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Protein

Ectonucleoside triphosphate diphosphohydrolase 1

Gene

ENTPD1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Catalytic activityi

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

Cofactori

Ca2+By similarity, Mg2+By similarity

Sites

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydrolase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 481444ExtracellularSequence AnalysisAdd
BLAST
Transmembranei482 – 50221HelicalSequence AnalysisAdd
BLAST
Topological domaini503 – 51311CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 513513Ectonucleoside triphosphate diphosphohydrolase 1PRO_0000209901Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi255 ↔ 300By similarity
Disulfide bondi281 ↔ 327By similarity
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi336 – 3361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi340 ↔ 345By similarity
Glycosylationi373 – 3731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi393 ↔ 416By similarity
Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO18956.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000045026.

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5371.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiO18956.
KOiK01510.

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.

O18956-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDRRESELK VFCSKNILSI LGFSCIIAVI ALLALGLTQN KALPENVKFG
60 70 80 90 100
IVLDAGSSHT SLYIYRWPAE KENDTGVVTQ IEESNVKGPG ISGFAKKVNE
110 120 130 140 150
INVYLTACME RAQKVIPSIQ HMETPVYLGA TAGMRLLRME NKQMADKILA
160 170 180 190 200
AVASSISEYP FDFQGARIIS GQEEGAYGWI TVNYLLGKFT QKLSWFNLKP
210 220 230 240 250
SKDDTQETYG ALDLGGASTQ ITFVPQNETT ESPNNNLYFR LYGKNYSVYT
260 270 280 290 300
HSFLCYGKDQ ALLQKLALGL QGTNGIIHEP CFHSRYMRKI KMSVLNEGFC
310 320 330 340 350
TKRHELNSSF YPLVDIEIRG AGNFQRCRQS IIQLFNTSYC PYSSCSFNGV
360 370 380 390 400
FLPPLHGQFG AFSAFYYVME FLNLTSEESV SVEQLTEKLE EFCAQRWEEV
410 420 430 440 450
QKNFGEVKEK YLSEYCFSGT YILVLLLNGY HFTAESWKNI HFMNKVRSTD
460 470 480 490 500
VGWTLGYMLN LTNKIPAEEP MSPPLPHSTY VFLMVLFSLI LLAVIIVGIV
510
VFHKPSYFWK DMV
Length:513
Mass (Da):58,114
Last modified:January 1, 1998 - v1
Checksum:i20FE98F27B6D2F96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti97 – 971K → N AA sequence (PubMed:8955160).Curated
Sequence conflicti101 – 1033INV → CGF AA sequence (PubMed:8955160).Curated
Sequence conflicti464 – 4641K → V AA sequence (PubMed:8955160).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005940 mRNA. Translation: AAB62382.1.
RefSeqiNP_776961.1. NM_174536.2.
UniGeneiBt.4117.

Genome annotation databases

GeneIDi282223.
KEGGibta:282223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005940 mRNA. Translation: AAB62382.1.
RefSeqiNP_776961.1. NM_174536.2.
UniGeneiBt.4117.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000045026.

Chemistry

BindingDBiO18956.
ChEMBLiCHEMBL2766.

Proteomic databases

PRIDEiO18956.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282223.
KEGGibta:282223.

Organism-specific databases

CTDi953.

Phylogenomic databases

eggNOGiCOG5371.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiO18956.
KOiK01510.

Miscellaneous databases

NextBioi20806045.

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. Chang A.S., Garcia R.L., Chang S.M., Schilling W.P.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Aortic endothelium.
  2. "Identification and characterization of CD39/vascular ATP diphosphohydrolase."
    Kaczmarek E., Koziak K., Sevigny J., Siegel J.B., Anrather J., Beaudoin A.R., Bach F.H., Robson S.C.
    J. Biol. Chem. 271:33116-33122(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 97-103; 123-133; 136-140; 145-168 AND 459-471.
    Tissue: Aorta.

Entry informationi

Entry nameiENTP1_BOVIN
AccessioniPrimary (citable) accession number: O18956
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 1, 1998
Last modified: April 1, 2015
This is version 100 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.