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P15396

- ENPP3_BOVIN

UniProt

P15396 - ENPP3_BOVIN

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Protein

Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

Gene

ENPP3

Organism
Bos taurus (Bovine)
Status
Reviewed - 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.
A dinucleotide + H2O = 2 mononucleotides.

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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi167 – 1671Zinc 1; catalyticBy similarity
Active sitei205 – 2051AMP-threonine intermediate1 Publication
Metal bindingi205 – 2051Zinc 1; catalyticBy similarity
Binding sitei226 – 2261SubstrateBy similarity
Binding sitei320 – 3201SubstrateBy similarity
Metal bindingi325 – 3251Zinc 2; catalyticBy similarity
Metal bindingi329 – 3291Zinc 2; via tele nitrogen; catalyticBy similarity
Metal bindingi372 – 3721Zinc 1; catalyticBy similarity
Metal bindingi373 – 3731Zinc 1; via tele nitrogen; catalyticBy similarity
Metal bindingi482 – 4821Zinc 2; via tele nitrogen; catalyticBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. NADH pyrophosphatase activity Source: UniProtKB-EC
  3. nucleic acid binding Source: InterPro
  4. phosphodiesterase I activity Source: UniProtKB-EC
  5. polysaccharide binding Source: InterPro
  6. scavenger receptor activity Source: InterPro

GO - Biological processi

  1. immune response Source: InterPro
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:3.1.4.1)
Nucleotide pyrophosphatase (EC:3.6.1.9)
Short name:
NPPase
Gene namesi
Name:ENPP3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: 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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3019Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini31 – 874844ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 874874Ectonucleotide pyrophosphatase/phosphodiesterase family member 3PRO_0000058534Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi380 ↔ 477PROSITE-ProRule annotation
Glycosylationi425 – 4251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi428 ↔ 817PROSITE-ProRule annotation
Glycosylationi532 – 5321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi574 ↔ 678PROSITE-ProRule annotation
Disulfide bondi576 ↔ 663PROSITE-ProRule annotation
Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi686 – 6861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi698 – 6981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi770 – 7701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi786 ↔ 796PROSITE-ProRule annotation
Glycosylationi788 – 7881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi820 – 8201N-linked (GlcNAc...)Sequence Analysis

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

PRIDEiP15396.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000026900.

Structurei

3D structure databases

ProteinModelPortaliP15396.
SMRiP15396. Positions 96-138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 9344SMB 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 13845SMB 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni140 – 509370PhosphodiesteraseAdd
BLAST
Regioni604 – 874271NucleaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 803Cell attachment siteSequence Analysis

Sequence similaritiesi

Contains 2 SMB (somatomedin-B) domains.Curated

Keywords - Domaini

Repeat, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1524.
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.
IPR020821. Extracellular_endonuc_su_A.
IPR002591. Phosphodiest/P_Trfase.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PANTHERiPTHR10151. PTHR10151. 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.
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 .
PIRi A25274.
RefSeqi NP_001069391.1. NM_001075923.2.
UniGenei Bt.9659.

3D structure databases

ProteinModelPortali P15396.
SMRi P15396. Positions 96-138.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000026900.

Proteomic databases

PRIDEi P15396.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 529405.
KEGGi bta:529405.

Organism-specific databases

CTDi 5169.

Phylogenomic databases

eggNOGi COG1524.
HOGENOMi HOG000037439.
HOVERGENi HBG051484.
InParanoidi P15396.
KOi K01513.

Enzyme and pathway databases

SABIO-RK P15396.

Miscellaneous databases

NextBioi 20875027.

Family and domain databases

Gene3Di 3.40.570.10. 1 hit.
3.40.720.10. 1 hit.
InterProi IPR017849. 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 ]
PANTHERi PTHR10151. PTHR10151. 1 hit.
Pfami PF01223. Endonuclease_NS. 1 hit.
PF01663. Phosphodiest. 1 hit.
PF01033. Somatomedin_B. 2 hits.
[Graphical view ]
SMARTi SM00892. Endonuclease_NS. 1 hit.
SM00477. NUC. 1 hit.
SM00201. SO. 2 hits.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 1 hit.
PROSITEi PS00524. SMB_1. 2 hits.
PS50958. SMB_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

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 26, 2014
This is version 95 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

External Data

Dasty 3