Reviewed, UniProtKB/Swiss-Prot Q6DYE8 (ENPP3_MOUSE)

Names and origin

Protein names

Recommended name:
    Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
      Short name=E-NPP 3
Alternative name(s):
    Phosphodiesterase I/nucleotide pyrophosphatase 3
    Phosphodiesterase I beta
      Short name=PD-Ibeta
    CD_antigen=CD203c
Including the following 2 domains:
    1- Recommended name:
            Alkaline phosphodiesterase I
              EC=3.1.4.1
    2- Recommended name:
            Nucleotide pyrophosphatase
                Short name=NPPase
              EC=3.6.1.9

Gene names

Name:

Enpp3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	874 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 + H(2)O = 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 By similarity.
Subcellular location	Membrane; Single-pass type II membrane proteinPotential. SecretedBy 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. 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.
Sequence similarities	Contains 2 SMB (somatomedin-B) domains.

Ontologies

Keywords
Cellular component	Membrane Secreted
Domain	Repeat Signal-anchor Transmembrane
Ligand	Metal-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	endonuclease activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid binding Inferred from electronic annotation. Source: InterPro nucleotide diphosphatase activity Inferred from electronic annotation. Source: EC phosphodiesterase I activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 874	874	Ectonucleotide pyrophosphatase/phosphodiesterase family member 3		PRO_0000281652
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 30	19	Signal-anchor for type II membrane protein Potential
	Topological domain	31 – 874	844	Extracellular Potential
	Domain	51 – 93	43	SMB 1
	Domain	94 – 138	45	SMB 2
	Region	140 – 509	370	Phosphodiesterase
	Region	605 – 874	270	Nuclease
	Motif	78 – 80	3	Cell attachment site Potential
Sites
	Active site	205	1	AMP-threonine intermediate By similarity
	Metal binding	167	1	Divalent metal cation 2 Probable
	Metal binding	325	1	Divalent metal cation 1 Probable
	Metal binding	329	1	Divalent metal cation 1 Probable
	Metal binding	372	1	Divalent metal cation 2 Probable
	Metal binding	373	1	Divalent metal cation 2 Probable
	Metal binding	482	1	Divalent metal cation 1 Probable
Amino acid modifications
	Glycosylation	236	1	N-linked (GlcNAc...) Potential
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
	Glycosylation	288	1	N-linked (GlcNAc...) Potential
	Glycosylation	425	1	N-linked (GlcNAc...) Potential
	Glycosylation	532	1	N-linked (GlcNAc...) Potential
	Glycosylation	594	1	N-linked (GlcNAc...) Potential
	Glycosylation	687	1	N-linked (GlcNAc...) Potential
	Glycosylation	701	1	N-linked (GlcNAc...) Potential
	Glycosylation	820	1	N-linked (GlcNAc...) Potential
	Disulfide bond	54 ↔ 71		Alternate By similarity
	Disulfide bond	54 ↔ 58		Alternate By similarity
	Disulfide bond	58 ↔ 89		Alternate By similarity
	Disulfide bond	69 ↔ 82		Alternate By similarity
	Disulfide bond	69 ↔ 71		Alternate By similarity
	Disulfide bond	75 ↔ 81		By similarity
	Disulfide bond	82 ↔ 89		Alternate By similarity
	Disulfide bond	98 ↔ 115		Alternate By similarity
	Disulfide bond	98 ↔ 103		Alternate By similarity
	Disulfide bond	103 ↔ 133		Alternate By similarity
	Disulfide bond	113 ↔ 126		Alternate By similarity
	Disulfide bond	113 ↔ 115		Alternate By similarity
	Disulfide bond	119 ↔ 125		By similarity
	Disulfide bond	126 ↔ 133		Alternate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6DYE8-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 5DF2A30C6855F063	FASTA	874	98,648
	10 20 30 40 50 60 MDSRLALATE EPIKKDSLKK YKILCVVLLA LLVIVSLGLG LGLGLRKPEE QGSCRKKCFD 70 80 90 100 110 120 SSHRGLEGCR CDSGCTGRGD CCWDFEDTCV KSTQIWTCNL FRCGENRLET ALCSCADDCL 130 140 150 160 170 180 QRKDCCADYK TVCQGESPWV TEACASSQEP QCPPGFDLPP VILFSMDGFR AEYLQTWSTL 190 200 210 220 230 240 LPNINKLKTC GIHSKYMRAM YPTKTFPNHY TSVTGLYPES HGIIDNNMYD VHLNKNFSLS 250 260 270 280 290 300 SVEKSNPAWW SGQPIWLTAM YQGLKAACYY WPGSDVAVNG SFPTIYRNYS NSVPYERRIT 310 320 330 340 350 360 TLLQWLDLPK ADRPSFYTIY VEEPDSAGHS SGPVSAGVIK ALQSVDNAFG MLMEGLKQRN 370 380 390 400 410 420 LHNCVNIIVL ADHGMDQTSC DRVEYMTDYF PKINFYMYQG PAPRIRTRNI PQDFFTFNSE 430 440 450 460 470 480 EIVRNLSCRK PDQHFKPYLT PDLPKRLHYA KNVRIDKAHL MVDRQWLAFR SKGSSNCGGG 490 500 510 520 530 540 THGYNNEFKS MEAIFLAHGP SFIEKTVIEP FENIEVYNLL CDLLHIEPAP NNGTHGSLNH 550 560 570 580 590 600 LLKTPFYKPS HAGELSTPAV CGFTTPLPTD PLDCSCPALQ NTPGLEEQAN QRLNLSEGEV 610 620 630 640 650 660 AATVKANLPF GRPRVMQKNG DHCLLYHRDY ISGYGKAMKM PMWSSYTVLK PGDTSSLPPT 670 680 690 700 710 720 VPDCLRADVR VAPSESQKCS FYLADKNITH GFLYPAIKGT NESRYDALIT SNLVPMYKEF 730 740 750 760 770 780 KKMWDYFHEV LLIKYAIERN GLNVVSGPIF DYNYDGHFDA PDEITQYVAG TDVPIPTHYF 790 800 810 820 830 840 VVLTSCKDQT HTPDSCPGWL DVLPFIVPHR PTNIESCSEN KTEDLWVEER FQAHVARVRD 850 860 870 VELLTGLDFY QEKAQPVSQI LQLKTYLPTF ETII

References

[1]	"Characterization of mouse ENPP3 (gp130RB13-6) as a lysophospholipase D." Lynch K.R., Lee S. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY630402 mRNA. Translation: AAT64421.1.
UniGene	Mm.338425
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q6DYE8.
Genome annotation databases
Ensembl	ENSMUSG00000019989. Mus musculus. [Contig view]
Organism-specific databases
MGI	MGI:2143702. Enpp3.
Phylogenomic databases
HOVERGEN	Q6DYE8.
Gene expression databases
ArrayExpress	Q6DYE8.
Family and domain databases
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR001604. Endonuclease. IPR002591. Phosphodiest/P_Trfase. IPR001212. Somatomedin_B. [Graphical view]
Gene3D	G3DSA:3.40.720.10. Alk_phosphtse. 1 hit. G3DSA:3.40.570.10. Endonuclease. 1 hit.
Pfam	PF01663. Phosphodiest. 1 hit. PF01033. Somatomedin_B. 2 hits. [Graphical view]
PRINTS	PR00022. SOMATOMEDINB.
SMART	SM00477. NUC. 1 hit. SM00201. SO. 2 hits. [Graphical view]
PROSITE	PS00524. SMB_1. 2 hits. PS50958. SMB_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

ENPP3_MOUSE

Accession

Primary (citable) accession number: Q6DYE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	August 16, 2004
Last modified:	November 25, 2008
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)