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F4JSH1 (APY7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable apyrase 7

Short name=AtAPY7
EC=3.6.1.5
Alternative name(s):
ATP-diphosphatase
ATP-diphosphohydrolase
Adenosine diphosphatase
Short name=ADPase
NTPDase
Nucleoside triphosphate diphosphohydrolase 7
Gene names
Name:APY7
Ordered Locus Names:At4g19180
ORF Names:T18B16.150
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length740 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the hydrolysis of phosphoanhydride bonds of nucleoside tri- and di-phosphates By similarity. Involved in the regulation of pollen and anther development. Ref.1

Catalytic activity

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

Cofactor

Calcium By similarity.

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Tissue specificity

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. Ref.1

Induction

By wounding and drought stress. Ref.1

Disruption phenotype

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. Ref.1

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Sequence caution

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 740740Probable apyrase 7
PRO_0000420345

Regions

Topological domain1 – 113113Cytoplasmic Potential
Transmembrane114 – 13421Helical; Potential
Topological domain135 – 581447Extracellular Potential
Transmembrane582 – 60221Helical; Potential
Topological domain603 – 740138Cytoplasmic Potential
Nucleotide binding147 – 15711ATP-binding Probable
Nucleotide binding309 – 31911ATP-binding Probable
Compositional bias625 – 735111Ser-rich

Sites

Active site2841Proton acceptor By similarity

Amino acid modifications

Glycosylation1371N-linked (GlcNAc...) Potential
Glycosylation2081N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4391N-linked (GlcNAc...) Potential
Glycosylation4841N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
F4JSH1 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: 4B282DAFC67F4ED0

FASTA74081,683
        10         20         30         40         50         60 
MVFGRITELF TAASSRLPAG SQSSVPYMPT GSSPDVGTSV SDSISIGNGG RKNCLRHSAS 

        70         80         90        100        110        120 
LQDFSSYHGF DPEESILPRE AISWGQNGSS FSKEKGSVPN GTNPSTRRKL IRAVMIVMCL 

       130        140        150        160        170        180 
FLFAFLVYIV SMYIYTNWSR GASRYYVVFD CGSTGTRAYV YQASINYKKD SSLPIVMKSL 

       190        200        210        220        230        240 
TEGISRKSRG RAYDRMETEP GFDKLVNNRT GLKTAIKPLI QWAEKQIPKN AHRTTSLFVY 

       250        260        270        280        290        300 
ATAGVRRLRP ADSSWILGNV WSILAKSPFT CRREWVKIIS GTEEAYFGWT ALNYQTSMLG 

       310        320        330        340        350        360 
ALPKKATFGA LDLGGSSLQV TFENEERTHN ETNLNLRIGS VNHHLSAYSL AGYGLNDAFD 

       370        380        390        400        410        420 
RSVVHLLKKL PNVNKSDLIE GKLEMKHPCL NSGYNGQYIC SQCASSVQGG KKGKSGVSIK 

       430        440        450        460        470        480 
LVGAPNWGEC SALAKNAVNS SEWSNAKHGV DCDLQPCALP DGYPRPHGQF YAVSGFFVVY 

       490        500        510        520        530        540 
RFFNLSAEAS LDDVLEKGRE FCDKAWQVAR TSVSPQPFIE QYCFRAPYIV SLLREGLYIT 

       550        560        570        580        590        600 
DKQIIIGSGS ITWTLGVALL ESGKALSSTL GLKSYETLSM KINPIALISI LILSLLLLLC 

       610        620        630        640        650        660 
ALSRVSNCLP RFFRKSYLPL FRHNSTSASS VLNIPSPFRF QRWSPMSTGV KTPLSPTVRG 

       670        680        690        700        710        720 
SPRRPFSFGS SIQLMESSLY SSSSCVMHSC SSDSLGDIQY DSTGSFWSSP RRSQMRLQSR 

       730        740 
RSQSREDLSS SLADSHMLKM 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT04439.
RefSeqNP_567579.2. NM_118037.6.
UniGeneAt.32833.

3D structure databases

ProteinModelPortalF4JSH1.
SMRF4JSH1. Positions 144-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT4G19180.1-P.

Proteomic databases

PRIDEF4JSH1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G19180.1; AT4G19180.1; AT4G19180.
GeneID827656.
KEGGath:AT4G19180.

Organism-specific databases

TAIRAT4G19180.

Phylogenomic databases

eggNOGCOG5371.
OMASKLVHNE.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERPTHR11782. PTHR11782. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPY7_ARATH
AccessionPrimary (citable) accession number: F4JSH1
Secondary accession number(s): O49676
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2012
Last sequence update: June 28, 2011
Last modified: May 14, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names