APY7_ARATH
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 03-AUG-2022, entry version 64.
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};
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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.AT4G19180.1; -.
DR iPTMnet; F4JSH1; -.
DR PaxDb; F4JSH1; -.
DR PRIDE; F4JSH1; -.
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; locus:2134731; AT4G19180.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_2_2_1; -.
DR InParanoid; F4JSH1; -.
DR OMA; PTNRKKC; -.
DR OrthoDB; 1337265at2759; -.
DR PRO; PR:F4JSH1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JSH1; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009901; P:anther dehiscence; IGI:TAIR.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 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
