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Protein

Ectonucleoside triphosphate diphosphohydrolase 2

Gene

ENTPD2

Organism
Homo sapiens (Human)
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. Hydrolyzes ADP only to a marginal extent. The order of activity with different substrates is ATP > GTP > CTP = ITP > UTP >> ADP = UDP.

Cofactori

Ca2+1 Publication, Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei165 – 1651Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2085ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000054179-MONOMER.
BRENDAi3.6.1.5. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Ectonucleoside triphosphate diphosphohydrolase 2 (EC:3.6.1.-)
Short name:
NTPDase 2
Alternative name(s):
CD39 antigen-like 1
Ecto-ATP diphosphohydrolase 2
Short name:
Ecto-ATPDase 2
Short name:
Ecto-ATPase 2
Gene namesi
Name:ENTPD2
Synonyms:CD39L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:3364. ENTPD2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence analysis
Transmembranei8 – 2821HelicalSequence analysisAdd
BLAST
Topological domaini29 – 462434ExtracellularSequence analysisAdd
BLAST
Transmembranei463 – 48321HelicalSequence analysisAdd
BLAST
Topological domaini484 – 49512CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi399 – 3991C → S: Abolishes ecto-ATPase activity, accumulates intracellularly. 1 Publication
Mutagenesisi443 – 4431N → D: 7% of wild-type ATPase activity, accumulates intracellularly. 1 Publication

Organism-specific databases

PharmGKBiPA27799.

Chemistry

ChEMBLiCHEMBL5049.
GuidetoPHARMACOLOGYi2889.

Polymorphism and mutation databases

BioMutaiENTPD2.
DMDMi18203633.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Ectonucleoside triphosphate diphosphohydrolase 2PRO_0000209906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence analysis
Disulfide bondi75 ↔ 99By similarity
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi242 ↔ 284By similarity
Disulfide bondi265 ↔ 310By similarity
Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence analysis
Disulfide bondi323 ↔ 328By similarity
Disulfide bondi377 ↔ 399By similarity
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence analysis
Glycosylationi443 – 4431N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9Y5L3.
MaxQBiQ9Y5L3.
PaxDbiQ9Y5L3.
PeptideAtlasiQ9Y5L3.
PRIDEiQ9Y5L3.

PTM databases

iPTMnetiQ9Y5L3.

Expressioni

Tissue specificityi

Brain, placenta, skeletal muscle, kidney, pancreas, heart, ovary, testis, colon, small intestine, prostate and pancreas. No expression in adult thymus, spleen, lung, liver and peripheral blood leukocytes.

Gene expression databases

BgeeiQ9Y5L3.
CleanExiHS_ENTPD2.
GenevisibleiQ9Y5L3. HS.

Organism-specific databases

HPAiHPA017676.

Interactioni

Protein-protein interaction databases

BioGridi107392. 1 interaction.
IntActiQ9Y5L3. 1 interaction.
STRINGi9606.ENSP00000347213.

Chemistry

BindingDBiQ9Y5L3.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5L3.
SMRiQ9Y5L3. Positions 36-461.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the GDA1/CD39 NTPase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1386. Eukaryota.
COG5371. LUCA.
GeneTreeiENSGT00550000074435.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiQ9Y5L3.
KOiK01509.
OMAiSPCTMAQ.
OrthoDBiEOG754HPX.
PhylomeDBiQ9Y5L3.
TreeFamiTF332859.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q9Y5L3-1) [UniParc]FASTAAdd to basket

Also known as: alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGKVRSLLP PLLLAAAGLA GLLLLCVPTR DVREPPALKY GIVLDAGSSH
60 70 80 90 100
TSMFIYKWPA DKENDTGIVG QHSSCDVPGG GISSYADNPS GASQSLVGCL
110 120 130 140 150
EQALQDVPKE RHAGTPLYLG ATAGMRLLNL TNPEASTSVL MAVTHTLTQY
160 170 180 190 200
PFDFRGARIL SGQEEGVFGW VTANYLLENF IKYGWVGRWF RPRKGTLGAM
210 220 230 240 250
DLGGASTQIT FETTSPAEDR ASEVQLHLYG QHYRVYTHSF LCYGRDQVLQ
260 270 280 290 300
RLLASALQTH GFHPCWPRGF STQVLLGDVY QSPCTMAQRP QNFNSSARVS
310 320 330 340 350
LSGSSDPHLC RDLVSGLFSF SSCPFSRCSF NGVFQPPVAG NFVAFSAFFY
360 370 380 390 400
TVDFLRTSMG LPVATLQQLE AAAVNVCNQT WAQLQARVPG QRARLADYCA
410 420 430 440 450
GAMFVQQLLS RGYGFDERAF GGVIFQKKAA DTAVGWALGY MLNLTNLIPA
460 470 480 490
DPPGLRKGTD FSSWVVLLLL FASALLAALV LLLRQVHSAK LPSTI
Length:495
Mass (Da):53,665
Last modified:November 1, 1999 - v1
Checksum:i3BDBA114A679B422
GO
Isoform Short (identifier: Q9Y5L3-2) [UniParc]FASTAAdd to basket

Also known as: beta

The sequence of this isoform differs from the canonical sequence as follows:
     383-405: Missing.

Note: Catalytically inactive.
Show »
Length:472
Mass (Da):51,162
Checksum:i72F7EF732D7E2835
GO
Isoform gamma (identifier: Q9Y5L3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     383-405: Missing.
     406-428: Missing.

Note: Catalytically inactive.
Show »
Length:449
Mass (Da):48,535
Checksum:i27AD75755F92FC13
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031A → V.
Corresponds to variant rs34618694 [ dbSNP | Ensembl ].
VAR_050307

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei383 – 40523Missing in isoform Short and isoform gamma. 1 PublicationVSP_003610Add
BLAST
Alternative sequencei406 – 42823Missing in isoform gamma. CuratedVSP_053548Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91510 mRNA. Translation: AAB81013.1.
AF144748 mRNA. Translation: AAD40239.1.
EF495152 mRNA. Translation: ABP58644.1.
AL807752 Genomic DNA. Translation: CAI12777.1.
CH471090 Genomic DNA. Translation: EAW88336.1.
CH471090 Genomic DNA. Translation: EAW88337.1.
BC035738 mRNA. Translation: AAH35738.1.
CCDSiCCDS7025.1. [Q9Y5L3-2]
CCDS7026.1. [Q9Y5L3-1]
RefSeqiNP_001237.1. NM_001246.3. [Q9Y5L3-2]
NP_982293.1. NM_203468.2. [Q9Y5L3-1]
UniGeneiHs.123036.

Genome annotation databases

EnsembliENST00000312665; ENSP00000312494; ENSG00000054179. [Q9Y5L3-2]
ENST00000355097; ENSP00000347213; ENSG00000054179. [Q9Y5L3-1]
GeneIDi954.
KEGGihsa:954.
UCSCiuc004ckw.3. human. [Q9Y5L3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U91510 mRNA. Translation: AAB81013.1.
AF144748 mRNA. Translation: AAD40239.1.
EF495152 mRNA. Translation: ABP58644.1.
AL807752 Genomic DNA. Translation: CAI12777.1.
CH471090 Genomic DNA. Translation: EAW88336.1.
CH471090 Genomic DNA. Translation: EAW88337.1.
BC035738 mRNA. Translation: AAH35738.1.
CCDSiCCDS7025.1. [Q9Y5L3-2]
CCDS7026.1. [Q9Y5L3-1]
RefSeqiNP_001237.1. NM_001246.3. [Q9Y5L3-2]
NP_982293.1. NM_203468.2. [Q9Y5L3-1]
UniGeneiHs.123036.

3D structure databases

ProteinModelPortaliQ9Y5L3.
SMRiQ9Y5L3. Positions 36-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107392. 1 interaction.
IntActiQ9Y5L3. 1 interaction.
STRINGi9606.ENSP00000347213.

Chemistry

BindingDBiQ9Y5L3.
ChEMBLiCHEMBL5049.
GuidetoPHARMACOLOGYi2889.

PTM databases

iPTMnetiQ9Y5L3.

Polymorphism and mutation databases

BioMutaiENTPD2.
DMDMi18203633.

Proteomic databases

EPDiQ9Y5L3.
MaxQBiQ9Y5L3.
PaxDbiQ9Y5L3.
PeptideAtlasiQ9Y5L3.
PRIDEiQ9Y5L3.

Protocols and materials databases

DNASUi954.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312665; ENSP00000312494; ENSG00000054179. [Q9Y5L3-2]
ENST00000355097; ENSP00000347213; ENSG00000054179. [Q9Y5L3-1]
GeneIDi954.
KEGGihsa:954.
UCSCiuc004ckw.3. human. [Q9Y5L3-1]

Organism-specific databases

CTDi954.
GeneCardsiENTPD2.
HGNCiHGNC:3364. ENTPD2.
HPAiHPA017676.
MIMi602012. gene.
neXtProtiNX_Q9Y5L3.
PharmGKBiPA27799.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1386. Eukaryota.
COG5371. LUCA.
GeneTreeiENSGT00550000074435.
HOGENOMiHOG000059572.
HOVERGENiHBG018982.
InParanoidiQ9Y5L3.
KOiK01509.
OMAiSPCTMAQ.
OrthoDBiEOG754HPX.
PhylomeDBiQ9Y5L3.
TreeFamiTF332859.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000054179-MONOMER.
BRENDAi3.6.1.5. 2681.

Miscellaneous databases

ChiTaRSiENTPD2. human.
GeneWikiiENTPD2.
GenomeRNAii954.
PROiQ9Y5L3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5L3.
CleanExiHS_ENTPD2.
GenevisibleiQ9Y5L3. HS.

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

« Hide 'large scale' publications
  1. "Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes."
    Chadwick B.P., Frischauf A.-M.
    Mamm. Genome 8:668-672(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    Tissue: Keratinocyte.
  2. "Functional expression of a cDNA encoding a human ecto-ATPase."
    Mateo J., Harden T.K., Boyer J.L.
    Br. J. Pharmacol. 128:396-402(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), CATALYTIC ACTIVITY, COFACTOR, CHARACTERIZATION.
  3. "Either the carboxyl- or the amino-terminal region of the human ecto-ATPase (E-NTPDase 2) confers detergent and temperature sensitivity to the chicken ecto-ATP-diphosphohydrolase (E-NTPDase 8)."
    Mukasa T., Lee Y., Knowles A.F.
    Biochemistry 44:11160-11170(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    Tissue: Brain.
  7. "Requirement of Cys399 for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme."
    Mateo J., Kreda S., Henry C.E., Harden T.K., Boyer J.L.
    J. Biol. Chem. 278:39960-39968(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, MUTAGENESIS OF CYS-399 AND ASN-443, GLYCOSYLATION AT ASN-443.

Entry informationi

Entry nameiENTP2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5L3
Secondary accession number(s): O15464, Q5SPY6, Q5SPY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.