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Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 (E-NPP 3) (B10) (Phosphodiesterase I beta) (PD-Ibeta) (Phosphodiesterase I/nucleotide pyrophosphatase 3) (RB13-6 antigen) (CD antigen CD203c) [Includes: Alkaline phosphodiesterase I (EC 3.1.4.1); Nucleotide pyrophosphatase (NPPase) (EC 3.6.1.9) (Nucleotide diphosphatase)]

 ENPP3_RAT               Reviewed;         875 AA.
P97675; P70641; P97676; Q4V8L6; Q63490;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
22-NOV-2017, entry version 136.
RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 3;
Short=E-NPP 3;
AltName: Full=B10;
AltName: Full=Phosphodiesterase I beta;
Short=PD-Ibeta;
AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 3;
AltName: Full=RB13-6 antigen;
AltName: CD_antigen=CD203c;
Includes:
RecName: Full=Alkaline phosphodiesterase I;
EC=3.1.4.1 {ECO:0000250|UniProtKB:P06802};
Includes:
RecName: Full=Nucleotide pyrophosphatase;
Short=NPPase;
EC=3.6.1.9 {ECO:0000250|UniProtKB:P06802};
AltName: Full=Nucleotide diphosphatase {ECO:0000305};
Name=Enpp3; Synonyms=Pdnp3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 331-339; 473-504;
544-558 AND 605-618, AND GLYCOSYLATION.
STRAIN=Sprague-Dawley; TISSUE=Fetal brain;
PubMed=7730366; DOI=10.1074/jbc.270.17.9849;
Deissler H., Lottspeich F., Rajewsky M.F.;
"Affinity purification and cDNA cloning of rat neural differentiation
and tumor cell surface antigen gp130RB13-6 reveals relationship to
human and murine PC-1.";
J. Biol. Chem. 270:9849-9855(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 494-503 AND 726-746,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Intestine;
PubMed=9096610; DOI=10.1002/hep.510250434;
Scott L.J., Delautier D., Meerson N.R., Trugnan G., Goding J.W.,
Maurice M.;
"Biochemical and molecular identification of distinct forms of
alkaline phosphodiesterase I expressed on the apical and basolateral
plasma membrane surfaces of rat hepatocytes.";
Hepatology 25:995-1002(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Small intestine;
Sano K.;
"Molecular cloning of phosphodiesterase I cDNA from rat small
intestine.";
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=11069764;
Meerson N.R., Bello V., Delaunay J.-L., Slimane T.A., Delautier D.,
Lenoir C., Trugnan G., Maurice M.;
"Intracellular traffic of the ecto-nucleotide
pyrophosphatase/phosphodiesterase NPP3 to the apical plasma membrane
of MDCK and Caco-2 cells: apical targeting occurs in the absence of N-
glycosylation.";
J. Cell Sci. 113:4193-4202(2000).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Cleaves a variety of phosphodiester and phosphosulfate
bonds including deoxynucleotides, nucleotide sugars, and NAD.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
oligonucleotides. {ECO:0000250|UniProtKB:P06802}.
-!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a
nucleotide + diphosphate. {ECO:0000250|UniProtKB:P06802}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000305};
Note=Binds 2 divalent metal cations per subunit. {ECO:0000305};
-!- ENZYME REGULATION: At low concentrations of ATP, a phosphorylated
active site intermediate can be formed which inhibits further
hydrolysis. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
membrane protein {ECO:0000305}. Secreted {ECO:0000250}.
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). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in intestinal epithelium.
Also expressed in liver. {ECO:0000269|PubMed:9096610}.
-!- PTM: The N-terminal is blocked.
-!- PTM: N-glycosylation is necessary for correct trafficking to the
apical surface, but is not the apical targeting signal. No O-
glycosylation. {ECO:0000269|PubMed:11069764,
ECO:0000269|PubMed:7730366}.
-!- SIMILARITY: Belongs to the nucleotide
pyrophosphatase/phosphodiesterase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z47987; CAA88029.1; -; mRNA.
EMBL; U78787; AAB61535.1; -; mRNA.
EMBL; U78788; AAB61536.1; -; mRNA.
EMBL; D30649; BAA06333.1; -; mRNA.
EMBL; BC097326; AAH97326.1; -; mRNA.
PIR; A57080; A57080.
RefSeq; NP_062243.2; NM_019370.2.
UniGene; Rn.44; -.
ProteinModelPortal; P97675; -.
SMR; P97675; -.
STRING; 10116.ENSRNOP00000018695; -.
iPTMnet; P97675; -.
PhosphoSitePlus; P97675; -.
PaxDb; P97675; -.
PRIDE; P97675; -.
Ensembl; ENSRNOT00000018695; ENSRNOP00000018695; ENSRNOG00000013791.
GeneID; 54410; -.
KEGG; rno:54410; -.
CTD; 5169; -.
RGD; 708511; Enpp3.
eggNOG; KOG2645; Eukaryota.
eggNOG; COG1524; LUCA.
GeneTree; ENSGT00760000119157; -.
HOGENOM; HOG000037439; -.
HOVERGEN; HBG051484; -.
InParanoid; P97675; -.
KO; K01513; -.
OMA; WDYFHSV; -.
OrthoDB; EOG091G017X; -.
PhylomeDB; P97675; -.
TreeFam; TF330032; -.
BRENDA; 3.6.1.9; 5301.
SABIO-RK; P97675; -.
PRO; PR:P97675; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000013791; -.
Genevisible; P97675; RN.
GO; GO:0009986; C:cell surface; TAS:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISO:RGD.
GO; GO:0004551; F:nucleotide diphosphatase activity; TAS:RGD.
GO; GO:0004528; F:phosphodiesterase I activity; TAS:RGD.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISO:RGD.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISO:RGD.
GO; GO:0051150; P:regulation of smooth muscle cell differentiation; NAS:RGD.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
InterPro; IPR020821; Extracellular_endonuc_su_A.
InterPro; IPR002591; Phosphodiest/P_Trfase.
InterPro; IPR036024; Somatomedin_B-like_dom_sf.
InterPro; IPR001212; Somatomedin_B_dom.
Pfam; PF01223; Endonuclease_NS; 1.
Pfam; PF01663; Phosphodiest; 1.
Pfam; PF01033; Somatomedin_B; 2.
SMART; SM00892; Endonuclease_NS; 1.
SMART; SM00477; NUC; 1.
SMART; SM00201; SO; 2.
SUPFAM; SSF53649; SSF53649; 1.
SUPFAM; SSF90188; SSF90188; 2.
PROSITE; PS00524; SMB_1; 2.
PROSITE; PS50958; SMB_2; 2.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Hydrolase; Membrane; Metal-binding; Polymorphism;
Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
Transmembrane helix; Zinc.
CHAIN 1 875 Ectonucleotide
pyrophosphatase/phosphodiesterase family
member 3.
/FTId=PRO_0000188571.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 30 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 31 875 Extracellular. {ECO:0000255}.
DOMAIN 51 94 SMB 1. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
DOMAIN 95 139 SMB 2. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REGION 141 510 Phosphodiesterase.
REGION 605 875 Nuclease.
MOTIF 79 81 Cell attachment site. {ECO:0000255}.
ACT_SITE 206 206 AMP-threonine intermediate.
{ECO:0000250}.
METAL 168 168 Zinc 1; catalytic. {ECO:0000250}.
METAL 206 206 Zinc 1; catalytic. {ECO:0000250}.
METAL 326 326 Zinc 2; catalytic. {ECO:0000250}.
METAL 330 330 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 373 373 Zinc 1; catalytic. {ECO:0000250}.
METAL 374 374 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000250}.
METAL 483 483 Zinc 2; via tele nitrogen; catalytic.
{ECO:0000250}.
BINDING 227 227 Substrate. {ECO:0000250}.
BINDING 321 321 Substrate. {ECO:0000250}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 280 280 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 533 533 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 574 574 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 702 702 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 789 789 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 72 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 59 90 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 70 83 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 76 82 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 99 116 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 104 134 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 114 127 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 120 126 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 145 191 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 153 365 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 381 478 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 429 818 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 575 679 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 577 664 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 787 797 {ECO:0000255|PROSITE-ProRule:PRU00350}.
VARIANT 124 124 K -> E.
VARIANT 201 201 M -> V.
VARIANT 596 597 SG -> NR.
CONFLICT 111 111 A -> T (in Ref. 3; BAA06333).
{ECO:0000305}.
CONFLICT 273 273 P -> L (in Ref. 1; CAA88029).
{ECO:0000305}.
CONFLICT 475 476 SS -> VP (in Ref. 3; BAA06333).
{ECO:0000305}.
CONFLICT 814 814 N -> KP (in Ref. 3; BAA06333).
{ECO:0000305}.
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


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