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Reviewed, UniProtKB/Swiss-Prot O75355 (ENTP3_HUMAN)

Last modified November 3, 2009. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Ectonucleoside triphosphate diphosphohydrolase 3
      Short name=NTPDase 3
    EC=3.6.1.5
Alternative name(s):
    Ecto-ATP diphosphohydrolase
      Short name=ATPDase
      Short name=Ecto-apyrase
    CD39 antigen-like 3
    HB6
Gene names
Name: ENTPD3
Synonyms: CD39L3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Has a threefold preference for the hydrolysis of ATP over ADP.

Catalytic activity

ATP + 2 H2O = AMP + 2 phosphate.

Cofactor

Calcium.

Magnesium.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed in adult brain, pancreas, spleen and prostate. Moderate or low expression is seen in most tissues. Not expressed in liver and peripheral blood leukocytes.

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

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Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
   LigandATP-binding
Calcium
Magnesium
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Ectonucleoside triphosphate diphosphohydrolase 3
PRO_0000209910

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4321 Potential
Topological domain44 – 485442Extracellular Potential
Transmembrane486 – 50621 Potential
Topological domain507 – 52923Cytoplasmic Potential

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1491N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential

Natural variations

Natural variant4401E → D: dbSNP rs4470483.
VAR_027541
Natural variant4961A → V: dbSNP rs1047855. Ref.1
VAR_027542
Natural variant5051L → F: dbSNP rs3733167.
VAR_027543

Experimental info

Mutagenesis671R → G: Increase of activity. Ref.5
Mutagenesis1431R → A: Loss of activity. Ref.5
Mutagenesis1431R → K: Increase of activity. Ref.5
Mutagenesis1461R → N: No effect. Ref.5
Mutagenesis1461R → P: Increase of ATPase activity, decrease of ADPase activity. Ref.5
Mutagenesis1461R → T: Increase of activity. Ref.5
Mutagenesis1821E → D: Complete loss of activity. Ref.5
Mutagenesis1821E → Q: Complete loss of activity. Ref.5
Mutagenesis1871W → A: Complete loss of activity. Ref.4
Mutagenesis1911N → A: Loss of ATPase activity, increase of ADPase activity. Ref.5
Mutagenesis2191D → E: Increase of activity. Ref.4
Mutagenesis2241S → A: Complete loss of activity. Ref.5
Mutagenesis2261Q → A: Loss of activity. Ref.5
Mutagenesis4591W → A: Increase of activity, especially the ATP hydrolysis. Ref.4

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Sequences

Sequence LengthMass (Da)Tools
O75355-1 [UniParc].

Last modified September 19, 2006. Version 2.
Checksum: 5043CF0202978B88

FASTA52959,105
        10         20         30         40         50         60 
MFTVLTRQPC EQAGLKALYR TPTIIALVVL LVSIVVLVSI TVIQIHKQEV LPPGLKYGIV 

        70         80         90        100        110        120 
LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV 

       130        140        150        160        170        180 
KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ 

       190        200        210        220        230        240 
EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS 

       250        260        270        280        290        300 
DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM 

       310        320        330        340        350        360 
GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ 

       370        380        390        400        410        420 
PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS 

       430        440        450        460        470        480 
YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL 

       490        500        510        520 
PIEPPVFVGT LAFFTAAALL CLAFLAYLCS ATRRKRHSEH AFDHAVDSD

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References

[1]"The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster."
Chadwick B.P., Frischauf A.-M.
Genomics 50:357-367(1998) [PubMed: 9676430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-496.
Tissue: Keratinocyte.
[2]"Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases."
Smith T.M., Kirley T.L.
Biochim. Biophys. Acta 1386:65-78(1998) [PubMed: 9675246] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Tissue: Brain.
[3]Smith T.M., Kirley T.L.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase."
Smith T.M., Lewis Carl S.A., Kirley T.L.
Biochemistry 38:5849-5857(1999) [PubMed: 10231536] [Abstract]
Cited for: MUTAGENESIS OF TRP-187; ASP-219 AND TRP-459.
[5]"Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions."
Yang F., Hicks-Berger C.A., Smith T.M., Kirley T.L.
Biochemistry 40:3943-3950(2001) [PubMed: 11300774] [Abstract]
Cited for: MUTAGENESIS OF ARG-67; ARG-143; ARG-146; GLU-182; ASN-191; SER-224 AND GLN-226.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF039917 mRNA. Translation: AAC39884.1.
AF034840 mRNA. Translation: AAC09236.2.
IPIIPI00025297.
RefSeqNP_001239.2.
UniGeneHs.441145

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGO75355.

Proteomic databases

PRIDEO75355.

Genome annotation databases

EnsemblENST00000301825; ENSP00000301825; ENSG00000168032; Homo sapiens. [Genome view]
ENST00000439533; ENSP00000406555; ENSG00000168032; Homo sapiens. [Genome view]
ENST00000445129; ENSP00000404671; ENSG00000168032; Homo sapiens. [Genome view]
ENST00000456402; ENSP00000401565; ENSG00000168032; Homo sapiens. [Genome view]
GeneID956.
KEGGhsa:956.
UCSCuc003ckd.2. human.

Organism-specific databases

CTD956.
GeneCardsGC03P040403.
H-InvDBHIX0003195.
HIX0031158.
HGNCHGNC:3365. ENTPD3.
MIM603161. gene.
PharmGKBPA27800.
GenAtlasSearch...

Phylogenomic databases

HOVERGENO75355.
OMAVYQWPAE.

Enzyme and pathway databases

BRENDA3.6.1.5. 247.

Gene expression databases

ArrayExpressO75355.
BgeeO75355.
CleanExHS_ENTPD3.
GenevestigatorO75355.
GermOnlineENSG00000168032. Homo sapiens.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERPTHR11782. GDA1_CD39_NTPase. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3982.
SOURCESearch...

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Entry information

Entry nameENTP3_HUMAN
AccessionPrimary (citable) accession number: O75355
Secondary accession number(s): O60495
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: September 19, 2006
Last modified: November 3, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents