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Protein

Ectonucleoside triphosphate diphosphohydrolase 1

Gene

ENTPD1

Organism
Sus scrofa (Pig)
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
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.1.5. 6170.

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
Cleaved into the following 2 chains:
Gene namesi
Name:ENTPD1
Synonyms:CD39
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
ProteomesiUP000008227 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 477440ExtracellularSequence AnalysisAdd
BLAST
Transmembranei478 – 49821HelicalSequence AnalysisAdd
BLAST
Topological domaini499 – 51012CytoplasmicSequence 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 – 510510Ectonucleoside triphosphate diphosphohydrolase 1PRO_0000019905Add
BLAST
Chaini1 – 201201Ectonucleoside triphosphate diphosphohydrolase 1 27 kDa subunitPRO_0000019906Add
BLAST
Chaini202 – 510309Ectonucleoside triphosphate diphosphohydrolase 1 54 kDa subunitPRO_0000019907Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi84 ↔ 108By similarity
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi255 ↔ 300By similarity
Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi281 ↔ 324By similarity
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi337 ↔ 342By similarity
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi390 ↔ 413By similarity
Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Cleaved into two polypeptides that seem to stay together by noncovalent interactions.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Highest expression found in vascular endothelium, smooth muscle, spleen and lung.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011184.

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5371.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiQ9MYU4.
KOiK01510.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
SUPFAMiSSF56327. SSF56327. 1 hit.
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9MYU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDRRESELK TFCSKNILVI LGFSSIIAVI ALLALGLTQN KPLPENVKFG
60 70 80 90 100
IVLDAGSSHT SLYIYKWPAE KENDTGVVSQ VEECKLKGPG ISEFAKKLGE
110 120 130 140 150
IDIYLEACME RARTVVPKSQ HAETPVYLGA TAGMRLLRMK NENLASKILS
160 170 180 190 200
TVAESITRYP FDFQGARIIT GQEEGAYGWI TINYLLDKFI QKSGWFNLKP
210 220 230 240 250
RKGDTQETYG ALDLGGASTQ ITFVPQNQVL ESPENTLHFR LYGKNYSVYT
260 270 280 290 300
HSFLCYGKDQ ALLQKLTKDL KNTNGTIHEP CFHSGYQRRM NVSHLYEAPC
310 320 330 340 350
TRRFLTSLPF PELEIQGTGD FQKCQQSIRP LFNTSYCPYS RCSFDGVFLP
360 370 380 390 400
LPQGDFAAFS AFYYVMGFLN LTSEEGSFQS KVTSTLEAFC SRPWAELQMY
410 420 430 440 450
FGDVKEKYLS EYCFSGTYIL TLLLSGYHFT AETWKNIHFM GKVQSTSVGW
460 470 480 490 500
TLGYMLNLTN MIPSEEPSST RLSHSTYVFL MVLFSLILVI VVIIGLFVCH
510
RPSYFWKDMV
Length:510
Mass (Da):57,757
Last modified:September 30, 2000 - v1
Checksum:i82F86869040D7735
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 2031G → S AA sequence (PubMed:8955160).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133746 mRNA. Translation: CAB95871.1.
RefSeqiNP_999318.1. NM_214153.1.
UniGeneiSsc.52334.

Genome annotation databases

GeneIDi397298.
KEGGissc:397298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133746 mRNA. Translation: CAB95871.1.
RefSeqiNP_999318.1. NM_214153.1.
UniGeneiSsc.52334.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000011184.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397298.
KEGGissc:397298.

Organism-specific databases

CTDi953.

Phylogenomic databases

eggNOGiCOG5371.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiQ9MYU4.
KOiK01510.

Enzyme and pathway databases

BRENDAi3.6.1.5. 6170.

Family and domain databases

InterProiIPR000407. GDA1_CD39_NTPase.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
[Graphical view]
PANTHERiPTHR11782. PTHR11782. 1 hit.
PfamiPF01150. GDA1_CD39. 1 hit.
[Graphical view]
SUPFAMiSSF56327. SSF56327. 1 hit.
PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Distribution, cloning, and characterization of porcine nucleoside triphosphate diphosphohydrolase-1."
    Lemmens R., Vanduffel L., Kittel A., Beaudoin A.R., Benrezzak O., Sevigny J.
    Eur. J. Biochem. 267:4106-4114(1999) [PubMed] [Europe PMC] [Abstract]
    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 202-220.
    Tissue: Pancreas.

Entry informationi

Entry nameiENTP1_PIG
AccessioniPrimary (citable) accession number: Q9MYU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 19, 2001
Last sequence update: September 30, 2000
Last modified: March 31, 2015
This is version 92 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.