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Protein

Ectonucleoside triphosphate diphosphohydrolase 1

Gene

Entpd1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.1 Publication

Catalytic activityi

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate.1 Publication

Cofactori

Ca2+1 Publication, Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei174 – 1741Proton acceptorBy similarity

GO - Molecular functioni

  1. adenosine-diphosphatase activity Source: RGD
  2. ATPase activity Source: RGD
  3. ATP binding Source: UniProtKB-KW
  4. identical protein binding Source: RGD

GO - Biological processi

  1. cellular response to aluminum ion Source: RGD
  2. cellular response to interferon-alpha Source: RGD
  3. cellular response to lipopolysaccharide Source: RGD
  4. cellular response to tumor necrosis factor Source: RGD
  5. metabolic process Source: GOC
  6. negative regulation of ATP biosynthetic process Source: RGD
  7. negative regulation of dopamine secretion Source: RGD
  8. protein homooligomerization Source: RGD
  9. response to ATP Source: RGD
  10. response to auditory stimulus Source: RGD
  11. response to caffeine Source: RGD
  12. response to gamma radiation Source: RGD
  13. response to interferon-beta Source: RGD
  14. response to L-arginine Source: RGD
  15. response to lipopolysaccharide Source: RGD
  16. response to morphine Source: RGD
  17. response to proline Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.1.5. 5301.
3.6.1.6. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleoside triphosphate diphosphohydrolase 1 (EC:3.6.1.5)
Short name:
NTPDase 1
Alternative name(s):
Ecto-ATP diphosphohydrolase 1
Short name:
Ecto-ATPDase 1
Short name:
Ecto-ATPase 1
Ecto-apyrase
Lymphoid cell activation antigen
CD_antigen: CD39
Gene namesi
Name:Entpd1
Synonyms:Cd39
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69265. Entpd1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 478441ExtracellularSequence AnalysisAdd
BLAST
Transmembranei479 – 49921HelicalSequence AnalysisAdd
BLAST
Topological domaini500 – 51112CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: RGD
  2. cell surface Source: RGD
  3. extracellular space Source: RGD
  4. integral component of membrane Source: UniProtKB-KW
  5. neuronal cell body Source: RGD
  6. neuron projection Source: RGD
  7. postsynaptic density Source: RGD
  8. synaptic membrane Source: RGD
  9. synaptic vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511Ectonucleoside triphosphate diphosphohydrolase 1PRO_0000209904Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi84 ↔ 1081 Publication
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi254 ↔ 3001 Publication
Disulfide bondi281 ↔ 3241 Publication
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi337 ↔ 3421 Publication
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi391 ↔ 4141 Publication
Glycosylationi429 – 4291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP97687.

PTM databases

PhosphoSiteiP97687.

Expressioni

Tissue specificityi

Expressed in primary neurons and astrocytes, kidney, liver, muscle, thymus, lung and spleen.1 Publication

Gene expression databases

GenevestigatoriP97687.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi47 – 559Combined sources
Beta strandi60 – 689Combined sources
Beta strandi79 – 857Combined sources
Beta strandi87 – 893Combined sources
Helixi91 – 944Combined sources
Helixi98 – 1003Combined sources
Helixi101 – 11515Combined sources
Helixi118 – 1214Combined sources
Beta strandi125 – 1306Combined sources
Helixi132 – 1409Combined sources
Helixi142 – 15716Combined sources
Beta strandi159 – 16810Combined sources
Helixi171 – 18515Combined sources
Turni186 – 1894Combined sources
Beta strandi209 – 2135Combined sources
Beta strandi215 – 2228Combined sources
Beta strandi229 – 2313Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2406Combined sources
Beta strandi243 – 25311Combined sources
Helixi257 – 26812Combined sources
Beta strandi273 – 2797Combined sources
Beta strandi287 – 2915Combined sources
Helixi292 – 2954Combined sources
Helixi299 – 3046Combined sources
Beta strandi311 – 3177Combined sources
Helixi321 – 3299Combined sources
Beta strandi338 – 3447Combined sources
Beta strandi356 – 3605Combined sources
Helixi361 – 37212Combined sources
Helixi380 – 39112Combined sources
Helixi395 – 4017Combined sources
Helixi407 – 4104Combined sources
Helixi413 – 42513Combined sources
Helixi432 – 4376Combined sources
Beta strandi438 – 4403Combined sources
Beta strandi442 – 4443Combined sources
Beta strandi447 – 4515Combined sources
Helixi452 – 4598Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZX0X-ray2.50A/B/C/D38-189[»]
A/B/C/D207-477[»]
3ZX2X-ray1.81A/B/C/D38-189[»]
A/B/C/D207-477[»]
3ZX3X-ray1.70A/B/C/D38-189[»]
A/B/C/D207-477[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 171126N-terminal lobeAdd
BLAST
Regioni205 – 441237C-terminal lobeAdd
BLAST

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG018982.
InParanoidiP97687.
KOiK01510.
PhylomeDBiP97687.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97687-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDIKDSKVK RFCSKNILII LGFSSVLAVI ALIAVGLTHN KPLPENVKYG
60 70 80 90 100
IVLDAGSSHT NLYIYKWPAE KENDTGVVQL LEECQVKGPG ISKYAQKTDE
110 120 130 140 150
IAAYLAECMK MSTERIPASK QHQTPVYLGA TAGMRLLRME SKQSADEVLA
160 170 180 190 200
AVSRSLKSYP FDFQGAKIIT GQEEGAYGWI TINYLLGRFT QEQSWLNFIS
210 220 230 240 250
DSQKQATFGA LDLGGSSTQV TFVPLNQTLE APETSLQFRL YGTDYTVYTH
260 270 280 290 300
SFLCYGKDQA LWQKLAQDIQ VSSGGILKDP CFYPGYKKVV NVSELYGTPC
310 320 330 340 350
TKRFEKKLPF NQFQVQGTGD YEQCHQSILK FFNNSHCPYS QCAFNGVFLP
360 370 380 390 400
PLQGSFGAFS AFYFVMDFFK KMANDSVSSQ EKMTEITKNF CSKPWEEVKA
410 420 430 440 450
SYPTVKEKYL SEYCFSGTYI LSLLLQGYNF TGTSWDQIHF MGKIKDSNAG
460 470 480 490 500
WTLGYMLNLT NMIPAEQPLS PPLPHSTYIS LMVLFSLVLV AMVITGLFIF
510
SKPSYFWKEA V
Length:511
Mass (Da):57,408
Last modified:April 30, 1997 - v1
Checksum:i4CC123D3E644C193
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti332 – 3321F → L (PubMed:10581401).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81295 mRNA. Translation: AAC53195.1.
Y15685 mRNA. Translation: CAA75730.1.
RefSeqiNP_072109.1. NM_022587.1.
UniGeneiRn.17491.

Genome annotation databases

GeneIDi64519.
KEGGirno:64519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U81295 mRNA. Translation: AAC53195.1.
Y15685 mRNA. Translation: CAA75730.1.
RefSeqiNP_072109.1. NM_022587.1.
UniGeneiRn.17491.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZX0X-ray2.50A/B/C/D38-189[»]
A/B/C/D207-477[»]
3ZX2X-ray1.81A/B/C/D38-189[»]
A/B/C/D207-477[»]
3ZX3X-ray1.70A/B/C/D38-189[»]
A/B/C/D207-477[»]
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP97687.
ChEMBLiCHEMBL2767.

PTM databases

PhosphoSiteiP97687.

Proteomic databases

PRIDEiP97687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64519.
KEGGirno:64519.

Organism-specific databases

CTDi953.
RGDi69265. Entpd1.

Phylogenomic databases

HOVERGENiHBG018982.
InParanoidiP97687.
KOiK01510.
PhylomeDBiP97687.

Enzyme and pathway databases

BRENDAi3.6.1.5. 5301.
3.6.1.6. 5301.

Miscellaneous databases

NextBioi613322.
PROiP97687.

Gene expression databases

GenevestigatoriP97687.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Characterization of brain ecto-apyrase: evidence for only one ecto-apyrase (CD39) gene."
    Wang T.-F., Rosenberg P.A., Guidotti G.
    Brain Res. Mol. Brain Res. 47:295-302(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION, COFACTOR, GLYCOSYLATION, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Hippocampus.
  2. "Evidence for alternative splicing of ecto-ATPase associated with termination of purinergic transmission."
    Vlajkovic S.M., Housley G.D., Greenwood D., Thorne P.R.
    Brain Res. Mol. Brain Res. 73:85-92(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Cochlea.
  3. "An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain."
    Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.
    Neuropharmacology 36:1189-1200(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 432-511.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  4. "Crystallographic evidence for a domain motion in rat nucleoside triphosphate diphosphohydrolase (NTPDase) 1."
    Zebisch M., Krauss M., Schafer P., Strater N.
    J. Mol. Biol. 415:288-306(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 38-477, DISULFIDE BONDS.

Entry informationi

Entry nameiENTP1_RAT
AccessioniPrimary (citable) accession number: P97687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 19, 2001
Last sequence update: April 30, 1997
Last modified: March 31, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.