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O75355

- ENTP3_HUMAN

UniProt

O75355 - ENTP3_HUMAN

Protein

Ectonucleoside triphosphate diphosphohydrolase 3

Gene

ENTPD3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (19 Sep 2006)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Ca2+ or Mg2+.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei182 – 1821Proton acceptorBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleoside-diphosphatase activity Source: Ensembl
    3. nucleoside-triphosphatase activity Source: Ensembl

    GO - Biological processi

    1. nucleoside diphosphate catabolic process Source: Ensembl
    2. nucleoside triphosphate catabolic process Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleoside triphosphate diphosphohydrolase 3 (EC:3.6.1.5)
    Short name:
    NTPDase 3
    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 namesi
    Name:ENTPD3
    Synonyms:CD39L3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3365. ENTPD3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671R → G: Increase of activity. 1 Publication
    Mutagenesisi143 – 1431R → A: Loss of activity. 1 Publication
    Mutagenesisi143 – 1431R → K: Increase of activity. 1 Publication
    Mutagenesisi146 – 1461R → N: No effect. 1 Publication
    Mutagenesisi146 – 1461R → P: Increase of ATPase activity, decrease of ADPase activity. 1 Publication
    Mutagenesisi146 – 1461R → T: Increase of activity. 1 Publication
    Mutagenesisi182 – 1821E → D: Complete loss of activity. 1 Publication
    Mutagenesisi182 – 1821E → Q: Complete loss of activity. 1 Publication
    Mutagenesisi187 – 1871W → A: Complete loss of activity. 1 Publication
    Mutagenesisi191 – 1911N → A: Loss of ATPase activity, increase of ADPase activity. 1 Publication
    Mutagenesisi219 – 2191D → E: Increase of activity. 1 Publication
    Mutagenesisi224 – 2241S → A: Complete loss of activity. 1 Publication
    Mutagenesisi226 – 2261Q → A: Loss of activity. 1 Publication
    Mutagenesisi459 – 4591W → A: Increase of activity, especially the ATP hydrolysis. 1 Publication

    Organism-specific databases

    PharmGKBiPA27800.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 529529Ectonucleoside triphosphate diphosphohydrolase 3PRO_0000209910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi92 ↔ 1161 Publication
    Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi238 – 2381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi261 ↔ 3081 Publication
    Disulfide bondi289 ↔ 3341 Publication
    Disulfide bondi347 ↔ 3531 Publication
    Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi392 – 3921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi399 ↔ 4221 Publication
    Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi454 – 4541N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO75355.
    PRIDEiO75355.

    PTM databases

    PhosphoSiteiO75355.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiO75355.
    BgeeiO75355.
    CleanExiHS_ENTPD3.
    GenevestigatoriO75355.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000301825.

    Structurei

    3D structure databases

    ProteinModelPortaliO75355.
    SMRiO75355. Positions 55-469.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini44 – 485442ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini507 – 52923CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei23 – 4321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei486 – 50621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5371.
    HOGENOMiHOG000059572.
    HOVERGENiHBG018982.
    InParanoidiO75355.
    KOiK01510.
    OMAiIMQVSLY.
    OrthoDBiEOG754HPX.
    PhylomeDBiO75355.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75355-1) [UniParc]FASTAAdd to Basket

    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

    MFTVLTRQPC EQAGLKALYR TPTIIALVVL LVSIVVLVSI TVIQIHKQEV    50
    LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS 100
    SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE 150
    TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK 200
    NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY 250
    VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM 300
    GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ 350
    ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS 400
    QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK 450
    EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPVFVGT LAFFTAAALL 500
    CLAFLAYLCS ATRRKRHSEH AFDHAVDSD 529
    Length:529
    Mass (Da):59,105
    Last modified:September 19, 2006 - v2
    Checksum:i5043CF0202978B88
    GO
    Isoform 2 (identifier: O75355-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         452-529: VGNSSIAWSL...HAFDHAVDSD → E

    Note: No experimental confirmation available.

    Show »
    Length:452
    Mass (Da):50,762
    Checksum:i28E1A42977EA63DC
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti24 – 241I → V.1 Publication
    Corresponds to variant rs17852714 [ dbSNP | Ensembl ].
    VAR_070813
    Natural varianti264 – 2641R → Q.
    Corresponds to variant rs34266806 [ dbSNP | Ensembl ].
    VAR_061384
    Natural varianti440 – 4401E → D.
    Corresponds to variant rs4470483 [ dbSNP | Ensembl ].
    VAR_027541
    Natural varianti496 – 4961A → V.1 Publication
    Corresponds to variant rs1047855 [ dbSNP | Ensembl ].
    VAR_027542
    Natural varianti505 – 5051L → F.
    Corresponds to variant rs3733167 [ dbSNP | Ensembl ].
    VAR_027543

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei452 – 52978VGNSS…AVDSD → E in isoform 2. 1 PublicationVSP_054237Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2691.1. [O75355-1]
    RefSeqiNP_001239.2. NM_001248.3. [O75355-1]
    UniGeneiHs.441145.

    Genome annotation databases

    EnsembliENST00000301825; ENSP00000301825; ENSG00000168032. [O75355-1]
    ENST00000445129; ENSP00000404671; ENSG00000168032. [O75355-2]
    ENST00000456402; ENSP00000401565; ENSG00000168032. [O75355-1]
    GeneIDi956.
    KEGGihsa:956.
    UCSCiuc003ckd.4. human. [O75355-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2691.1. [O75355-1 ]
    RefSeqi NP_001239.2. NM_001248.3. [O75355-1 ]
    UniGenei Hs.441145.

    3D structure databases

    ProteinModelPortali O75355.
    SMRi O75355. Positions 55-469.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000301825.

    Chemistry

    BindingDBi O75355.
    ChEMBLi CHEMBL5897.

    PTM databases

    PhosphoSitei O75355.

    Proteomic databases

    PaxDbi O75355.
    PRIDEi O75355.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301825 ; ENSP00000301825 ; ENSG00000168032 . [O75355-1 ]
    ENST00000445129 ; ENSP00000404671 ; ENSG00000168032 . [O75355-2 ]
    ENST00000456402 ; ENSP00000401565 ; ENSG00000168032 . [O75355-1 ]
    GeneIDi 956.
    KEGGi hsa:956.
    UCSCi uc003ckd.4. human. [O75355-1 ]

    Organism-specific databases

    CTDi 956.
    GeneCardsi GC03P040403.
    HGNCi HGNC:3365. ENTPD3.
    MIMi 603161. gene.
    neXtProti NX_O75355.
    PharmGKBi PA27800.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5371.
    HOGENOMi HOG000059572.
    HOVERGENi HBG018982.
    InParanoidi O75355.
    KOi K01510.
    OMAi IMQVSLY.
    OrthoDBi EOG754HPX.
    PhylomeDBi O75355.
    TreeFami TF332859.

    Miscellaneous databases

    GeneWikii ENTPD3.
    GenomeRNAii 956.
    NextBioi 35518201.
    PROi O75355.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75355.
    Bgeei O75355.
    CleanExi HS_ENTPD3.
    Genevestigatori O75355.

    Family and domain databases

    InterProi IPR000407. GDA1_CD39_NTPase.
    [Graphical view ]
    PANTHERi PTHR11782. PTHR11782. 1 hit.
    Pfami PF01150. GDA1_CD39. 1 hit.
    [Graphical view ]
    PROSITEi PS01238. GDA1_CD39_NTPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiENTP3_HUMAN
    AccessioniPrimary (citable) accession number: O75355
    Secondary accession number(s): B2R8D0
    , G5E9N0, O60495, Q8N6K2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: September 19, 2006
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 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 3
      Human chromosome 3: 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

    External Data

    Dasty 3