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UniProtKB/Swiss-Prot entry Q6DYE8

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ENPP3_MOUSE
Primary accession number Q6DYE8
Secondary accession numbers None
Integrated into Swiss-Prot on March 20, 2007
Sequence was last modified on August 16, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 26)
Name and origin of the protein
Protein name Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Synonyms E-NPP 3
Phosphodiesterase I/nucleotide pyrophosphatase 3
Phosphodiesterase I beta
PD-Ibeta
CD203c antigen
Includes Alkaline phosphodiesterase I
     (EC 3.1.4.1)
Nucleotide pyrophosphatase
     (NPPase)
     (EC 3.6.1.9)
Gene name
Name: Enpp3
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
Lynch K.R., Lee S.;
"Characterization of mouse ENPP3 (gp130RB13-6) as a lysophospholipase D.";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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 is formed which inhibits further ATP 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).
  • PTM: N-glycosylation is necessary for correct trafficking to the apical surface, but is not the apical targeting signal (By similarity).
  • 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: 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
AY630402; AAT64421.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
UniGene Mm.338425
3D structure databases
ModBase Q6DYE8.
PTM databases
PhosphoSite Q6DYE8; -.
Organism-specific databases
MGI MGI:2143702; Enpp3.
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 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 Q6DYE8.
Genome annotation databases
Ensembl ENSMUSG00000019989; Mus musculus. [Contig view]
Phylogenomic databases
HOVERGEN Q6DYE8; -.
Other
SOURCE Enpp3; Mus musculus.
ProtoNet Q6DYE8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycoprotein; Hydrolase; Membrane; Metal-binding; Multifunctional enzyme; Repeat; Secreted; Signal-anchor; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   874  874     Ectonucleotide pyrophosphatase/phosphodiesterase family member 3. PRO_0000281652
TOPO_DOM   1    11  11     Cytoplasmic (Potential). 
TRANSMEM   12    30  19     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   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). 
ACT_SITE   205   205        AMP-threonine intermediate (By similarity). 
METAL   167   167        Divalent metal cation 2 (Probable). 
METAL   325   325        Divalent metal cation 1 (Probable). 
METAL   329   329        Divalent metal cation 1 (Probable). 
METAL   372   372        Divalent metal cation 2 (Probable). 
METAL   373   373        Divalent metal cation 2 (Probable). 
METAL   482   482        Divalent metal cation 1 (Probable). 
CARBOHYD   236   236        N-linked (GlcNAc...) (Potential). 
CARBOHYD   279   279        N-linked (GlcNAc...) (Potential). 
CARBOHYD   288   288        N-linked (GlcNAc...) (Potential). 
CARBOHYD   425   425        N-linked (GlcNAc...) (Potential). 
CARBOHYD   532   532        N-linked (GlcNAc...) (Potential). 
CARBOHYD   594   594        N-linked (GlcNAc...) (Potential). 
CARBOHYD   687   687        N-linked (GlcNAc...) (Potential). 
CARBOHYD   701   701        N-linked (GlcNAc...) (Potential). 
CARBOHYD   820   820        N-linked (GlcNAc...) (Potential). 
DISULFID   54    71        Alternate (By similarity). 
DISULFID   54    58        Alternate (By similarity). 
DISULFID   58    89        Alternate (By similarity). 
DISULFID   69    82        Alternate (By similarity). 
DISULFID   69    71        Alternate (By similarity). 
DISULFID   75    81        By similarity. 
DISULFID   82    89        Alternate (By similarity). 
DISULFID   98   115        Alternate (By similarity). 
DISULFID   98   103        Alternate (By similarity). 
DISULFID   103   133        Alternate (By similarity). 
DISULFID   113   126        Alternate (By similarity). 
DISULFID   113   115        Alternate (By similarity). 
DISULFID   119   125        By similarity. 
DISULFID   126   133        Alternate (By similarity). 
Sequence information
Length: 874 AA [This is the length of the unprocessed precursor] Molecular weight: 98648 Da [This is the MW of the unprocessed precursor] CRC64: 5DF2A30C6855F063 [This is a checksum on the sequence] 
        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
Q6DYE8 in FASTA format

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