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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
ENPP3_RAT, Rattus norvegicus (Norway rat) Enpp3 RB13-6 antigen Functions
wild_type
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Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 Ectonucleotide pyrophosphatase/phosphodiesterase family member 3;
Alternative name(s):
 B10
Phosphodiesterase I beta
Phosphodiesterase I/nucleotide pyrophosphatase 3
RB13-6 antigen
Alkaline phosphodiesterase I
Nucleotide pyrophosphatase
Protein IDs
(Accession numbers)
UniProtKB
 P97675
NCBI RefSeq

NP_062243.2, NM_019370.2.
Organism
Latin Name/
(Common Name)
Rattus norvegicus (Rat).
Taxonomic Identifier (NCBI)
 10116
Gene Names
 Enpp3 [GenPool]
GeneID

54410
Genome
Annotation (Ensembl)

ENSRNOT00000018695, ENSRNOP00000018695; ENSRNOG00000013791
Protein Sequence
 
SEQUENCE   875 AA;  99072 MW;  4205F263E8A933EA CRC64;
MDSRLALATE EPIKKDSLKR YKILCAVLLA LLVIVSLGLG LGLGLRKPEE HIGSCRKKCF
DSSHRGLEGC RCDSGCTDRG DCCWDFEDTC VKSTQIWTCN SFRCGETRLE AALCSCADDC
LQRKDCCTDY KAVCQGEVPW VTEACASSQE PQCPEGFDQP PVILFSMDGF RAEYLQTWST
LLPNINKLKT CGLHSKYMRA MYPTKTFPNH YTIVTGLYPE SHGIIDNNMY DVYLNKNFSL
SSVEKSNPAW WSGQPIWLTA MYQGLKAASY YWPGSDVAVN GSFPNIYRNY SNSVPYESRI
ATLLQWLDLP KAERPSFYTI YVEEPDSAGH KSGPVSAGVI KALQLVDDAF GMLMEGLKQR
NLHNCVNIIV LADHGMDQTS CDRVEYMTDY FPEINFYMYQ GPAPRIRTRN IPQDFFTFNS
EEIVRDLSCR KSDQHFKPYL TPDLPKRLHY AKNVRIDKVH LMVDRQWLAY RNKGSSNCEG
GTHGYNNEFK SMEAIFLAHG PSFKEKTVIE PFENIEVYNL LCDLLHIQPA PNNGSHGSLN
HLLKAPFYQP SHAEELSKSA GCGFTTPLPK DSLNCSCLAL QTSGQEEQVN QRLNLSGGEV
SATEKTNLPF GRPRVIQKNK DHCLLYHREY VSGFGKAMKM PMWSSYTVPK PGDTSSLPPT
VPDCLRADVR VDPSESQKCS FYLADQNIDH GFLYPPAIKG NNESQYDALI TSNLVPMYKE
FKKMWDYFHK VLLIKYAIER NGVNVVSGPI FDYNYDGHFD APDEITNYVA GTDVPVPTHY
FVVLTSCKNK THTPDSCPGW LDVLPFVVPH RPTNVESCPE NKAEDLWVEE RFKAHIARVR
DVELLTGLDF YQEKTQPVSE ILQLKTYLPT FETII
General annotation
Function
 Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity).
Cofactor
 Binds 2 divalent metal cations per subunit (Probable).
Subunit structure
Subcellular location

Membrane; Single-pass type II membrane protein (Potential). 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).
Tissue specificity
 Highly expressed in intestinal epithelium. Also expressed in liver.
Induction
Domain
Post-translational modification

The N-terminal is blocked.

N-glycosylation is necessary for correct trafficking to theapical surface, but is not the apical targeting signal. No O-glycosylation.

It has been suggested that the active SMB domain may bepermitted considerable disulfide bond heterogeneity orvariability, thus two alternate disulfide patterns based on 3Dstructures are described with 1 disulfide bond conserved in both.
Involvement in disease

References

  • "Affinity purification and cDNA cloning of rat neural differentiationand tumor cell surface antigen gp130RB13-6 reveals relationship tohuman and murine PC-1.";,Deissler H., Lottspeich F., Rajewsky M.F.;,J. Biol. Chem. 270:9849-9855(1995)., PubMeb:7730366 DOI:10.1074/jbc.270.17.9849

  • "Biochemical and molecular identification of distinct forms ofalkaline phosphodiesterase I expressed on the apical and basolateralplasma membrane surfaces of rat hepatocytes.";,Scott L.J., Delautier D., Meerson N.R., Trugnan G., Goding J.W.,Maurice M.;,Hepatology 25:995-1002(1997)., PubMeb:9096610 DOI:10.1002/hep.510250434

  • "Molecular cloning of phosphodiesterase I cDNA from rat smallintestine.";,Sano K.;,Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.

  • "The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).";,Genome Res. 14:2121-2127(2004).,PubMeb:15489334 DOI:10.1101/gr.2596504

  • "Intracellular traffic of the ecto-nucleotidepyrophosphatase/phosphodiesterase NPP3 to the apical plasma membraneof MDCK and Caco-2 cells: apical targeting occurs in the absence of N-glycosylation.";,Meerson N.R., Bello V., Delaunay J.-L., Slimane T.A., Delautier D.,Lenoir C., Trugnan G., Maurice M.;,J. Cell Sci. 113:4193-4202(2000).,PubMeb:11069764

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Protein Domain Databases | 3D Structure Database  | Sequence Annotation | Protein-protein Interaction Databases  | 
Binary Interactions | Enzyme and Pathway Databases |  Phylogenomic Database | Proteomics Database | 
Comparative Toxicogenomics Database | Order
Protein Domain Databases
InterPro

IPR017849, Alkaline_Pase-like_a/b/a.

IPR017850, Alkaline_phosphatase_core.

IPR001604, DNA/RNA_non-sp_Endonuclease.

IPR020821, Extracellular_endonuc_su_A.

IPR002591, Phosphodiest/P_Trfase.

IPR001212, Somatomedin_B_dom.
Gene3D

G3DSA:3.40.720.10, Alk_phosphtse; 2.

G3DSA:3.40.570.10, Endonuclease; 1.
PANTHER
Pfam

PF01223, Endonuclease_NS; 1.

PF01663, Phosphodiest; 1.

PF01033, Somatomedin_B; 2.
PRINTS
SUPFAM

SSF53649, Alkaline_phosphatase_core; 1.
PROSITE

PS00524, SMB_1; 2.

PS50958, SMB_2; 2.
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Polypeptide chain 1 - 875 875 Ectonucleotide /FTId=PRO_0000188571.
Topological domain 1 - 11 11 Cytoplasmic (Potential).
Topological domain 31 - 875 845 Extracellular (Potential).
Transmembrane region 12 - 30 19 Helical; Signal-anchor for type II
Domain 51 - 94 44 SMB 1.
Domain 95 - 139 45 SMB 2.
Region 141 - 510 370 Phosphodiesterase.
Region 605 - 875 271 Nuclease.
Sequence motif 79 - 81 3 Cell attachment site (Potential).
Amino acid(s) 206 1 AMP-threonine intermediate (By
Metal ion 168 1 Divalent metal cation 2 (Probable).
Metal ion 326 1 Divalent metal cation 1 (Probable).
Metal ion 330 1 Divalent metal cation 1 (Probable).
Metal ion 373 1 Divalent metal cation 2 (Probable).
Metal ion 374 1 Divalent metal cation 2 (Probable).
Metal ion 483 1 Divalent metal cation 1 (Probable).
Glycosylation site 237 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 280 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 289 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 533 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 574 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 594 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 702 1 N-linked (GlcNAc...) (Potential).
Glycosylation site 789 1 N-linked (GlcNAc...) (Potential).
Disulfide bond 55 - 72 18 Alternate (By similarity).
Disulfide bond 55 - 59 5 Alternate (By similarity).
Disulfide bond 59 - 90 32 Alternate (By similarity).
Disulfide bond 70 - 83 14 Alternate (By similarity).
Disulfide bond 70 - 72 3 Alternate (By similarity).
Disulfide bond 76 - 82 7 By similarity.
Disulfide bond 83 - 90 8 Alternate (By similarity).
Disulfide bond 99 - 116 18 Alternate (By similarity).
Disulfide bond 99 - 104 6 Alternate (By similarity).
Disulfide bond 104 - 134 31 Alternate (By similarity).
Disulfide bond 114 - 127 14 Alternate (By similarity).
Disulfide bond 114 - 116 3 Alternate (By similarity).
Disulfide bond 120 - 126 7 By similarity.
Disulfide bond 127 - 134 8 Alternate (By similarity).
Natural variance 124 1 K -> E.
Natural variance 201 1 M -> V.
Natural variance 596 - 597 2 SG -> NR.
Different sources report differing sequences 111 1 A -> T (in Ref. 3; BAA06333).
Different sources report differing sequences 273 1 P -> L (in Ref. 1; CAA88029).
Different sources report differing sequences 475 - 476 2 SS -> VP (in Ref. 3; BAA06333).
Different sources report differing sequences 814 1 N -> KP (in Ref. 3; BAA06333).
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING

P97675
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG051484
InParanoid

P97675
OMA

FGMLMEG
OrthoDB

EOG43FGW7
Proteomics
Database (PRIDE)

P97675
Comparative
Toxicogenomics
Database (CTD)

5169
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