Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15396 (ENPP3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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.

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.

Sequence similarities

Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.

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_0000058534

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3019Helical; Signal-anchor for type II membrane protein; Potential
Topological domain31 – 874844Extracellular Potential
Domain50 – 9344SMB 1
Domain94 – 13845SMB 2
Region140 – 509370Phosphodiesterase
Region604 – 874271Nuclease
Motif78 – 803Cell attachment site Potential

Sites

Active site2051AMP-threonine intermediate Ref.2
Metal binding1671Zinc 1; catalytic By similarity
Metal binding2051Zinc 1; catalytic By similarity
Metal binding3251Zinc 2; catalytic By similarity
Metal binding3291Zinc 2; via tele nitrogen; catalytic By similarity
Metal binding3721Zinc 1; catalytic By similarity
Metal binding3731Zinc 1; via tele nitrogen; catalytic By similarity
Metal binding4821Zinc 2; via tele nitrogen; catalytic By similarity
Binding site2261Substrate By similarity
Binding site3201Substrate By similarity

Amino acid modifications

Glycosylation2361N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential
Glycosylation5321N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation6861N-linked (GlcNAc...) Potential
Glycosylation6981N-linked (GlcNAc...) Potential
Glycosylation7701N-linked (GlcNAc...) Potential
Glycosylation7881N-linked (GlcNAc...) Potential
Glycosylation8201N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 71 By similarity
Disulfide bond58 ↔ 89 By similarity
Disulfide bond69 ↔ 82 By similarity
Disulfide bond75 ↔ 81 By similarity
Disulfide bond98 ↔ 115 By similarity
Disulfide bond103 ↔ 133 By similarity
Disulfide bond113 ↔ 126 By similarity
Disulfide bond119 ↔ 125 By similarity
Disulfide bond144 ↔ 190 By similarity
Disulfide bond152 ↔ 364 By similarity
Disulfide bond380 ↔ 477 By similarity
Disulfide bond428 ↔ 817 By similarity
Disulfide bond574 ↔ 678 By similarity
Disulfide bond576 ↔ 663 By similarity
Disulfide bond786 ↔ 796 By similarity

Sequences

Sequence LengthMass (Da)Tools
P15396 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: A901CC5B7E787F40

FASTA87499,523
        10         20         30         40         50         60 
MQSTLNLSTE EPVKRNTVKK YKIICIVLLI LLVAVSLALG LVAGLRQQEE QGSCRKKCFD 

        70         80         90        100        110        120 
ASHRGLEGCR CDVGCKGRGD CCWDFEDTCV QSTQIWTCNK FRCGETRLES SLCSCSDDCL 

       130        140        150        160        170        180 
QRKDCCADYK SVCQGETSWV DEDCSTAQQP QCPEGFDLPP VILFSMDGFR AEYLQTWSTL 

       190        200        210        220        230        240 
VPNINKLKTC GVHSQYLRPA YPTKTFPNHY TIVTGLYPES HGIIDNNMYD INLNKNFSLS 

       250        260        270        280        290        300 
SKEKDNPAWW QGQPIWLTAM YQGLKVGTYF WPGSDVAING TFPSIYKIYN RSVTYEERIF 

       310        320        330        340        350        360 
TLLKWLDLPK AERPDFYTIY VEEPDSQGHN YGPVSAGVIQ ALQLVDKTFG LLMEGLKQRN 

       370        380        390        400        410        420 
LVNCVNIILL ADHGMDQTYC DKLEYMADYF SSINFYMFEG PAPRIRTRNI PQDFFTFNSE 

       430        440        450        460        470        480 
EIVRNLSCRK PDQHFKPYLS PDLPKRLHFA KNVRIDKVNL LVDRQWQAVR NRAYSYCGGG 

       490        500        510        520        530        540 
NHGYDNEFKS MEAIFLAHGP SFKQKTEVEP FDNIEVYNLL CDLLHIQPAP NNGTHGSLNH 

       550        560        570        580        590        600 
LLKVPFYEPS HAEELSKFSV CGFTVPLPTD TLGCSCSRLQ TNSDLERVNQ MLDLTQDEIT 

       610        620        630        640        650        660 
ATEKLNLPFG RPRLIQKNKE PCLLYHREYV SGFDKTLRMP LWSSYTVPKP GDTSPLPPTV 

       670        680        690        700        710        720 
PDCLRADVRV APSESQNCSF SLADKNITHG FLYPPANNRT SNSQYDALIT SNLVPMYEAF 

       730        740        750        760        770        780 
KTMWNYFHSV LLVKYAMERN GVNVVSGPVF DYDYDGHFDA PDEIADYAVN TSVPIPTHYF 

       790        800        810        820        830        840 
VVLTSCKNQS QTPDACTGWL DVLPFVIPHR PTNVESCPEN KSESLWVEER FNVHTARVRD 

       850        860        870 
VELLTGLDFY QEKAQPVSEI LQLKTYLPVF ETVI 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[2]"Amino acid sequence of the active site peptide of bovine intestinal 5'-nucleotide phosphodiesterase and identification of the active site residue as threonine."
Culp J.S., Blytt H.J., Hermodson M., Butler L.G.
J. Biol. Chem. 260:8320-8324(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 167-226, ACTIVE SITE THR-205.
Tissue: Intestine.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC122742 mRNA. Translation: AAI22743.1.
PIRA25274.
RefSeqNP_001069391.1. NM_001075923.2.
UniGeneBt.9659.

3D structure databases

ProteinModelPortalP15396.
SMRP15396. Positions 96-138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000026900.

Proteomic databases

PRIDEP15396.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID529405.
KEGGbta:529405.

Organism-specific databases

CTD5169.

Phylogenomic databases

eggNOGCOG1524.
HOGENOMHOG000037439.
HOVERGENHBG051484.
InParanoidP15396.
KOK01513.

Enzyme and pathway databases

SABIO-RKP15396.

Family and domain databases

Gene3D3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
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]
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. SSF53649. 1 hit.
PROSITEPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20875027.

Entry information

Entry nameENPP3_BOVIN
AccessionPrimary (citable) accession number: P15396
Secondary accession number(s): Q0II99
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families