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O35795

- ENTP2_RAT

UniProt

O35795 - ENTP2_RAT

Protein

Ectonucleoside triphosphate diphosphohydrolase 2

Gene

Entpd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent.

    Cofactori

    Ca2+ or Mg2+.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei165 – 1651Proton acceptor1 Publication

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydrolase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Nucleotide-binding

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi69266. Entpd2.

    Subcellular locationi

    Isoform 1 : Cell membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 495495Ectonucleoside triphosphate diphosphohydrolase 2PRO_0000209908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi75 ↔ 991 Publication
    Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi242 ↔ 2841 Publication
    Disulfide bondi265 ↔ 3101 Publication
    Glycosylationi294 – 2941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi323 ↔ 3281 Publication
    Disulfide bondi377 ↔ 3991 Publication
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO35795.
    PRIDEiO35795.

    Expressioni

    Tissue specificityi

    Expressed in brain, heart, vas deferens, kidney, skeletal muscle, thymus, lung and spleen. Weak expression in liver.

    Inductioni

    By FSH in Sertoli cells but not in peritubular cells; by cAMP in both type of cells.

    Gene expression databases

    GenevestigatoriO35795.

    Interactioni

    Structurei

    Secondary structure

    1
    495
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 469
    Beta strandi51 – 599
    Helixi60 – 623
    Beta strandi70 – 767
    Beta strandi78 – 803
    Helixi82 – 854
    Helixi90 – 956
    Helixi97 – 10610
    Helixi109 – 1146
    Beta strandi116 – 1216
    Helixi123 – 1319
    Helixi133 – 14715
    Beta strandi150 – 15910
    Helixi162 – 17615
    Turni177 – 1804
    Beta strandi198 – 2025
    Beta strandi204 – 2129
    Helixi220 – 2223
    Beta strandi223 – 2286
    Beta strandi231 – 24111
    Helixi245 – 25915
    Beta strandi261 – 2633
    Beta strandi271 – 2755
    Helixi276 – 2805
    Turni283 – 2875
    Beta strandi298 – 3036
    Helixi307 – 3159
    Beta strandi324 – 3307
    Beta strandi342 – 3465
    Helixi347 – 35711
    Helixi366 – 37813
    Helixi381 – 3855
    Helixi395 – 3973
    Helixi398 – 41013
    Turni411 – 4133
    Helixi417 – 4204
    Beta strandi423 – 4253
    Beta strandi427 – 4293
    Helixi437 – 4448
    Helixi453 – 4586

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CJ1X-ray1.70A29-461[»]
    3CJ7X-ray1.80A29-461[»]
    3CJ9X-ray1.80A29-461[»]
    3CJAX-ray2.10A29-461[»]
    4BQZX-ray2.05A28-462[»]
    4BR0X-ray2.05A28-462[»]
    4BR2X-ray2.00A28-462[»]
    4CD1X-ray2.00A28-462[»]
    4CD3X-ray2.19A28-461[»]
    ProteinModelPortaliO35795.
    SMRiO35795. Positions 36-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO35795.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44CytoplasmicSequence Analysis
    Topological domaini26 – 462437ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini484 – 49512CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei463 – 48321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5371.
    HOGENOMiHOG000059572.
    HOVERGENiHBG018982.
    KOiK01509.
    PhylomeDBiO35795.

    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: O35795-1) [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

    MAGKLVSLVP PLLLAAAGLT GLLLLCVPTQ DVREPPALKY GIVLDAGSSH    50
    TSMFVYKWPA DKENDTGIVG QHSSCDVQGG GISSYANDPS KAGQSLVRCL 100
    EQALRDVPRD RHASTPLYLG ATAGMRPFNL TSPEATARVL EAVTQTLTQY 150
    PFDFRGARIL SGQDEGVFGW VTANYLLENF IKYGWVGRWI RPRKGTLGAM 200
    DLGGASTQIT FETTSPSEDP GNEVHLRLYG QHYRVYTHSF LCYGRDQILL 250
    RLLASALQIH RFHPCWPKGY STQVLLQEVY QSPCTMGQRP RAFNGSAIVS 300
    LSGTSNATLC RDLVSRLFNI SSCPFSQCSF NGVFQPPVAG NFIAFSAFYY 350
    TVDFLTTVMG LPVGTLKQLE EATEITCNQT WTELQARVPG QKTRLADYCA 400
    VAMFIHQLLS RGYHFDERSF REVVFQKKAA DTAVGWALGY MLNLTNLIPA 450
    DLPGLRKGTH FSSWVALLLL FTVLILAALV LLLRQVRSAK SPGAL 495
    Length:495
    Mass (Da):54,390
    Last modified:January 1, 1998 - v1
    Checksum:i237B999F1BEB8E00
    GO
    Isoform 2 (identifier: O35795-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         486-495: VRSAKSPGAL → DVRSQPVTQGEVHSEWDFCSDLQGPGNFLSGPLERQAPEPTGWESVPCLLVKTFVIKDFS

    Show »
    Length:545
    Mass (Da):60,067
    Checksum:i9802C097CA40E93C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201T → A in AAF87740. (PubMed:11229804)Curated
    Sequence conflicti127 – 1282PF → LL in AAF87740. (PubMed:11229804)Curated
    Sequence conflicti339 – 3391A → T in AAF87740. (PubMed:11229804)Curated
    Sequence conflicti444 – 4441L → F in AAF87740. (PubMed:11229804)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei486 – 49510VRSAKSPGAL → DVRSQPVTQGEVHSEWDFCS DLQGPGNFLSGPLERQAPEP TGWESVPCLLVKTFVIKDFS in isoform 2. 1 PublicationVSP_003613

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11835 mRNA. Translation: CAA72533.1.
    AF276940 mRNA. Translation: AAF87740.1.
    AF129103 mRNA. Translation: AAD42303.1.
    RefSeqiNP_742027.1. NM_172030.1.
    UniGeneiRn.8276.

    Genome annotation databases

    GeneIDi64467.
    KEGGirno:64467.
    UCSCiRGD:69266. rat. [O35795-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11835 mRNA. Translation: CAA72533.1 .
    AF276940 mRNA. Translation: AAF87740.1 .
    AF129103 mRNA. Translation: AAD42303.1 .
    RefSeqi NP_742027.1. NM_172030.1.
    UniGenei Rn.8276.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CJ1 X-ray 1.70 A 29-461 [» ]
    3CJ7 X-ray 1.80 A 29-461 [» ]
    3CJ9 X-ray 1.80 A 29-461 [» ]
    3CJA X-ray 2.10 A 29-461 [» ]
    4BQZ X-ray 2.05 A 28-462 [» ]
    4BR0 X-ray 2.05 A 28-462 [» ]
    4BR2 X-ray 2.00 A 28-462 [» ]
    4CD1 X-ray 2.00 A 28-462 [» ]
    4CD3 X-ray 2.19 A 28-461 [» ]
    ProteinModelPortali O35795.
    SMRi O35795. Positions 36-461.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi O35795.
    ChEMBLi CHEMBL3300.

    Proteomic databases

    PaxDbi O35795.
    PRIDEi O35795.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64467.
    KEGGi rno:64467.
    UCSCi RGD:69266. rat. [O35795-1 ]

    Organism-specific databases

    CTDi 954.
    RGDi 69266. Entpd2.

    Phylogenomic databases

    eggNOGi COG5371.
    HOGENOMi HOG000059572.
    HOVERGENi HBG018982.
    KOi K01509.
    PhylomeDBi O35795.

    Miscellaneous databases

    EvolutionaryTracei O35795.
    NextBioi 613232.
    PROi O35795.

    Gene expression databases

    Genevestigatori O35795.

    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. "An ecto-ATPase and an ecto-ATP diphosphohydrolase are expressed in rat brain."
      Kegel B., Braun N., Heine P., Maliszewski C.R., Zimmermann H.
      Neuropharmacology 36:1189-1200(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "Ecto-ATPase mRNA is regulated by FSH in Sertoli cells."
      Lu Q., Porter L.D., Cui X., Sanborn B.M.
      J. Androl. 22:289-301(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: Sprague-Dawley.
      Tissue: Sertoli cell.
    3. "Evidence for alternative splicing of ecto-ATPase associated with termination of purinergic transmission."
      Vlajkovic S.M., Housley G.D., Greenwood D., Thorne P.R.
      Brain Res. Mol. Brain Res. 73:85-92(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 379-495 (ISOFORM 2).
      Strain: Wistar.
      Tissue: Cochlea.
    4. "Structural insight into signal conversion and inactivation by NTPDase2 in purinergic signaling."
      Zebisch M., Strater N.
      Proc. Natl. Acad. Sci. U.S.A. 105:6882-6887(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-461 ALONE AND IN COMPLEX WITH ATP ANALOGS AND CALCIUM, ACTIVE SITE, DISULFIDE BONDS.

    Entry informationi

    Entry nameiENTP2_RAT
    AccessioniPrimary (citable) accession number: O35795
    Secondary accession number(s): Q9JHY5, Q9WVE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 103 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3