[1]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 331-339; 473-504; 544-558 AND 605-618, AND GLYCOSYLATION. STRAIN=Sprague-Dawley; TISSUE=Fetal brain; DOI=10.1074/jbc.270.17.9849; PubMed=7730366 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1002/hep.510250434; PubMed=9096610 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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).

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.
CATALYTIC ACTIVITY: A dinucleotide + H₂O = 2 mononucleotides.
COFACTOR: Binds 2 divalent metal cations per subunit (Probable).
ENZYME REGULATION: At low concentrations of ATP, a phosphorylated active site intermediate can be formed which inhibits further hydrolysis (By similarity).
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.
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.
PTM: 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.
SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.
SIMILARITY: Contains 2 SMB (somatomedin-B) domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z47987; CAA88029.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78787; AAB61535.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U78788; AAB61536.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D30649; BAA06333.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC097326; AAH97326.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A57080; A57080.

NP_062243.2; -.

3D structure databases

ModBase

P97675.

Organism-specific databases

RGD

708511; Enpp3.

Gene expression databases

ArrayExpress

P97675; -.

GermOnline

ENSRNOG00000013791; Rattus norvegicus.

Family and domain databases

InterPro

IPR017849; Alkaline_Pase-like_a/b/a.
IPR001604; Endonuclease.
IPR002591; Phosphodiest/P_Trfase.
IPR001212; Somatomedin_B.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.720.10; Alk_phosphtse; 1.
G3DSA:3.40.570.10; Endonuclease; 1.

Pfam

PF01663; Phosphodiest; 1.
PF01033; Somatomedin_B; 2.
Pfam graphical view of domain structure.

PRINTS

PR00022; SOMATOMEDINB.

SMART

SM00477; NUC; 1.
SM00201; SO; 2.
SMART graphical view of domain structure.

PROSITE

PS00524; SMB_1; 2.
PS50958; SMB_2; 2.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P97675.

Genome annotation databases

Ensembl

ENSRNOG00000013791; Rattus norvegicus. [Contig view]

GeneID

54410; -.

KEGG

rno:54410; -.

Phylogenomic databases

HOVERGEN

P97675; -.

Other

ProtoNet

P97675.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Metal-binding; Multifunctional enzyme; Polymorphism; Repeat; Secreted; Signal-anchor; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 875`	`875`	`Ectonucleotide pyrophosphatase/phosphodiesterase family member 3.`	`PRO_0000188571`
`TOPO_DOM`	`1 11`	`11`	`Cytoplasmic (Potential).`
`TRANSMEM`	`12 30`	`19`	`Signal-anchor for type II membrane protein (Potential).`
`TOPO_DOM`	`31 875`	`845`	`Extracellular (Potential).`
`DOMAIN`	`51 94`	`44`	`SMB 1.`
`DOMAIN`	`95 139`	`45`	`SMB 2.`
`REGION`	`141 510`	`370`	`Phosphodiesterase.`
`REGION`	`605 875`	`271`	`Nuclease.`
`MOTIF`	`79 81`	`3`	`Cell attachment site (Potential).`
`ACT_SITE`	`206 206`		`AMP-threonine intermediate (By similarity).`
`METAL`	`168 168`		`Divalent metal cation 2 (Probable).`
`METAL`	`326 326`		`Divalent metal cation 1 (Probable).`
`METAL`	`330 330`		`Divalent metal cation 1 (Probable).`
`METAL`	`373 373`		`Divalent metal cation 2 (Probable).`
`METAL`	`374 374`		`Divalent metal cation 2 (Probable).`
`METAL`	`483 483`		`Divalent metal cation 1 (Probable).`
`CARBOHYD`	`237 237`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`280 280`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`289 289`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`533 533`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`574 574`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`594 594`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`702 702`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`789 789`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`55 72`		`Alternate (By similarity).`
`DISULFID`	`55 59`		`Alternate (By similarity).`
`DISULFID`	`59 90`		`Alternate (By similarity).`
`DISULFID`	`70 83`		`Alternate (By similarity).`
`DISULFID`	`70 72`		`Alternate (By similarity).`
`DISULFID`	`76 82`		`By similarity.`
`DISULFID`	`83 90`		`Alternate (By similarity).`
`DISULFID`	`99 116`		`Alternate (By similarity).`
`DISULFID`	`99 104`		`Alternate (By similarity).`
`DISULFID`	`104 134`		`Alternate (By similarity).`
`DISULFID`	`114 127`		`Alternate (By similarity).`
`DISULFID`	`114 116`		`Alternate (By similarity).`
`DISULFID`	`120 126`		`By similarity.`
`DISULFID`	`127 134`		`Alternate (By similarity).`
`VARIANT`	`124 124`	`1`	`K -> E.`
`VARIANT`	`201 201`	`1`	`M -> V.`
`VARIANT`	`596 597`	`2`	`SG -> NR.`
`CONFLICT`	`111 111`		`A -> T (in Ref. 3; BAA06333).`
`CONFLICT`	`273 273`		`P -> L (in Ref. 1; CAA88029).`
`CONFLICT`	`475 476`		`SS -> VP (in Ref. 3; BAA06333).`
`CONFLICT`	`814 814`		`N -> KP (in Ref. 3; BAA06333).`

Sequence information

Length: 875 AA [This is the length of the unprocessed precursor]

Molecular weight: 99072 Da [This is the MW of the unprocessed precursor]

CRC64: 4205F263E8A933EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDSRLALATE EPIKKDSLKR YKILCAVLLA LLVIVSLGLG LGLGLRKPEE HIGSCRKKCF 

        70         80         90        100        110        120 
DSSHRGLEGC RCDSGCTDRG DCCWDFEDTC VKSTQIWTCN SFRCGETRLE AALCSCADDC 

       130        140        150        160        170        180 
LQRKDCCTDY KAVCQGEVPW VTEACASSQE PQCPEGFDQP PVILFSMDGF RAEYLQTWST 

       190        200        210        220        230        240 
LLPNINKLKT CGLHSKYMRA MYPTKTFPNH YTIVTGLYPE SHGIIDNNMY DVYLNKNFSL 

       250        260        270        280        290        300 
SSVEKSNPAW WSGQPIWLTA MYQGLKAASY YWPGSDVAVN GSFPNIYRNY SNSVPYESRI 

       310        320        330        340        350        360 
ATLLQWLDLP KAERPSFYTI YVEEPDSAGH KSGPVSAGVI KALQLVDDAF GMLMEGLKQR 

       370        380        390        400        410        420 
NLHNCVNIIV LADHGMDQTS CDRVEYMTDY FPEINFYMYQ GPAPRIRTRN IPQDFFTFNS 

       430        440        450        460        470        480 
EEIVRDLSCR KSDQHFKPYL TPDLPKRLHY AKNVRIDKVH LMVDRQWLAY RNKGSSNCEG 

       490        500        510        520        530        540 
GTHGYNNEFK SMEAIFLAHG PSFKEKTVIE PFENIEVYNL LCDLLHIQPA PNNGSHGSLN 

       550        560        570        580        590        600 
HLLKAPFYQP SHAEELSKSA GCGFTTPLPK DSLNCSCLAL QTSGQEEQVN QRLNLSGGEV 

       610        620        630        640        650        660 
SATEKTNLPF GRPRVIQKNK DHCLLYHREY VSGFGKAMKM PMWSSYTVPK PGDTSSLPPT 

       670        680        690        700        710        720 
VPDCLRADVR VDPSESQKCS FYLADQNIDH GFLYPPAIKG NNESQYDALI TSNLVPMYKE 

       730        740        750        760        770        780 
FKKMWDYFHK VLLIKYAIER NGVNVVSGPI FDYNYDGHFD APDEITNYVA GTDVPVPTHY 

       790        800        810        820        830        840 
FVVLTSCKNK THTPDSCPGW LDVLPFVVPH RPTNVESCPE NKAEDLWVEE RFKAHIARVR 

       850        860        870 
DVELLTGLDF YQEKTQPVSE ILQLKTYLPT FETII

P97675 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools