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UniProtKB/Swiss-Prot entry Q5R5M5

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

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Entry information
Entry name ENPP3_PONAB
Primary accession number Q5R5M5
Secondary accession numbers None
Integrated into Swiss-Prot on March 20, 2007
Sequence was last modified on December 21, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 20)
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
Pongo abelii (Sumatran orangutan) [TaxID: 9601] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Pongo.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
The German cDNA consortium;
Submitted (NOV-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
CR860832; CAH92941.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase Q5R5M5.
Ontologies
GO
GO:0004551; Molecular function: nucleotide diphosphatase activity (inferred from electronic annotation from EC).
GO:0004528; Molecular function: phosphodiesterase I activity (inferred from electronic annotation from EC).
QuickGo view.
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 Q5R5M5.
Phylogenomic databases
HOVERGEN Q5R5M5; -.
Other
ProtoNet Q5R5M5.
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   873  873     Ectonucleotide pyrophosphatase/phosphodiesterase family member 3. PRO_0000282961
TOPO_DOM   1    11  11     Cytoplasmic (Potential). 
TRANSMEM   12    30  19     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   31   873  843     Extracellular (Potential). 
DOMAIN   51    93  43     SMB 1. 
DOMAIN   94   138  45     SMB 2. 
REGION   140   509  370     Phosphodiesterase. 
REGION   603   873  271     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   290   290        N-linked (GlcNAc...) (Potential). 
CARBOHYD   425   425        N-linked (GlcNAc...) (Potential). 
CARBOHYD   532   532        N-linked (GlcNAc...) (Potential). 
CARBOHYD   592   592        N-linked (GlcNAc...) (Potential). 
CARBOHYD   685   685        N-linked (GlcNAc...) (Potential). 
CARBOHYD   697   697        N-linked (GlcNAc...) (Potential). 
CARBOHYD   787   787        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: 873 AA [This is the length of the unprocessed precursor] Molecular weight: 99908 Da [This is the MW of the unprocessed precursor] CRC64: 823149DFF08875BD [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MESMLTLAME QPVKRNTLKK YKIACIVLLA LLVIVSLGLG LGLGLRKPEK QGSCRKKCFD 

        70         80         90        100        110        120 
ASFRGLENCR CDVACKDRGD CCWDFEDTCV ESTRIWMCNQ FRCGETRLEA SLCSCSDDCL 

       130        140        150        160        170        180 
QRKDCCADYK SVCQGETSWL EENCDTAQQS QCPEGFDLPP VILFSMDGFR AEYLHTWDTL 

       190        200        210        220        230        240 
MPNINKLKTC GIHSKYMRAM YPTKTFPNHY TIVMGLYPES HGIIDNNMYD VNLNKNFSLS 

       250        260        270        280        290        300 
SKEQNNPAWW HGQPMWLTAM YQGLKAATYF WPGSEAAING SFPSIYMPYN GSVPFEERIS 

       310        320        330        340        350        360 
TLLKWLDLPK AERPRFYTMY FEEPDFSGHA GGPVSARVIK ALQIVDHAFG MLMEGLKQRN 

       370        380        390        400        410        420 
LHNCVNIILL ADHGMEQTYC NKMEYMTDYF PRINFYMYEG PAPRIRAHSI PHDFFSFNSE 

       430        440        450        460        470        480 
EIVRNLSCRK PDQHFKPYLT PDLPKRLHYA KNVRIDKVHL FVDRQWLAVR SKSNTNCGGG 

       490        500        510        520        530        540 
NHGYNNEFRS MEAIFLAHGP SFKEKTEVEP FENIEVYNLM CDLLRIQPAP NNGTHGSLNH 

       550        560        570        580        590        600 
LLKVPFYEPS HAEEVSKFSV CGFANPLPAE SDCLCPHLQN SIQLEQVNQM LNLTQEEITA 

       610        620        630        640        650        660 
TVKVNLPFGR PRVLQKNVDH CLLYHREYVS GFGKAMRMPM WSSYTVPQLG DTSPLPPTVP 

       670        680        690        700        710        720 
DCLRADVRVP PSESQKCSFY LADKNITHGF LYPPASNRTS DSQYDALITS NLVPMYEEFT 

       730        740        750        760        770        780 
KMWDYFHSVL LIKHATERNG VNVVSGPIFD YNYDGHFDAP DEITKHLANT DVPIPTHYFV 

       790        800        810        820        830        840 
VLTSCKNKSH TPENCPGWLD VLPFIIPHRP TNMESCPEGK PEALWVEERF TAHIARVRDV 

       850        860        870 
ELLTGLDFYQ EKVQPVSEIL QLKTYLPTFE TTI
Q5R5M5 in FASTA format

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