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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

Gene

Enpp3

Organism
Rattus norvegicus (Rat)
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 can be formed which inhibits further hydrolysis.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi168Zinc 1; catalyticBy similarity1
Active sitei206AMP-threonine intermediateBy similarity1
Metal bindingi206Zinc 1; catalyticBy similarity1
Binding sitei227SubstrateBy similarity1
Binding sitei321SubstrateBy similarity1
Metal bindingi326Zinc 2; catalyticBy similarity1
Metal bindingi330Zinc 2; via tele nitrogen; catalyticBy similarity1
Metal bindingi373Zinc 1; catalyticBy similarity1
Metal bindingi374Zinc 1; via tele nitrogen; catalyticBy similarity1
Metal bindingi483Zinc 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

BRENDAi3.6.1.9. 5301.
SABIO-RKP97675.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Short name:
E-NPP 3
Alternative name(s):
B10
Phosphodiesterase I beta
Short name:
PD-Ibeta
Phosphodiesterase I/nucleotide pyrophosphatase 3
RB13-6 antigen
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
Synonyms:Pdnp3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi708511. Enpp3.

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 – 875ExtracellularSequence analysisAdd BLAST845

GO - Cellular componenti

  • cell surface Source: RGD
  • extracellular exosome Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001885711 – 875Ectonucleotide pyrophosphatase/phosphodiesterase family member 3Add BLAST875

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi55 ↔ 72PROSITE-ProRule annotation
Disulfide bondi59 ↔ 90PROSITE-ProRule annotation
Disulfide bondi70 ↔ 83PROSITE-ProRule annotation
Disulfide bondi76 ↔ 82PROSITE-ProRule annotation
Disulfide bondi99 ↔ 116PROSITE-ProRule annotation
Disulfide bondi104 ↔ 134PROSITE-ProRule annotation
Disulfide bondi114 ↔ 127PROSITE-ProRule annotation
Disulfide bondi120 ↔ 126PROSITE-ProRule annotation
Disulfide bondi145 ↔ 191PROSITE-ProRule annotation
Disulfide bondi153 ↔ 365PROSITE-ProRule annotation
Glycosylationi237N-linked (GlcNAc...)Sequence analysis1
Glycosylationi280N-linked (GlcNAc...)Sequence analysis1
Glycosylationi289N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi381 ↔ 478PROSITE-ProRule annotation
Disulfide bondi429 ↔ 818PROSITE-ProRule annotation
Glycosylationi533N-linked (GlcNAc...)Sequence analysis1
Glycosylationi574N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi575 ↔ 679PROSITE-ProRule annotation
Disulfide bondi577 ↔ 664PROSITE-ProRule annotation
Glycosylationi594N-linked (GlcNAc...)Sequence analysis1
Glycosylationi702N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi787 ↔ 797PROSITE-ProRule annotation
Glycosylationi789N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP97675.
PRIDEiP97675.

PTM databases

iPTMnetiP97675.
PhosphoSitePlusiP97675.

Expressioni

Tissue specificityi

Highly expressed in intestinal epithelium. Also expressed in liver.1 Publication

Gene expression databases

BgeeiENSRNOG00000013791.
GenevisibleiP97675. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018695.

Structurei

3D structure databases

ProteinModelPortaliP97675.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 94SMB 1PROSITE-ProRule annotationAdd BLAST44
Domaini95 – 139SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni141 – 510PhosphodiesteraseAdd BLAST370
Regioni605 – 875NucleaseAdd BLAST271

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi79 – 81Cell 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.
GeneTreeiENSGT00760000119157.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiP97675.
KOiK01513.
OMAiRTSDSQY.
OrthoDBiEOG091G017X.
PhylomeDBiP97675.
TreeFamiTF330032.

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.

P97675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSRLALATE EPIKKDSLKR YKILCAVLLA LLVIVSLGLG LGLGLRKPEE
60 70 80 90 100
HIGSCRKKCF DSSHRGLEGC RCDSGCTDRG DCCWDFEDTC VKSTQIWTCN
110 120 130 140 150
SFRCGETRLE AALCSCADDC LQRKDCCTDY KAVCQGEVPW VTEACASSQE
160 170 180 190 200
PQCPEGFDQP PVILFSMDGF RAEYLQTWST LLPNINKLKT CGLHSKYMRA
210 220 230 240 250
MYPTKTFPNH YTIVTGLYPE SHGIIDNNMY DVYLNKNFSL SSVEKSNPAW
260 270 280 290 300
WSGQPIWLTA MYQGLKAASY YWPGSDVAVN GSFPNIYRNY SNSVPYESRI
310 320 330 340 350
ATLLQWLDLP KAERPSFYTI YVEEPDSAGH KSGPVSAGVI KALQLVDDAF
360 370 380 390 400
GMLMEGLKQR NLHNCVNIIV LADHGMDQTS CDRVEYMTDY FPEINFYMYQ
410 420 430 440 450
GPAPRIRTRN IPQDFFTFNS EEIVRDLSCR KSDQHFKPYL TPDLPKRLHY
460 470 480 490 500
AKNVRIDKVH LMVDRQWLAY RNKGSSNCEG GTHGYNNEFK SMEAIFLAHG
510 520 530 540 550
PSFKEKTVIE PFENIEVYNL LCDLLHIQPA PNNGSHGSLN HLLKAPFYQP
560 570 580 590 600
SHAEELSKSA GCGFTTPLPK DSLNCSCLAL QTSGQEEQVN QRLNLSGGEV
610 620 630 640 650
SATEKTNLPF GRPRVIQKNK DHCLLYHREY VSGFGKAMKM PMWSSYTVPK
660 670 680 690 700
PGDTSSLPPT VPDCLRADVR VDPSESQKCS FYLADQNIDH GFLYPPAIKG
710 720 730 740 750
NNESQYDALI TSNLVPMYKE FKKMWDYFHK VLLIKYAIER NGVNVVSGPI
760 770 780 790 800
FDYNYDGHFD APDEITNYVA GTDVPVPTHY FVVLTSCKNK THTPDSCPGW
810 820 830 840 850
LDVLPFVVPH RPTNVESCPE NKAEDLWVEE RFKAHIARVR DVELLTGLDF
860 870
YQEKTQPVSE ILQLKTYLPT FETII
Length:875
Mass (Da):99,072
Last modified:September 19, 2002 - v2
Checksum:i4205F263E8A933EA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti111A → T in BAA06333 (Ref. 3) Curated1
Sequence conflicti273P → L in CAA88029 (PubMed:7730366).Curated1
Sequence conflicti475 – 476SS → VP in BAA06333 (Ref. 3) Curated2
Sequence conflicti814N → KP in BAA06333 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti124K → E.1
Natural varianti201M → V.1
Natural varianti596 – 597SG → NR.2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA57080.
RefSeqiNP_062243.2. NM_019370.2.
UniGeneiRn.44.

Genome annotation databases

EnsembliENSRNOT00000018695; ENSRNOP00000018695; ENSRNOG00000013791.
GeneIDi54410.
KEGGirno:54410.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA57080.
RefSeqiNP_062243.2. NM_019370.2.
UniGeneiRn.44.

3D structure databases

ProteinModelPortaliP97675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018695.

PTM databases

iPTMnetiP97675.
PhosphoSitePlusiP97675.

Proteomic databases

PaxDbiP97675.
PRIDEiP97675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018695; ENSRNOP00000018695; ENSRNOG00000013791.
GeneIDi54410.
KEGGirno:54410.

Organism-specific databases

CTDi5169.
RGDi708511. Enpp3.

Phylogenomic databases

eggNOGiKOG2645. Eukaryota.
COG1524. LUCA.
GeneTreeiENSGT00760000119157.
HOGENOMiHOG000037439.
HOVERGENiHBG051484.
InParanoidiP97675.
KOiK01513.
OMAiRTSDSQY.
OrthoDBiEOG091G017X.
PhylomeDBiP97675.
TreeFamiTF330032.

Enzyme and pathway databases

BRENDAi3.6.1.9. 5301.
SABIO-RKP97675.

Miscellaneous databases

PROiP97675.

Gene expression databases

BgeeiENSRNOG00000013791.
GenevisibleiP97675. RN.

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_RAT
AccessioniPrimary (citable) accession number: P97675
Secondary accession number(s): P70641
, P97676, Q4V8L6, Q63490
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: November 2, 2016
This is version 130 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.