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O75355 (ENTP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ectonucleoside triphosphate diphosphohydrolase 3

Short name=NTPDase 3
EC=3.6.1.5
Alternative name(s):
CD39 antigen-like 3
Ecto-ATP diphosphohydrolase 3
Short name=Ecto-ATPDase 3
Short name=Ecto-ATPase 3
Ecto-apyrase 3
HB6
Gene names
Name:ENTPD3
Synonyms:CD39L3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length529 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has a threefold preference for the hydrolysis of ATP over ADP.

Catalytic activity

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

Cofactor

Ca2+ or Mg2+.

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Tissue specificity

Expressed in adult brain, pancreas, spleen and prostate. Moderate or low expression is seen in most tissues. Not expressed in liver and peripheral blood leukocytes.

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75355-1)

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.
Isoform 2 (identifier: O75355-2)

The sequence of this isoform differs from the canonical sequence as follows:
     452-529: VGNSSIAWSL...HAFDHAVDSD → E
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 529529Ectonucleoside triphosphate diphosphohydrolase 3
PRO_0000209910

Regions

Topological domain1 – 2222Cytoplasmic Potential
Transmembrane23 – 4321Helical; Potential
Topological domain44 – 485442Extracellular Potential
Transmembrane486 – 50621Helical; Potential
Topological domain507 – 52923Cytoplasmic Potential

Sites

Active site1821Proton acceptor By similarity

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation1491N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation3811N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Disulfide bond92 ↔ 116 Ref.10
Disulfide bond261 ↔ 308 Ref.10
Disulfide bond289 ↔ 334 Ref.10
Disulfide bond347 ↔ 353 Ref.10
Disulfide bond399 ↔ 422 Ref.10

Natural variations

Alternative sequence452 – 52978VGNSS…AVDSD → E in isoform 2.
VSP_054237
Natural variant241I → V. Ref.7
Corresponds to variant rs17852714 [ dbSNP | Ensembl ].
VAR_070813
Natural variant2641R → Q.
Corresponds to variant rs34266806 [ dbSNP | Ensembl ].
VAR_061384
Natural variant4401E → D.
Corresponds to variant rs4470483 [ dbSNP | Ensembl ].
VAR_027541
Natural variant4961A → V. Ref.1
Corresponds to variant rs1047855 [ dbSNP | Ensembl ].
VAR_027542
Natural variant5051L → F.
Corresponds to variant rs3733167 [ dbSNP | Ensembl ].
VAR_027543

Experimental info

Mutagenesis671R → G: Increase of activity. Ref.9
Mutagenesis1431R → A: Loss of activity. Ref.9
Mutagenesis1431R → K: Increase of activity. Ref.9
Mutagenesis1461R → N: No effect. Ref.9
Mutagenesis1461R → P: Increase of ATPase activity, decrease of ADPase activity. Ref.9
Mutagenesis1461R → T: Increase of activity. Ref.9
Mutagenesis1821E → D: Complete loss of activity. Ref.9
Mutagenesis1821E → Q: Complete loss of activity. Ref.9
Mutagenesis1871W → A: Complete loss of activity. Ref.8
Mutagenesis1911N → A: Loss of ATPase activity, increase of ADPase activity. Ref.9
Mutagenesis2191D → E: Increase of activity. Ref.8
Mutagenesis2241S → A: Complete loss of activity. Ref.9
Mutagenesis2261Q → A: Loss of activity. Ref.9
Mutagenesis4591W → A: Increase of activity, especially the ATP hydrolysis. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 19, 2006. Version 2.
Checksum: 5043CF0202978B88

FASTA52959,105
        10         20         30         40         50         60 
MFTVLTRQPC EQAGLKALYR TPTIIALVVL LVSIVVLVSI TVIQIHKQEV LPPGLKYGIV 

        70         80         90        100        110        120 
LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV 

       130        140        150        160        170        180 
KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ 

       190        200        210        220        230        240 
EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS 

       250        260        270        280        290        300 
DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM 

       310        320        330        340        350        360 
GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ 

       370        380        390        400        410        420 
PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS 

       430        440        450        460        470        480 
YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL 

       490        500        510        520 
PIEPPVFVGT LAFFTAAALL CLAFLAYLCS ATRRKRHSEH AFDHAVDSD 

« Hide

Isoform 2 [UniParc].

Checksum: 28E1A42977EA63DC
Show »

FASTA45250,762

References

« Hide 'large scale' references
[1]"The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster."
Chadwick B.P., Frischauf A.-M.
Genomics 50:357-367(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-496.
Tissue: Keratinocyte.
[2]"Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases."
Smith T.M., Kirley T.L.
Biochim. Biophys. Acta 1386:65-78(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
Tissue: Brain.
[3]Smith T.M., Kirley T.L.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Esophagus.
[5]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 2), VARIANT VAL-24.
Tissue: Brain.
[8]"Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase."
Smith T.M., Lewis Carl S.A., Kirley T.L.
Biochemistry 38:5849-5857(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-187; ASP-219 AND TRP-459.
[9]"Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions."
Yang F., Hicks-Berger C.A., Smith T.M., Kirley T.L.
Biochemistry 40:3943-3950(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-67; ARG-143; ARG-146; GLU-182; ASN-191; SER-224 AND GLN-226.
[10]"Characterization of disulfide bonds in human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): implications for NTPDase structural modeling."
Ivanenkov V.V., Meller J., Kirley T.L.
Biochemistry 44:8998-9012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039917 mRNA. Translation: AAC39884.1.
AF034840 mRNA. Translation: AAC09236.2.
AK313322 mRNA. Translation: BAG36127.1.
AC104186 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64600.1.
CH471055 Genomic DNA. Translation: EAW64601.1.
BC029869 mRNA. Translation: AAH29869.1.
CCDSCCDS2691.1.
RefSeqNP_001239.2. NM_001248.3. [O75355-1]
UniGeneHs.441145.

3D structure databases

ProteinModelPortalO75355.
SMRO75355. Positions 55-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000301825.

Chemistry

BindingDBO75355.
ChEMBLCHEMBL5897.

PTM databases

PhosphoSiteO75355.

Proteomic databases

PaxDbO75355.
PRIDEO75355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301825; ENSP00000301825; ENSG00000168032.
ENST00000445129; ENSP00000404671; ENSG00000168032.
ENST00000456402; ENSP00000401565; ENSG00000168032.
GeneID956.
KEGGhsa:956.
UCSCuc003ckd.4. human. [O75355-1]

Organism-specific databases

CTD956.
GeneCardsGC03P040403.
HGNCHGNC:3365. ENTPD3.
MIM603161. gene.
neXtProtNX_O75355.
PharmGKBPA27800.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5371.
HOGENOMHOG000059572.
HOVERGENHBG018982.
InParanoidO75355.
KOK01510.
OMAIMQVSLY.
OrthoDBEOG754HPX.
PhylomeDBO75355.
TreeFamTF332859.

Gene expression databases

ArrayExpressO75355.
BgeeO75355.
CleanExHS_ENTPD3.
GenevestigatorO75355.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERPTHR11782. PTHR11782. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiENTPD3.
GenomeRNAi956.
NextBio35518201.
PROO75355.
SOURCESearch...

Entry information

Entry nameENTP3_HUMAN
AccessionPrimary (citable) accession number: O75355
Secondary accession number(s): B2R8D0 expand/collapse secondary AC list , G5E9N0, O60495, Q8N6K2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: September 19, 2006
Last modified: July 9, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM