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F4JSH1

- APY7_ARATH

UniProt

F4JSH1 - APY7_ARATH

Protein

Probable apyrase 7

Gene

APY7

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates By similarity. Involved in the regulation of pollen and anther development.By similarity1 Publication

    Catalytic activityi

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

    Cofactori

    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei284 – 2841Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi147 – 15711ATP-bindingCuratedAdd
    BLAST
    Nucleotide bindingi309 – 31911ATP-bindingCuratedAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. anther dehiscence Source: TAIR
    2. pollen exine formation Source: TAIR

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable apyrase 7 (EC:3.6.1.5)
    Short name:
    AtAPY7
    Alternative name(s):
    ATP-diphosphatase
    ATP-diphosphohydrolase
    Adenosine diphosphatase
    Short name:
    ADPase
    NTPDase
    Nucleoside triphosphate diphosphohydrolase 7
    Gene namesi
    Name:APY7
    Ordered Locus Names:At4g19180
    ORF Names:T18B16.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G19180.

    Subcellular locationi

    Membrane By similarity; Multi-pass membrane protein By similarity

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Apy6 and dapy7 double mutant exhibits late anther dehiscence and low male fertility. Pollen grains of double mutant are largely deformed in shape and in most cases, the cell walls of the pollen grains are interconnected.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 740740Probable apyrase 7PRO_0000420345Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiF4JSH1.

    Expressioni

    Tissue specificityi

    Detected in mature pollen grains. Also expressed in more diverse tissues such as roots, leaves, stems, pistils and sepals. More particularly expressed in the vascular bundle.1 Publication

    Inductioni

    By wounding and drought stress.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT4G19180.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliF4JSH1.
    SMRiF4JSH1. Positions 144-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 113113CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini135 – 581447ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini603 – 740138CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei114 – 13421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei582 – 60221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi625 – 735111Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GDA1/CD39 NTPase family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5371.
    OMAiSKLVHNE.

    Family and domain databases

    InterProiIPR000407. GDA1_CD39_NTPase.
    [Graphical view]
    PANTHERiPTHR11782. PTHR11782. 1 hit.
    PfamiPF01150. GDA1_CD39. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    F4JSH1-1 [UniParc]FASTAAdd to Basket

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    MVFGRITELF TAASSRLPAG SQSSVPYMPT GSSPDVGTSV SDSISIGNGG    50
    RKNCLRHSAS LQDFSSYHGF DPEESILPRE AISWGQNGSS FSKEKGSVPN 100
    GTNPSTRRKL IRAVMIVMCL FLFAFLVYIV SMYIYTNWSR GASRYYVVFD 150
    CGSTGTRAYV YQASINYKKD SSLPIVMKSL TEGISRKSRG RAYDRMETEP 200
    GFDKLVNNRT GLKTAIKPLI QWAEKQIPKN AHRTTSLFVY ATAGVRRLRP 250
    ADSSWILGNV WSILAKSPFT CRREWVKIIS GTEEAYFGWT ALNYQTSMLG 300
    ALPKKATFGA LDLGGSSLQV TFENEERTHN ETNLNLRIGS VNHHLSAYSL 350
    AGYGLNDAFD RSVVHLLKKL PNVNKSDLIE GKLEMKHPCL NSGYNGQYIC 400
    SQCASSVQGG KKGKSGVSIK LVGAPNWGEC SALAKNAVNS SEWSNAKHGV 450
    DCDLQPCALP DGYPRPHGQF YAVSGFFVVY RFFNLSAEAS LDDVLEKGRE 500
    FCDKAWQVAR TSVSPQPFIE QYCFRAPYIV SLLREGLYIT DKQIIIGSGS 550
    ITWTLGVALL ESGKALSSTL GLKSYETLSM KINPIALISI LILSLLLLLC 600
    ALSRVSNCLP RFFRKSYLPL FRHNSTSASS VLNIPSPFRF QRWSPMSTGV 650
    KTPLSPTVRG SPRRPFSFGS SIQLMESSLY SSSSCVMHSC SSDSLGDIQY 700
    DSTGSFWSSP RRSQMRLQSR RSQSREDLSS SLADSHMLKM 740
    Length:740
    Mass (Da):81,683
    Last modified:June 28, 2011 - v1
    Checksum:i4B282DAFC67F4ED0
    GO

    Sequence cautioni

    The sequence CAA16707.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 2 genes: At4g19180 and At4g19185.
    The sequence CAB78920.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 2 genes: At4g19180 and At4g19185.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JF830012 mRNA. Translation: AEJ38088.1.
    JQ965809 mRNA. Translation: AFL69929.1.
    AL021687 Genomic DNA. Translation: CAA16707.1. Sequence problems.
    AL161550 Genomic DNA. Translation: CAB78920.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE84155.1.
    PIRiT04439.
    RefSeqiNP_567579.2. NM_118037.6.
    UniGeneiAt.32833.

    Genome annotation databases

    EnsemblPlantsiAT4G19180.1; AT4G19180.1; AT4G19180.
    GeneIDi827656.
    KEGGiath:AT4G19180.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    JF830012 mRNA. Translation: AEJ38088.1 .
    JQ965809 mRNA. Translation: AFL69929.1 .
    AL021687 Genomic DNA. Translation: CAA16707.1 . Sequence problems.
    AL161550 Genomic DNA. Translation: CAB78920.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE84155.1 .
    PIRi T04439.
    RefSeqi NP_567579.2. NM_118037.6.
    UniGenei At.32833.

    3D structure databases

    ProteinModelPortali F4JSH1.
    SMRi F4JSH1. Positions 144-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT4G19180.1-P.

    Proteomic databases

    PRIDEi F4JSH1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G19180.1 ; AT4G19180.1 ; AT4G19180 .
    GeneIDi 827656.
    KEGGi ath:AT4G19180.

    Organism-specific databases

    TAIRi AT4G19180.

    Phylogenomic databases

    eggNOGi COG5371.
    OMAi SKLVHNE.

    Family and domain databases

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

    Publicationsi

    1. "Functional analyses of Arabidopsis apyrases 3 through 7."
      Yang J.
      Thesis (2011), University of Texas, United States
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION, FUNCTION.
      Strain: cv. Columbia.
    2. "Cloning the Arabidopsis apyrase gene, APY7."
      Lao J., Loque D., Heazlewood J.L.
      Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
      Tissue: Stem.
    3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.

    Entry informationi

    Entry nameiAPY7_ARATH
    AccessioniPrimary (citable) accession number: F4JSH1
    Secondary accession number(s): O49676
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2012
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 27 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3