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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

Gene

ENPP3

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi167Divalent metal cation 2Curated1
Active sitei205AMP-threonine intermediateBy similarity1
Metal bindingi325Divalent metal cation 1Curated1
Metal bindingi329Divalent metal cation 1Curated1
Metal bindingi372Divalent metal cation 2Curated1
Metal bindingi373Divalent metal cation 2Curated1
Metal bindingi482Divalent metal cation 1Curated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 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 – 873ExtracellularSequence analysisAdd BLAST843

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002829611 – 873Ectonucleotide pyrophosphatase/phosphodiesterase family member 3Add BLAST873

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 71PROSITE-ProRule annotation
Disulfide bondi54 ↔ 58PROSITE-ProRule annotation
Disulfide bondi58 ↔ 89PROSITE-ProRule annotation
Disulfide bondi69 ↔ 82PROSITE-ProRule annotation
Disulfide bondi69 ↔ 71AlternatePROSITE-ProRule annotation
Disulfide bondi75 ↔ 81PROSITE-ProRule annotation
Disulfide bondi82 ↔ 89PROSITE-ProRule annotation
Disulfide bondi98 ↔ 115AlternatePROSITE-ProRule annotation
Disulfide bondi98 ↔ 103AlternatePROSITE-ProRule annotation
Disulfide bondi103 ↔ 133AlternatePROSITE-ProRule annotation
Disulfide bondi113 ↔ 126AlternatePROSITE-ProRule annotation
Disulfide bondi113 ↔ 115AlternatePROSITE-ProRule annotation
Disulfide bondi119 ↔ 125PROSITE-ProRule annotation
Disulfide bondi126 ↔ 133AlternatePROSITE-ProRule annotation
Glycosylationi236N-linked (GlcNAc...)Sequence analysis1
Glycosylationi279N-linked (GlcNAc...)Sequence analysis1
Glycosylationi290N-linked (GlcNAc...)Sequence analysis1
Glycosylationi425N-linked (GlcNAc...)Sequence analysis1
Glycosylationi532N-linked (GlcNAc...)Sequence analysis1
Glycosylationi592N-linked (GlcNAc...)Sequence analysis1
Glycosylationi685N-linked (GlcNAc...)Sequence analysis1
Glycosylationi697N-linked (GlcNAc...)Sequence analysis1
Glycosylationi787N-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
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.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ5R5M5.

Structurei

3D structure databases

ProteinModelPortaliQ5R5M5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 93SMB 1PROSITE-ProRule annotationAdd BLAST43
Domaini94 – 138SMB 2PROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni140 – 509PhosphodiesteraseAdd BLAST370
Regioni603 – 873NucleaseAdd 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

HOVERGENiHBG051484.
InParanoidiQ5R5M5.
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.

Q5R5M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESMLTLAME QPVKRNTLKK YKIACIVLLA LLVIVSLGLG LGLGLRKPEK
60 70 80 90 100
QGSCRKKCFD ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRIWMCNQ
110 120 130 140 150
FRCGETRLEA SLCSCSDDCL QRKDCCADYK SVCQGETSWL EENCDTAQQS
160 170 180 190 200
QCPEGFDLPP VILFSMDGFR AEYLHTWDTL MPNINKLKTC GIHSKYMRAM
210 220 230 240 250
YPTKTFPNHY TIVMGLYPES HGIIDNNMYD VNLNKNFSLS SKEQNNPAWW
260 270 280 290 300
HGQPMWLTAM YQGLKAATYF WPGSEAAING SFPSIYMPYN GSVPFEERIS
310 320 330 340 350
TLLKWLDLPK AERPRFYTMY FEEPDFSGHA GGPVSARVIK ALQIVDHAFG
360 370 380 390 400
MLMEGLKQRN LHNCVNIILL ADHGMEQTYC NKMEYMTDYF PRINFYMYEG
410 420 430 440 450
PAPRIRAHSI PHDFFSFNSE EIVRNLSCRK PDQHFKPYLT PDLPKRLHYA
460 470 480 490 500
KNVRIDKVHL FVDRQWLAVR SKSNTNCGGG NHGYNNEFRS MEAIFLAHGP
510 520 530 540 550
SFKEKTEVEP FENIEVYNLM CDLLRIQPAP NNGTHGSLNH LLKVPFYEPS
560 570 580 590 600
HAEEVSKFSV CGFANPLPAE SDCLCPHLQN SIQLEQVNQM LNLTQEEITA
610 620 630 640 650
TVKVNLPFGR PRVLQKNVDH CLLYHREYVS GFGKAMRMPM WSSYTVPQLG
660 670 680 690 700
DTSPLPPTVP DCLRADVRVP PSESQKCSFY LADKNITHGF LYPPASNRTS
710 720 730 740 750
DSQYDALITS NLVPMYEEFT KMWDYFHSVL LIKHATERNG VNVVSGPIFD
760 770 780 790 800
YNYDGHFDAP DEITKHLANT DVPIPTHYFV VLTSCKNKSH TPENCPGWLD
810 820 830 840 850
VLPFIIPHRP TNMESCPEGK PEALWVEERF TAHIARVRDV ELLTGLDFYQ
860 870
EKVQPVSEIL QLKTYLPTFE TTI
Length:873
Mass (Da):99,908
Last modified:December 21, 2004 - v1
Checksum:i823149DFF08875BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860832 mRNA. Translation: CAH92941.1.
RefSeqiNP_001126732.1. NM_001133260.1.

Genome annotation databases

GeneIDi100173734.
KEGGipon:100173734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR860832 mRNA. Translation: CAH92941.1.
RefSeqiNP_001126732.1. NM_001133260.1.

3D structure databases

ProteinModelPortaliQ5R5M5.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5R5M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100173734.
KEGGipon:100173734.

Organism-specific databases

CTDi5169.

Phylogenomic databases

HOVERGENiHBG051484.
InParanoidiQ5R5M5.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiENPP3_PONAB
AccessioniPrimary (citable) accession number: Q5R5M5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, 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.