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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

Gene

ENPP3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.By similarity
A nucleoside triphosphate + H2O = a nucleotide + diphosphate.By similarity

Cofactori

a divalent metal cationCuratedNote: Binds 2 divalent metal cations per subunit.Curated

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi167Zinc 1; catalyticBy similarity1
Active sitei205AMP-threonine intermediate1 Publication1
Metal bindingi205Zinc 1; catalyticBy similarity1
Binding sitei226SubstrateBy similarity1
Binding sitei320SubstrateBy similarity1
Metal bindingi325Zinc 2; catalyticBy similarity1
Metal bindingi329Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi372Zinc 1; catalyticBy similarity1
Metal bindingi373Zinc 1; via tele nitrogen; catalyticBy similarity1
Metal bindingi482Zinc 2; via tele nitrogen; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKP15396.

Names & Taxonomyi

Protein namesi
Recommended 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:
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
Gene namesi
Name:ENPP3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Membrane Curated; Single-pass type II membrane protein Curated
  • 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).By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 30Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST19
Topological domaini31 – 874ExtracellularSequence analysisAdd BLAST844

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3593152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000585341 – 874Ectonucleotide pyrophosphatase/phosphodiesterase family member 3Add BLAST874

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 71PROSITE-ProRule annotation
Disulfide bondi58 ↔ 89PROSITE-ProRule annotation
Disulfide bondi69 ↔ 82PROSITE-ProRule annotation
Disulfide bondi75 ↔ 81PROSITE-ProRule annotation
Disulfide bondi98 ↔ 115PROSITE-ProRule annotation
Disulfide bondi103 ↔ 133PROSITE-ProRule annotation
Disulfide bondi113 ↔ 126PROSITE-ProRule annotation
Disulfide bondi119 ↔ 125PROSITE-ProRule annotation
Disulfide bondi144 ↔ 190PROSITE-ProRule annotation
Disulfide bondi152 ↔ 364PROSITE-ProRule annotation
Glycosylationi236N-linked (GlcNAc...)Sequence analysis1
Glycosylationi279N-linked (GlcNAc...)Sequence analysis1
Glycosylationi290N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi380 ↔ 477PROSITE-ProRule annotation
Glycosylationi425N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi428 ↔ 817PROSITE-ProRule annotation
Glycosylationi532N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi574 ↔ 678PROSITE-ProRule annotation
Disulfide bondi576 ↔ 663PROSITE-ProRule annotation
Glycosylationi677N-linked (GlcNAc...)Sequence analysis1
Glycosylationi686N-linked (GlcNAc...)Sequence analysis1
Glycosylationi698N-linked (GlcNAc...)Sequence analysis1
Glycosylationi770N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi786 ↔ 796PROSITE-ProRule annotation
Glycosylationi788N-linked (GlcNAc...)Sequence analysis1
Glycosylationi820N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP15396.
PRIDEiP15396.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000026900.

Structurei

3D structure databases

ProteinModelPortaliP15396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini50 – 93SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini94 – 138SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni140 – 509PhosphodiesteraseAdd BLAST370
Regioni604 – 874NucleaseAdd BLAST271

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi78 – 80Cell attachment siteSequence analysis3

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2645. Eukaryota.
COG1524. LUCA.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiP15396.
KOiK01513.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR029885. ENPP3.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF64. PTHR10151:SF64. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
SSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSTLNLSTE EPVKRNTVKK YKIICIVLLI LLVAVSLALG LVAGLRQQEE
60 70 80 90 100
QGSCRKKCFD ASHRGLEGCR CDVGCKGRGD CCWDFEDTCV QSTQIWTCNK
110 120 130 140 150
FRCGETRLES SLCSCSDDCL QRKDCCADYK SVCQGETSWV DEDCSTAQQP
160 170 180 190 200
QCPEGFDLPP VILFSMDGFR AEYLQTWSTL VPNINKLKTC GVHSQYLRPA
210 220 230 240 250
YPTKTFPNHY TIVTGLYPES HGIIDNNMYD INLNKNFSLS SKEKDNPAWW
260 270 280 290 300
QGQPIWLTAM YQGLKVGTYF WPGSDVAING TFPSIYKIYN RSVTYEERIF
310 320 330 340 350
TLLKWLDLPK AERPDFYTIY VEEPDSQGHN YGPVSAGVIQ ALQLVDKTFG
360 370 380 390 400
LLMEGLKQRN LVNCVNIILL ADHGMDQTYC DKLEYMADYF SSINFYMFEG
410 420 430 440 450
PAPRIRTRNI PQDFFTFNSE EIVRNLSCRK PDQHFKPYLS PDLPKRLHFA
460 470 480 490 500
KNVRIDKVNL LVDRQWQAVR NRAYSYCGGG NHGYDNEFKS MEAIFLAHGP
510 520 530 540 550
SFKQKTEVEP FDNIEVYNLL CDLLHIQPAP NNGTHGSLNH LLKVPFYEPS
560 570 580 590 600
HAEELSKFSV CGFTVPLPTD TLGCSCSRLQ TNSDLERVNQ MLDLTQDEIT
610 620 630 640 650
ATEKLNLPFG RPRLIQKNKE PCLLYHREYV SGFDKTLRMP LWSSYTVPKP
660 670 680 690 700
GDTSPLPPTV PDCLRADVRV APSESQNCSF SLADKNITHG FLYPPANNRT
710 720 730 740 750
SNSQYDALIT SNLVPMYEAF KTMWNYFHSV LLVKYAMERN GVNVVSGPVF
760 770 780 790 800
DYDYDGHFDA PDEIADYAVN TSVPIPTHYF VVLTSCKNQS QTPDACTGWL
810 820 830 840 850
DVLPFVIPHR PTNVESCPEN KSESLWVEER FNVHTARVRD VELLTGLDFY
860 870
QEKAQPVSEI LQLKTYLPVF ETVI
Length:874
Mass (Da):99,523
Last modified:March 20, 2007 - v2
Checksum:iA901CC5B7E787F40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC122742 mRNA. Translation: AAI22743.1.
PIRiA25274.
RefSeqiNP_001069391.1. NM_001075923.2.
UniGeneiBt.9659.

Genome annotation databases

GeneIDi529405.
KEGGibta:529405.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC122742 mRNA. Translation: AAI22743.1.
PIRiA25274.
RefSeqiNP_001069391.1. NM_001075923.2.
UniGeneiBt.9659.

3D structure databases

ProteinModelPortaliP15396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000026900.

Chemistry databases

ChEMBLiCHEMBL3593152.

Proteomic databases

PaxDbiP15396.
PRIDEiP15396.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi529405.
KEGGibta:529405.

Organism-specific databases

CTDi5169.

Phylogenomic databases

eggNOGiKOG2645. Eukaryota.
COG1524. LUCA.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiP15396.
KOiK01513.

Enzyme and pathway databases

SABIO-RKP15396.

Family and domain databases

Gene3Di3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR001604. DNA/RNA_non-sp_Endonuclease.
IPR024873. E-NPP.
IPR029885. ENPP3.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 1 hit.
PTHR10151:SF64. PTHR10151:SF64. 1 hit.
PfamiPF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view]
SMARTiSM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
SSF90188. SSF90188. 2 hits.
PROSITEiPS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiENPP3_BOVIN
AccessioniPrimary (citable) accession number: P15396
Secondary accession number(s): Q0II99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: March 20, 2007
Last modified: November 30, 2016
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.