ID   APY7_ARATH              Reviewed;         740 AA.
AC   F4JSH1; O49676;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Probable apyrase 7;
DE            Short=AtAPY7;
DE            EC=3.6.1.5;
DE   AltName: Full=ATP-diphosphatase;
DE   AltName: Full=ATP-diphosphohydrolase;
DE   AltName: Full=Adenosine diphosphatase;
DE            Short=ADPase;
DE   AltName: Full=NTPDase;
DE   AltName: Full=Nucleoside triphosphate diphosphohydrolase 7;
GN   Name=APY7; OrderedLocusNames=At4g19180; ORFNames=T18B16.150;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, TISSUE SPECIFICITY,
RP   INDUCTION, AND FUNCTION.
RC   STRAIN=cv. Columbia;
RA   Yang J.;
RT   "Functional analyses of Arabidopsis apyrases 3 through 7.";
RL   Thesis (2011), University of Texas, United States.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Stem;
RA   Lao J., Loque D., Heazlewood J.L.;
RT   "Cloning the Arabidopsis apyrase gene, APY7.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC       nucleoside tri- and di-phosphates (By similarity). Involved in the
CC       regulation of pollen and anther development. {ECO:0000250,
CC       ECO:0000269|Ref.1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside
CC         5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in mature pollen grains. Also expressed in
CC       more diverse tissues such as roots, leaves, stems, pistils and sepals.
CC       More particularly expressed in the vascular bundle.
CC       {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: By wounding and drought stress. {ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Apy6 and dapy7 double
CC       mutant exhibits late anther dehiscence and low male fertility. Pollen
CC       grains of double mutant are largely deformed in shape and in most
CC       cases, the cell walls of the pollen grains are interconnected.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA16707.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At4g19180 and At4g19185.; Evidence={ECO:0000305};
CC       Sequence=CAB78920.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 2 genes: At4g19180 and At4g19185.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JF830012; AEJ38088.1; -; mRNA.
DR   EMBL; JQ965809; AFL69929.1; -; mRNA.
DR   EMBL; AL021687; CAA16707.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161550; CAB78920.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84155.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM68162.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM68163.1; -; Genomic_DNA.
DR   PIR; T04439; T04439.
DR   RefSeq; NP_001329939.1; NM_001341328.1.
DR   RefSeq; NP_001329940.1; NM_001341329.1.
DR   RefSeq; NP_567579.2; NM_118037.7.
DR   AlphaFoldDB; F4JSH1; -.
DR   SMR; F4JSH1; -.
DR   STRING; 3702.F4JSH1; -.
DR   GlyCosmos; F4JSH1; 6 sites, No reported glycans.
DR   iPTMnet; F4JSH1; -.
DR   PaxDb; 3702-AT4G19180-1; -.
DR   ProteomicsDB; 240603; -.
DR   EnsemblPlants; AT4G19180.1; AT4G19180.1; AT4G19180.
DR   EnsemblPlants; AT4G19180.2; AT4G19180.2; AT4G19180.
DR   EnsemblPlants; AT4G19180.3; AT4G19180.3; AT4G19180.
DR   GeneID; 827656; -.
DR   Gramene; AT4G19180.1; AT4G19180.1; AT4G19180.
DR   Gramene; AT4G19180.2; AT4G19180.2; AT4G19180.
DR   Gramene; AT4G19180.3; AT4G19180.3; AT4G19180.
DR   KEGG; ath:AT4G19180; -.
DR   Araport; AT4G19180; -.
DR   TAIR; AT4G19180; APY7.
DR   eggNOG; KOG1386; Eukaryota.
DR   HOGENOM; CLU_010246_2_2_1; -.
DR   InParanoid; F4JSH1; -.
DR   OMA; PEYYVIL; -.
DR   OrthoDB; 1222189at2759; -.
DR   PRO; PR:F4JSH1; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; F4JSH1; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009901; P:anther dehiscence; IGI:TAIR.
DR   GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR   InterPro; IPR000407; GDA1_CD39_NTPase.
DR   PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR11782:SF125; APYRASE 7-RELATED; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Glycoprotein; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..740
FT                   /note="Probable apyrase 7"
FT                   /id="PRO_0000420345"
FT   TOPO_DOM        1..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..581
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        582..602
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        603..740
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          706..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        284
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         147..157
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         309..319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        484
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   740 AA;  81683 MW;  4B282DAFC67F4ED0 CRC64;
     MVFGRITELF TAASSRLPAG SQSSVPYMPT GSSPDVGTSV SDSISIGNGG RKNCLRHSAS
     LQDFSSYHGF DPEESILPRE AISWGQNGSS FSKEKGSVPN GTNPSTRRKL IRAVMIVMCL
     FLFAFLVYIV SMYIYTNWSR GASRYYVVFD CGSTGTRAYV YQASINYKKD SSLPIVMKSL
     TEGISRKSRG RAYDRMETEP GFDKLVNNRT GLKTAIKPLI QWAEKQIPKN AHRTTSLFVY
     ATAGVRRLRP ADSSWILGNV WSILAKSPFT CRREWVKIIS GTEEAYFGWT ALNYQTSMLG
     ALPKKATFGA LDLGGSSLQV TFENEERTHN ETNLNLRIGS VNHHLSAYSL AGYGLNDAFD
     RSVVHLLKKL PNVNKSDLIE GKLEMKHPCL NSGYNGQYIC SQCASSVQGG KKGKSGVSIK
     LVGAPNWGEC SALAKNAVNS SEWSNAKHGV DCDLQPCALP DGYPRPHGQF YAVSGFFVVY
     RFFNLSAEAS LDDVLEKGRE FCDKAWQVAR TSVSPQPFIE QYCFRAPYIV SLLREGLYIT
     DKQIIIGSGS ITWTLGVALL ESGKALSSTL GLKSYETLSM KINPIALISI LILSLLLLLC
     ALSRVSNCLP RFFRKSYLPL FRHNSTSASS VLNIPSPFRF QRWSPMSTGV KTPLSPTVRG
     SPRRPFSFGS SIQLMESSLY SSSSCVMHSC SSDSLGDIQY DSTGSFWSSP RRSQMRLQSR
     RSQSREDLSS SLADSHMLKM
//