Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9MYU4

- ENTP1_PIG

UniProt

Q9MYU4 - ENTP1_PIG

Protein

Ectonucleoside triphosphate diphosphohydrolase 1

Gene

ENTPD1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

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

    Catalytic activityi

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

    Cofactori

    Ca2+ or Mg2+.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei174 – 1741Proton acceptorBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydrolase activity Source: UniProtKB-KW
    3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Magnesium, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ectonucleoside triphosphate diphosphohydrolase 1 (EC:3.6.1.5)
    Short name:
    NTPDase 1
    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:
    Gene namesi
    Name:ENTPD1
    Synonyms:CD39
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 510510Ectonucleoside triphosphate diphosphohydrolase 1PRO_0000019905Add
    BLAST
    Chaini1 – 201201Ectonucleoside triphosphate diphosphohydrolase 1 27 kDa subunitPRO_0000019906Add
    BLAST
    Chaini202 – 510309Ectonucleoside triphosphate diphosphohydrolase 1 54 kDa subunitPRO_0000019907Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi84 ↔ 108By similarity
    Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi255 ↔ 300By similarity
    Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi281 ↔ 324By similarity
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi337 ↔ 342By similarity
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi390 ↔ 413By similarity
    Glycosylationi457 – 4571N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

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

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.By similarity

    Protein-protein interaction databases

    STRINGi9823.ENSSSCP00000011184.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9MYU4.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini38 – 477440ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini499 – 51012CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei17 – 3721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei478 – 49821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5371.
    HOGENOMiHOG000059572.
    HOVERGENiHBG018982.
    KOiK01510.

    Family and domain databases

    InterProiIPR000407. GDA1_CD39_NTPase.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    [Graphical view]
    PANTHERiPTHR11782. PTHR11782. 1 hit.
    PfamiPF01150. GDA1_CD39. 1 hit.
    [Graphical view]
    SUPFAMiSSF56327. SSF56327. 1 hit.
    PROSITEiPS01238. GDA1_CD39_NTPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9MYU4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEDRRESELK TFCSKNILVI LGFSSIIAVI ALLALGLTQN KPLPENVKFG    50
    IVLDAGSSHT SLYIYKWPAE KENDTGVVSQ VEECKLKGPG ISEFAKKLGE 100
    IDIYLEACME RARTVVPKSQ HAETPVYLGA TAGMRLLRMK NENLASKILS 150
    TVAESITRYP FDFQGARIIT GQEEGAYGWI TINYLLDKFI QKSGWFNLKP 200
    RKGDTQETYG ALDLGGASTQ ITFVPQNQVL ESPENTLHFR LYGKNYSVYT 250
    HSFLCYGKDQ ALLQKLTKDL KNTNGTIHEP CFHSGYQRRM NVSHLYEAPC 300
    TRRFLTSLPF PELEIQGTGD FQKCQQSIRP LFNTSYCPYS RCSFDGVFLP 350
    LPQGDFAAFS AFYYVMGFLN LTSEEGSFQS KVTSTLEAFC SRPWAELQMY 400
    FGDVKEKYLS EYCFSGTYIL TLLLSGYHFT AETWKNIHFM GKVQSTSVGW 450
    TLGYMLNLTN MIPSEEPSST RLSHSTYVFL MVLFSLILVI VVIIGLFVCH 500
    RPSYFWKDMV 510
    Length:510
    Mass (Da):57,757
    Last modified:October 1, 2000 - v1
    Checksum:i82F86869040D7735
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti203 – 2031G → S AA sequence (PubMed:8955160)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133746 mRNA. Translation: CAB95871.1.
    RefSeqiNP_999318.1. NM_214153.1.
    UniGeneiSsc.52334.

    Genome annotation databases

    GeneIDi397298.
    KEGGissc:397298.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ133746 mRNA. Translation: CAB95871.1 .
    RefSeqi NP_999318.1. NM_214153.1.
    UniGenei Ssc.52334.

    3D structure databases

    ProteinModelPortali Q9MYU4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9823.ENSSSCP00000011184.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397298.
    KEGGi ssc:397298.

    Organism-specific databases

    CTDi 953.

    Phylogenomic databases

    eggNOGi COG5371.
    HOGENOMi HOG000059572.
    HOVERGENi HBG018982.
    KOi K01510.

    Family and domain databases

    InterProi IPR000407. GDA1_CD39_NTPase.
    IPR015955. Lactate_DH/Glyco_Ohase_4_C.
    [Graphical view ]
    PANTHERi PTHR11782. PTHR11782. 1 hit.
    Pfami PF01150. GDA1_CD39. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56327. SSF56327. 1 hit.
    PROSITEi PS01238. GDA1_CD39_NTPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 202-220.
      Tissue: Pancreas.

    Entry informationi

    Entry nameiENTP1_PIG
    AccessioniPrimary (citable) accession number: Q9MYU4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 88 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3