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P80595

- APY_SOLTU

UniProt

P80595 - APY_SOLTU

Protein

Apyrase

Gene

RROP1

Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates.

    Catalytic activityi

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

    Cofactori

    Calcium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei170 – 1701Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 5811ATP-bindingCuratedAdd
    BLAST
    Nucleotide bindingi194 – 20411ATP-bindingCuratedAdd
    BLAST

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16862.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apyrase (EC:3.6.1.5)
    Alternative name(s):
    ATP-diphosphatase
    ATP-diphosphohydrolase
    Adenosine diphosphatase
    Short name:
    ADPase
    Gene namesi
    Name:RROP1
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: 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 – 454454ApyrasePRO_0000019904Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi262 – 2621N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP80595.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77CytoplasmicSequence Analysis
    Topological domaini29 – 454426ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi324 – 3296Poly-Gly

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    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]

    Sequencei

    Sequence statusi: Complete.

    P80595-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLNQNSHFIF IILAIFLVLP LSLLSKNVNA QIPLRRHLLS HESEHYAVIF    50
    DAGSTGSRVH VFRFDEKLGL LPIGNNIEYF MATEPGLSSY AEDPKAAANS 100
    LEPLLDGAEG VVPQELQSET PLELGATAGL RMLKGDAAEK ILQAVRNLVK 150
    NQSTFHSKDQ WVTILDGTQE GSYMWAAINY LLGNLGKDYK STTATIDLGG 200
    GSVQMAYAIS NEQFAKAPQN EDGEPYVQQK HLMSKDYNLY VHSYLNYGQL 250
    AGRAEIFKAS RNESNPCALE GCDGYYSYGG VDYKVKAPKK GSSWKRCRRL 300
    TRHALKINAK CNIEECTFNG VWNGGGGDGQ KNIHASSFFY DIGAQVGIVD 350
    TKFPSALAKP IQYLNAAKVA CQTNVADIKS IFPKTQDRNI PYLCMDLIYE 400
    YTLLVDGFGL NPHKEITVIH DVQYKNYLVG AAWPLGCAID LVSSTTNKIR 450
    VASS 454
    Length:454
    Mass (Da):50,041
    Last modified:November 1, 1997 - v2
    Checksum:i9D9EFE431DA2F52F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58597 mRNA. Translation: AAB02720.1.
    PIRiJC4616.
    UniGeneiStu.216.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58597 mRNA. Translation: AAB02720.1 .
    PIRi JC4616.
    UniGenei Stu.216.

    3D structure databases

    ProteinModelPortali P80595.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16862.

    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. "Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase) from potato tubers (Solanum tuberosum)."
      Handa M., Guidotti G.
      Biochem. Biophys. Res. Commun. 218:916-923(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 59-160; 236-253 AND 332-345.
      Tissue: Tuber.
    2. "Partial purification and immunohistochemical localization of ATP diphosphohydrolase from Schistosoma mansoni. Immunological cross-reactivities with potato apyrase and Toxoplasma gondii nucleoside triphosphate hydrolase."
      Vasconcelos E.G., Ferreira S.T., de Carvalho T.M.U., de Souza W., Kettlun A.M., Mancilla M., Valenzuela M.A., Verjovski-Almeida S.
      J. Biol. Chem. 271:22139-22145(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 42-54; 68-95 AND 236-253.
      Strain: cv. Desiree.

    Entry informationi

    Entry nameiAPY_SOLTU
    AccessioniPrimary (citable) accession number: P80595
    Secondary accession number(s): Q43164
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 66 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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