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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)DescriptionActionsGraphical viewLength
Active sitei174Proton acceptorBy similarity1

GO - Molecular functioni

  • adenosine-diphosphatase activity Source: RGD
  • ATPase activity Source: RGD
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: RGD

GO - Biological processi

  • cellular response to aluminum ion Source: RGD
  • cellular response to interferon-alpha Source: RGD
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • negative regulation of ATP biosynthetic process Source: RGD
  • negative regulation of dopamine secretion Source: RGD
  • protein homooligomerization Source: RGD
  • response to ATP Source: RGD
  • response to auditory stimulus Source: RGD
  • response to caffeine Source: RGD
  • response to gamma radiation Source: RGD
  • response to interferon-beta Source: RGD
  • response to L-arginine Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to morphine Source: RGD
  • 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
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69265. Entpd1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 16CytoplasmicSequence analysisAdd BLAST16
Transmembranei17 – 37HelicalSequence analysisAdd BLAST21
Topological domaini38 – 478ExtracellularSequence analysisAdd BLAST441
Transmembranei479 – 499HelicalSequence analysisAdd BLAST21
Topological domaini500 – 511CytoplasmicSequence analysisAdd BLAST12

GO - Cellular componenti

  • basolateral plasma membrane Source: RGD
  • cell surface Source: RGD
  • extracellular space Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • postsynaptic density Source: RGD
  • synaptic membrane Source: RGD
  • synaptic vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2767.
GuidetoPHARMACOLOGYi2888.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002099041 – 511Ectonucleoside triphosphate diphosphohydrolase 1Add BLAST511

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi73N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi84 ↔ 1081 Publication
Glycosylationi226N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi254 ↔ 3001 Publication
Disulfide bondi281 ↔ 3241 Publication
Glycosylationi291N-linked (GlcNAc...)Sequence analysis1
Glycosylationi333N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi337 ↔ 3421 Publication
Glycosylationi374N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi391 ↔ 4141 Publication
Glycosylationi429N-linked (GlcNAc...)Sequence analysis1
Glycosylationi458N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP97687.
PRIDEiP97687.

PTM databases

iPTMnetiP97687.
PhosphoSitePlusiP97687.

Expressioni

Tissue specificityi

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

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051602.

Chemistry databases

BindingDBiP97687.

Structurei

Secondary structure

1511
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi47 – 55Combined sources9
Beta strandi60 – 68Combined sources9
Beta strandi79 – 85Combined sources7
Beta strandi87 – 89Combined sources3
Helixi91 – 94Combined sources4
Helixi98 – 100Combined sources3
Helixi101 – 115Combined sources15
Helixi118 – 121Combined sources4
Beta strandi125 – 130Combined sources6
Helixi132 – 140Combined sources9
Helixi142 – 157Combined sources16
Beta strandi159 – 168Combined sources10
Helixi171 – 185Combined sources15
Turni186 – 189Combined sources4
Beta strandi209 – 213Combined sources5
Beta strandi215 – 222Combined sources8
Beta strandi229 – 231Combined sources3
Helixi232 – 234Combined sources3
Beta strandi235 – 240Combined sources6
Beta strandi243 – 253Combined sources11
Helixi257 – 268Combined sources12
Beta strandi273 – 279Combined sources7
Beta strandi287 – 291Combined sources5
Helixi292 – 295Combined sources4
Helixi299 – 304Combined sources6
Beta strandi311 – 317Combined sources7
Helixi321 – 329Combined sources9
Beta strandi338 – 344Combined sources7
Beta strandi356 – 360Combined sources5
Helixi361 – 372Combined sources12
Helixi380 – 391Combined sources12
Helixi395 – 401Combined sources7
Helixi407 – 410Combined sources4
Helixi413 – 425Combined sources13
Helixi432 – 437Combined sources6
Beta strandi438 – 440Combined sources3
Beta strandi442 – 444Combined sources3
Beta strandi447 – 451Combined sources5
Helixi452 – 459Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP97687.
SMRiP97687.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 171N-terminal lobeAdd BLAST126
Regioni205 – 441C-terminal lobeAdd BLAST237

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1386. Eukaryota.
COG5371. LUCA.
HOVERGENiHBG018982.
InParanoidiP97687.
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:May 1, 1997 - v1
Checksum:i4CC123D3E644C193
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti332F → L (PubMed:10581401).Curated1

Sequence databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP97687.
SMRiP97687.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000051602.

Chemistry databases

BindingDBiP97687.
ChEMBLiCHEMBL2767.
GuidetoPHARMACOLOGYi2888.

PTM databases

iPTMnetiP97687.
PhosphoSitePlusiP97687.

Proteomic databases

PaxDbiP97687.
PRIDEiP97687.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi69265. Entpd1.

Phylogenomic databases

eggNOGiKOG1386. Eukaryota.
COG5371. LUCA.
HOVERGENiHBG018982.
InParanoidiP97687.
PhylomeDBiP97687.

Enzyme and pathway databases

BRENDAi3.6.1.5. 5301.
3.6.1.6. 5301.

Miscellaneous databases

PROiP97687.

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...

Entry informationi

Entry nameiENTP1_RAT
AccessioniPrimary (citable) accession number: P97687
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 113 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

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 one 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.