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Q9MYU4 (ENTP1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ectonucleoside triphosphate diphosphohydrolase 1
Short name=NTPDase 1
EC=3.6.1.5
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:

  1. Ectonucleoside triphosphate diphosphohydrolase 1 27 kDa subunit
  2. Ectonucleoside triphosphate diphosphohydrolase 1 54 kDa subunit
Gene names
Name:ENTPD1
Synonyms:CD39
OrganismSus scrofa (Pig) [Complete proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

ATP + 2 H2O = AMP + 2 phosphate.

Cofactor

Calcium By similarity.

Magnesium By similarity.

Subunit structure

Homodimer; disulfide-linked By similarity.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

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

Post-translational modification

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

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510Ectonucleoside triphosphate diphosphohydrolase 1
PRO_0000019905
Chain1 – 201201Ectonucleoside triphosphate diphosphohydrolase 1 27 kDa subunit
PRO_0000019906
Chain202 – 510309Ectonucleoside triphosphate diphosphohydrolase 1 54 kDa subunit
PRO_0000019907

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 477440Extracellular Potential
Transmembrane478 – 49821Helical; Potential
Topological domain499 – 51012Cytoplasmic Potential

Sites

Active site1741Proton acceptor By similarity

Amino acid modifications

Modified residue651Phosphotyrosine By similarity
Glycosylation731N-linked (GlcNAc...) Potential
Glycosylation2451N-linked (GlcNAc...) Potential
Glycosylation2741N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4571N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2031G → S AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9MYU4 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 82F86869040D7735

FASTA51057,757
        10         20         30         40         50         60 
MEDRRESELK TFCSKNILVI LGFSSIIAVI ALLALGLTQN KPLPENVKFG IVLDAGSSHT 

        70         80         90        100        110        120 
SLYIYKWPAE KENDTGVVSQ VEECKLKGPG ISEFAKKLGE IDIYLEACME RARTVVPKSQ 

       130        140        150        160        170        180 
HAETPVYLGA TAGMRLLRMK NENLASKILS TVAESITRYP FDFQGARIIT GQEEGAYGWI 

       190        200        210        220        230        240 
TINYLLDKFI QKSGWFNLKP RKGDTQETYG ALDLGGASTQ ITFVPQNQVL ESPENTLHFR 

       250        260        270        280        290        300 
LYGKNYSVYT HSFLCYGKDQ ALLQKLTKDL KNTNGTIHEP CFHSGYQRRM NVSHLYEAPC 

       310        320        330        340        350        360 
TRRFLTSLPF PELEIQGTGD FQKCQQSIRP LFNTSYCPYS RCSFDGVFLP LPQGDFAAFS 

       370        380        390        400        410        420 
AFYYVMGFLN LTSEEGSFQS KVTSTLEAFC SRPWAELQMY FGDVKEKYLS EYCFSGTYIL 

       430        440        450        460        470        480 
TLLLSGYHFT AETWKNIHFM GKVQSTSVGW TLGYMLNLTN MIPSEEPSST RLSHSTYVFL 

       490        500        510 
MVLFSLILVI VVIIGLFVCH RPSYFWKDMV

« Hide

References

[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(2000) [PubMed: 10866813] [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(1996) [PubMed: 8955160] [Abstract]
Cited for: PROTEIN SEQUENCE OF 202-220.
Tissue: Pancreas.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ133746 mRNA. Translation: CAB95871.1.
RefSeqNP_999318.1. NM_214153.1.
UniGeneSsc.52334.

3D structure databases

ProteinModelPortalQ9MYU4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9MYU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397298.
KEGGssc:397298.

Organism-specific databases

CTD953.

Phylogenomic databases

GeneTreeENSGT00550000074435.
HOVERGENHBG018982.
OrthoDBEOG48WC1R.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
[Graphical view]
KOK01510.
PANTHERPTHR11782. GDA1_CD39_NTPase. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
SUPFAMSSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameENTP1_PIG
AccessionPrimary (citable) accession number: Q9MYU4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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