP SFIEKTVIEP FENIEVYNLL CDLLHIEPAP NNGTHGSLNH 

       550        560        570        580        590        600 
LLKTPFYKPS HAGELSTPAD CGFTTPLPTD PLDCSCPALQ NTPGLEEQAN QRLNLSEGEV 

       610        620        630        640        650        660 
AATVKANLPF GRPRVMQKNG DHCLLYHRDY ISGYGKAMKM PMWSSYTVLK PGDTSSLPPT 

       670        680        690        700        710        720 
VPDCLRADVR VAPSESQKCS FYLADKNITH GFLYPAIKGT NESRYDALIT SNLVPMYKEF 

       730        740        750        760        770        780 
KKMWDYFHEV LLIKYAIERN GLNVVSGPIF DYNYDGHFDA PDEITQYVAG TDVPIPTHYF 

       790        800        810        820        830        840 
VVLTSCKDQT HTPDSCPGWL DVLPFIVPHR PTNIESCSEN KTEDLWVEER FQAHAARVRD 

       850        860        870 
VELLTGLDFY QEKAQPVSQI LQLKTYLPTF ETII

« Hide

References

« Hide 'large scale' references
[1]"Characterization of mouse ENPP3 (gp130RB13-6) as a lysophospholipase D."
Lynch K.R., Lee S.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[3]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-594, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY630402 mRNA. Translation: AAT64421.1.
AC158616 Genomic DNA. No translation available.
IPIIPI00458003.
RefSeqNP_598766.2. NM_134005.2.
UniGeneMm.338425.

3D structure databases

ProteinModelPortalQ6DYE8.
SMRQ6DYE8. Positions 50-871.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6DYE8.

PTM databases

PhosphoSiteQ6DYE8.

Proteomic databases

PRIDEQ6DYE8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020169; ENSMUSP00000020169; ENSMUSG00000019989.
GeneID209558.
KEGGmmu:209558.
UCSCuc007era.1. mouse.

Organism-specific databases

CTD5169.
MGIMGI:2143702. Enpp3.

Phylogenomic databases

HOGENOMHBG357577.
HOVERGENHBG051484.
InParanoidQ6DYE8.
OrthoDBEOG43FGW7.
PhylomeDBQ6DYE8.

Gene expression databases

ArrayExpressQ6DYE8.
BgeeQ6DYE8.
GenevestigatorQ6DYE8.

Family and domain databases

InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR001212. Somatomedin_B_dom.
[Graphical view]
Gene3DG3DSA:3.40.720.10. Alk_phosphtse. 2 hits.
G3DSA:3.40.570.10. Endonuclease. 1 hit.
KOK01513.
PANTHERPTHR10151. PTHR10151. 1 hit.
PfamPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
SMARTSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMSSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITEPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameENPP3_MOUSE
AccessionPrimary (citable) accession number: Q6DYE8
Secondary accession number(s): E9QMU8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents