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E0D877

- APY_AEDAL

UniProt

E0D877 - APY_AEDAL

Protein

Apyrase

Gene
N/A
Organism
Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 22 (01 Oct 2014)
      Sequence version 1 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. May reduce probing time by facilitating the speed of locating blood. Platelet aggregation was inhibited by 6% when 0.4 µM recombinant apyrase was added and by 9.5% when the concentration of recombinant apyrase was 0.8 µM.1 Publication

    Catalytic activityi

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

    Cofactori

    Divalent metal cations.By similarity

    Kineticsi

    1. KM=11.6 µM for the recombinant enzyme1 Publication

    Vmax=1.02 nmol/sec/µg enzyme toward ATP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi48 – 481Divalent metal cation 1By similarity
    Metal bindingi50 – 501Divalent metal cation 1By similarity
    Metal bindingi99 – 991Divalent metal cation 1By similarity
    Metal bindingi99 – 991Divalent metal cation 2By similarity
    Metal bindingi131 – 1311Divalent metal cation 2By similarity
    Sitei132 – 1321Transition state stabilizerBy similarity
    Sitei135 – 1351Transition state stabilizerBy similarity
    Metal bindingi234 – 2341Divalent metal cation 2By similarity
    Metal bindingi258 – 2581Divalent metal cation 2By similarity
    Binding sitei425 – 4251SubstrateBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. hydrolase activity, acting on ester bonds Source: InterPro
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. nucleotide catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apyrase1 Publication (EC:3.6.1.51 Publication)
    Alternative name(s):
    ATP-diphosphataseBy similarity
    Short name:
    ADPaseBy similarity
    ATP-diphosphohydrolaseBy similarity
    Adenosine diphosphataseBy similarity1 Publication
    Allergen: Aed al 11 Publication
    OrganismiAedes albopictus (Asian tiger mosquito) (Stegomyia albopicta)
    Taxonomic identifieri7160 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeCulicinaeAediniAedesStegomyia

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Allergenic propertiesi

    Causes an allergic reaction in human.1 Publication

    Keywords - Diseasei

    Allergen

    Protein family/group databases

    Allergomei1345. Aed al 1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25251 PublicationAdd
    BLAST
    Chaini26 – 564539Apyrase1 PublicationPRO_5000623950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi391 – 3911N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Tissue specificityi

    Salivary gland specific.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliE0D877.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni509 – 5157Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the 5'-nucleotidase family.Sequence Analysis

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    3.90.780.10. 1 hit.
    InterProiIPR008334. 5'-Nucleotdase_C.
    IPR006146. 5'-Nucleotdase_CS.
    IPR006179. 5_nucleotidase/apyrase.
    IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view]
    PANTHERiPTHR11575. PTHR11575. 1 hit.
    PfamiPF02872. 5_nucleotid_C. 1 hit.
    PF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR01607. APYRASEFAMLY.
    SUPFAMiSSF55816. SSF55816. 1 hit.
    SSF56300. SSF56300. 1 hit.
    PROSITEiPS00785. 5_NUCLEOTIDASE_1. 1 hit.
    PS00786. 5_NUCLEOTIDASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    E0D877-1 [UniParc]FASTAAdd to Basket

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    MAGKPGIQLF VIFLLLSSFA AVVWAMDNMP ADKDVSKLFP LTLIHINDLH    50
    ARFDETNMKS NACTAKDQCI AGIARVYQKI QDLLKEYKSK NAIYLNAGDN 100
    FQGTLWYNLL RWQVTADFIT KLKPTAMTLG NHEFDHTPKG LAPYLAELDK 150
    AGIPTLVANL VMNDDPDLKS SKIQKSIKVT VGGKTIGIIG VLYDKTHEIA 200
    QTGKVTLSNA VETVKREAAA LKKDKVDIIV VLSHCSYDED KKIAKEAGQD 250
    IDVIVGAHSH SFLYSKESNK PYDQKDKIEG PYPTIVESNN KRKIPIVQAK 300
    SFGKYVGRLT LYFDNEGEVK HWEGYPEFID NKVKQDPKIL EALIPWRKKV 350
    QEIGSTKVGE TTIELDRDSC RDKECTLGVL YADAFADHYT NSSFRPFAII 400
    QAGNFRNPIK VGKITNGDII EAAPFGSTAD LIRLKGDNLW AVAEHSLALD 450
    DENRTNCLQV SGLRIVIDPS KSVGSRVVKI DVMDNRNPKS EDLKPLDRNA 500
    EYFIALPSYL ADGKDGFSAM KEATARWTGP LDSDVFKSYV EKIKKVDKLK 550
    LDRVIVCKAG SPCT 564
    Length:564
    Mass (Da):62,751
    Last modified:November 2, 2010 - v1
    Checksum:i15B9F0F2D3BD0825
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141L → I in AAV90659. (PubMed:17244540)Curated
    Sequence conflicti25 – 262AM → TT in AAV90659. (PubMed:17244540)Curated
    Sequence conflicti26 – 261M → T AA sequence (PubMed:17244540)Curated
    Sequence conflicti438 – 4381N → S in AAV90659. (PubMed:17244540)Curated
    Sequence conflicti447 – 4471L → F in AAV90659. (PubMed:17244540)Curated
    Sequence conflicti472 – 4732SV → KI in AAV90659. (PubMed:17244540)Curated
    Sequence conflicti498 – 4981R → K in AAV90659. (PubMed:17244540)Curated
    Sequence conflicti522 – 5221E → K in AAV90659. (PubMed:17244540)Curated
    Sequence conflicti551 – 5522LD → WG in AAV90659. (PubMed:17244540)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB576780 mRNA. Translation: BAJ14796.1.
    AY826087 mRNA. Translation: AAV90659.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB576780 mRNA. Translation: BAJ14796.1 .
    AY826087 mRNA. Translation: AAV90659.1 .

    3D structure databases

    ProteinModelPortali E0D877.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 1345. Aed al 1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    3.90.780.10. 1 hit.
    InterProi IPR008334. 5'-Nucleotdase_C.
    IPR006146. 5'-Nucleotdase_CS.
    IPR006179. 5_nucleotidase/apyrase.
    IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view ]
    PANTHERi PTHR11575. PTHR11575. 1 hit.
    Pfami PF02872. 5_nucleotid_C. 1 hit.
    PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR01607. APYRASEFAMLY.
    SUPFAMi SSF55816. SSF55816. 1 hit.
    SSF56300. SSF56300. 1 hit.
    PROSITEi PS00785. 5_NUCLEOTIDASE_1. 1 hit.
    PS00786. 5_NUCLEOTIDASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and characterization of salivary apyrase from Aedes albopictus."
      Dong F., Fu Y., Li X., Jiang J., Sun J., Cheng X.
      Parasitol. Res. 110:931-937(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Salivary glandImported.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-45, TISSUE SPECIFICITY, ALLERGEN.
      Tissue: Salivary glandImported.

    Entry informationi

    Entry nameiAPY_AEDAL
    AccessioniPrimary (citable) accession number: E0D877
    Secondary accession number(s): Q5MIX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 22 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3