ID   APY1_ARATH              Reviewed;         471 AA.
AC   Q9SQG2;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Apyrase 1;
DE            Short=AtAPY1;
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 1;
GN   Name=APY1; OrderedLocusNames=At3g04080; ORFNames=T6K12.30;
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], COFACTOR, FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RX   DOI=10.1016/S0981-9428(00)01209-2;
RA   Steinebrunner I.A., Jeter C.R., Song C., Roux S.J.;
RT   "Molecular and biochemical comparison of two different apyrases from
RT   Arabidopsis thaliana.";
RL   Plant Physiol. Biochem. 38:913-922(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=22430844; DOI=10.1104/pp.111.193151;
RA   Parsons H.T., Christiansen K., Knierim B., Carroll A., Ito J., Batth T.S.,
RA   Smith-Moritz A.M., Morrison S., McInerney P., Hadi M.Z., Auer M.,
RA   Mukhopadhyay A., Petzold C.J., Scheller H.V., Loque D., Heazlewood J.L.;
RT   "Isolation and proteomic characterization of the Arabidopsis Golgi defines
RT   functional and novel components involved in plant cell wall biosynthesis.";
RL   Plant Physiol. 159:12-26(2012).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
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).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF Clone.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=12692323; DOI=10.1104/pp.102.014308;
RA   Steinebrunner I., Wu J., Sun Y., Corbett A., Roux S.J.;
RT   "Disruption of apyrases inhibits pollen germination in Arabidopsis.";
RL   Plant Physiol. 131:1638-1647(2003).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=17534719; DOI=10.1007/s11103-007-9184-5;
RA   Wolf C., Hennig M., Romanovicz D., Steinebrunner I.;
RT   "Developmental defects and seedling lethality in apyrase AtAPY1 and AtAPY2
RT   double knockout mutants.";
RL   Plant Mol. Biol. 64:657-672(2007).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=17434987; DOI=10.1104/pp.107.097568;
RA   Wu J., Steinebrunner I., Sun Y., Butterfield T., Torres J., Arnold D.,
RA   Gonzalez A., Jacob F., Reichler S., Roux S.J.;
RT   "Apyrases (nucleoside triphosphate-diphosphohydrolases) play a key role in
RT   growth control in Arabidopsis.";
RL   Plant Physiol. 144:961-975(2007).
RN   [9]
RP   INDUCTION.
RX   PubMed=19502745; DOI=10.1271/bbb.80660;
RA   Kim S.H., Yang S.H., Kim T.J., Han J.S., Suh J.W.;
RT   "Hypertonic stress increased extracellular ATP levels and the expression of
RT   stress-responsive genes in Arabidopsis thaliana seedlings.";
RL   Biosci. Biotechnol. Biochem. 73:1252-1256(2009).
RN   [10]
RP   FUNCTION.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=21636723; DOI=10.1104/pp.111.174466;
RA   Clark G., Fraley D., Steinebrunner I., Cervantes A., Onyirimba J., Liu A.,
RA   Torres J., Tang W., Kim J., Roux S.J.;
RT   "Extracellular nucleotides and apyrases regulate stomatal aperture in
RT   Arabidopsis.";
RL   Plant Physiol. 156:1740-1753(2011).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC       nucleoside tri- and di-phosphates. Substrate preference is ATP > ADP.
CC       Functions with APY2 to reduce extracellular ATP level which is
CC       essential for pollen germination and normal plant development. Plays a
CC       role in the regulation of stomatal function by modulating extracellular
CC       ATP levels in guard cells. {ECO:0000269|PubMed:12692323,
CC       ECO:0000269|PubMed:17434987, ECO:0000269|PubMed:17534719,
CC       ECO:0000269|PubMed:21636723, 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:0000269|Ref.1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=30 uM for ATP {ECO:0000269|Ref.1};
CC         Vmax=26 umol/min/mg enzyme {ECO:0000269|Ref.1};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:22430844}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:22430844}. Membrane {ECO:0000305|PubMed:22430844};
CC       Single-pass type II membrane protein {ECO:0000305|PubMed:22430844}.
CC       Note=As cell membrane protein, the functional domain could be at the
CC       extracellular side.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, root hairs, root cap, leaves,
CC       stems, trichomes, phloem throughout the plant, guard cells, filaments
CC       of young stamens, stipules, papillae of stigmas, pollen, pollen tubes
CC       and the abscission zone of siliques. {ECO:0000269|PubMed:12692323,
CC       ECO:0000269|PubMed:17434987, ECO:0000269|PubMed:17534719,
CC       ECO:0000269|Ref.1}.
CC   -!- INDUCTION: By hypertonic stress. {ECO:0000269|PubMed:19502745}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions. Apy1 and apy2 double mutant displays developmental defects
CC       including the lack of functional root and shoot meristems, and
CC       morphogenetic and patterning abnormalities of the cotyledons. Double
CC       mutant exhibits a complete inhibition of pollen germination.
CC       {ECO:0000269|PubMed:12692323, ECO:0000269|PubMed:17434987,
CC       ECO:0000269|PubMed:17534719}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; AF093604; AAF00071.1; -; mRNA.
DR   EMBL; JQ937231; AFI41199.1; -; mRNA.
DR   EMBL; AC016829; AAF26805.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74035.1; -; Genomic_DNA.
DR   EMBL; BT029157; ABJ17092.1; -; mRNA.
DR   RefSeq; NP_187058.1; NM_111279.5.
DR   AlphaFoldDB; Q9SQG2; -.
DR   SMR; Q9SQG2; -.
DR   STRING; 3702.Q9SQG2; -.
DR   GlyCosmos; Q9SQG2; 1 site, No reported glycans.
DR   PaxDb; 3702-AT3G04080-1; -.
DR   ProteomicsDB; 244488; -.
DR   EnsemblPlants; AT3G04080.1; AT3G04080.1; AT3G04080.
DR   GeneID; 819563; -.
DR   Gramene; AT3G04080.1; AT3G04080.1; AT3G04080.
DR   KEGG; ath:AT3G04080; -.
DR   Araport; AT3G04080; -.
DR   TAIR; AT3G04080; APY1.
DR   eggNOG; KOG1385; Eukaryota.
DR   HOGENOM; CLU_010246_0_0_1; -.
DR   InParanoid; Q9SQG2; -.
DR   OMA; VVYIKWH; -.
DR   OrthoDB; 180318at2759; -.
DR   PhylomeDB; Q9SQG2; -.
DR   BioCyc; ARA:AT3G04080-MONOMER; -.
DR   BRENDA; 3.6.1.5; 399.
DR   BRENDA; 3.6.1.6; 399.
DR   PRO; PR:Q9SQG2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SQG2; baseline and differential.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004382; F:GDP phosphatase activity; IDA:TAIR.
DR   GO; GO:0045134; F:UDP phosphatase activity; IDA:TAIR.
DR   GO; GO:0009846; P:pollen germination; IGI:TAIR.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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:SF126; APYRASE 1; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
DR   Genevisible; Q9SQG2; AT.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..471
FT                   /note="Apyrase 1"
FT                   /id="PRO_0000419905"
FT   TOPO_DOM        1..21
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        22..42
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        43..471
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        194
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..82
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         218..228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  51194 MW;  6EF17A73207ECDA2 CRC64;
     MTAKRAIGRH ESLADKVHRH RGLLLVISIP IVLIALVLLL MPGTSTSVSV IEYTMKNHEG
     GSNSRGPKNY AVIFDAGSSG SRVHVYCFDQ NLDLVPLENE LELFLQLKPG LSAYPNDPRQ
     SANSLVTLLD KAEASVPREL RPKTPVRVGA TAGLRALGHQ ASENILQAVR ELLKGRSRLK
     TEANAVTVLD GTQEGSYQWV TINYLLRTLG KPYSDTVGVV DLGGGSVQMA YAIPEEDAAT
     APKPVEGEDS YVREMYLKGR KYFLYVHSYL HYGLLAARAE ILKVSEDSNN PCIATGYAGT
     YKYGGKAFKA AASPSGASLD ECRRVAINAL KVNNSLCTHM KCTFGGVWNG GGGGGQKKMF
     VASFFFDRAA EAGFVDPNQP VAEVRPLDFE KAANKACNMR MEEGKSKFPR VEEDNLPYLC
     LDLVYQYTLL VDGFGLKPSQ TITLVKKVKY GDYAVEAAWP LGSAIEAVSS P
//