APY1_ARATH
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 03-AUG-2022, entry version 118.
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.AT3G04080.1; -.
DR PaxDb; Q9SQG2; -.
DR PRIDE; Q9SQG2; -.
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; locus:2103040; AT3G04080.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_0_0_1; -.
DR InParanoid; Q9SQG2; -.
DR OMA; PFVCMDL; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q9SQG2; -.
DR BioCyc; ARA:AT3G04080-MON; -.
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 Genevisible; Q9SQG2; AT.
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:0016021; C:integral component of membrane; IDA:TAIR.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
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:0004382; F:guanosine-diphosphatase activity; IDA:TAIR.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IDA:TAIR.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0009846; P:pollen germination; IGI:TAIR.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
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
