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Apyrase 1 (AtAPY1) (EC 3.6.1.5) (ATP-diphosphatase) (ATP-diphosphohydrolase) (Adenosine diphosphatase) (ADPase) (NTPDase) (Nucleoside triphosphate diphosphohydrolase 1)

 APY1_ARATH              Reviewed;         471 AA.
Q9SQG2;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 95.
RecName: Full=Apyrase 1;
Short=AtAPY1;
EC=3.6.1.5;
AltName: Full=ATP-diphosphatase;
AltName: Full=ATP-diphosphohydrolase;
AltName: Full=Adenosine diphosphatase;
Short=ADPase;
AltName: Full=NTPDase;
AltName: Full=Nucleoside triphosphate diphosphohydrolase 1;
Name=APY1; OrderedLocusNames=At3g04080; ORFNames=T6K12.30;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], COFACTOR, FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
DOI=10.1016/S0981-9428(00)01209-2;
Steinebrunner I.A., Jeter C.R., Song C., Roux S.J.;
"Molecular and biochemical comparison of two different apyrases from
Arabidopsis thaliana.";
Plant Physiol. Biochem. 38:913-922(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
STRAIN=cv. Landsberg erecta;
PubMed=22430844; DOI=10.1104/pp.111.193151;
Parsons H.T., Christiansen K., Knierim B., Carroll A., Ito J.,
Batth T.S., Smith-Moritz A.M., Morrison S., McInerney P., Hadi M.Z.,
Auer M., Mukhopadhyay A., Petzold C.J., Scheller H.V., Loque D.,
Heazlewood J.L.;
"Isolation and proteomic characterization of the Arabidopsis Golgi
defines functional and novel components involved in plant cell wall
biosynthesis.";
Plant Physiol. 159:12-26(2012).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
"Arabidopsis ORF Clone.";
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Wassilewskija;
PubMed=12692323; DOI=10.1104/pp.102.014308;
Steinebrunner I., Wu J., Sun Y., Corbett A., Roux S.J.;
"Disruption of apyrases inhibits pollen germination in Arabidopsis.";
Plant Physiol. 131:1638-1647(2003).
[7]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Wassilewskija;
PubMed=17534719; DOI=10.1007/s11103-007-9184-5;
Wolf C., Hennig M., Romanovicz D., Steinebrunner I.;
"Developmental defects and seedling lethality in apyrase AtAPY1 and
AtAPY2 double knockout mutants.";
Plant Mol. Biol. 64:657-672(2007).
[8]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Wassilewskija;
PubMed=17434987; DOI=10.1104/pp.107.097568;
Wu J., Steinebrunner I., Sun Y., Butterfield T., Torres J., Arnold D.,
Gonzalez A., Jacob F., Reichler S., Roux S.J.;
"Apyrases (nucleoside triphosphate-diphosphohydrolases) play a key
role in growth control in Arabidopsis.";
Plant Physiol. 144:961-975(2007).
[9]
INDUCTION.
PubMed=19502745; DOI=10.1271/bbb.80660;
Kim S.H., Yang S.H., Kim T.J., Han J.S., Suh J.W.;
"Hypertonic stress increased extracellular ATP levels and the
expression of stress-responsive genes in Arabidopsis thaliana
seedlings.";
Biosci. Biotechnol. Biochem. 73:1252-1256(2009).
[10]
FUNCTION.
STRAIN=cv. Wassilewskija;
PubMed=21636723; DOI=10.1104/pp.111.174466;
Clark G., Fraley D., Steinebrunner I., Cervantes A., Onyirimba J.,
Liu A., Torres J., Tang W., Kim J., Roux S.J.;
"Extracellular nucleotides and apyrases regulate stomatal aperture in
Arabidopsis.";
Plant Physiol. 156:1740-1753(2011).
-!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
nucleoside tri- and di-phosphates. Substrate preference is ATP >
ADP. Functions with APY2 to reduce extracellular ATP level which
is essential for pollen germination and normal plant development.
Plays a role in the regulation of stomatal function by modulating
extracellular ATP levels in guard cells.
{ECO:0000269|PubMed:12692323, ECO:0000269|PubMed:17434987,
ECO:0000269|PubMed:17534719, ECO:0000269|PubMed:21636723,
ECO:0000269|Ref.1}.
-!- CATALYTIC ACTIVITY: A nucleoside 5'-triphosphate + 2 H(2)O = a
nucleoside 5'-phosphate + 2 phosphate.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|Ref.1};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=30 uM for ATP {ECO:0000269|Ref.1};
Vmax=26 umol/min/mg enzyme {ECO:0000269|Ref.1};
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:22430844}; Single-pass type II membrane
protein {ECO:0000269|PubMed:22430844}. Membrane
{ECO:0000305|PubMed:22430844}; Single-pass type II membrane
protein {ECO:0000305|PubMed:22430844}. Note=As cell membrane
protein, the functional domain could be at the extracellular side.
-!- TISSUE SPECIFICITY: Expressed in roots, root hairs, root cap,
leaves, stems, trichomes, phloem throughout the plant, guard
cells, filaments of young stamens, stipules, papillae of stigmas,
pollen, pollen tubes and the abscission zone of siliques.
{ECO:0000269|PubMed:12692323, ECO:0000269|PubMed:17434987,
ECO:0000269|PubMed:17534719, ECO:0000269|Ref.1}.
-!- INDUCTION: By hypertonic stress. {ECO:0000269|PubMed:19502745}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions. Apy1 and apy2 double mutant displays developmental
defects including the lack of functional root and shoot meristems,
and morphogenetic and patterning abnormalities of the cotyledons.
Double mutant exhibits a complete inhibition of pollen
germination. {ECO:0000269|PubMed:12692323,
ECO:0000269|PubMed:17434987, ECO:0000269|PubMed:17534719}.
-!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF093604; AAF00071.1; -; mRNA.
EMBL; JQ937231; AFI41199.1; -; mRNA.
EMBL; AC016829; AAF26805.1; -; Genomic_DNA.
EMBL; CP002686; AEE74035.1; -; Genomic_DNA.
EMBL; BT029157; ABJ17092.1; -; mRNA.
RefSeq; NP_187058.1; NM_111279.5.
UniGene; At.16940; -.
ProteinModelPortal; Q9SQG2; -.
SMR; Q9SQG2; -.
STRING; 3702.AT3G04080.1; -.
PaxDb; Q9SQG2; -.
EnsemblPlants; AT3G04080.1; AT3G04080.1; AT3G04080.
GeneID; 819563; -.
Gramene; AT3G04080.1; AT3G04080.1; AT3G04080.
KEGG; ath:AT3G04080; -.
Araport; AT3G04080; -.
TAIR; locus:2103040; AT3G04080.
eggNOG; KOG1385; Eukaryota.
eggNOG; COG5371; LUCA.
HOGENOM; HOG000220904; -.
InParanoid; Q9SQG2; -.
KO; K14641; -.
OMA; DNEMFHS; -.
OrthoDB; EOG09360CC7; -.
PhylomeDB; Q9SQG2; -.
BioCyc; ARA:AT3G04080-MONOMER; -.
Reactome; R-ATH-8850843; Phosphate bond hydrolysis by NTPDase proteins.
PRO; PR:Q9SQG2; -.
Proteomes; UP000006548; Chromosome 3.
Genevisible; Q9SQG2; AT.
GO; GO:0005768; C:endosome; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IDA:TAIR.
GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
GO; GO:0102490; F:8-oxo-dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102485; F:dATP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102486; F:dCTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102491; F:dGTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102488; F:dTTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102487; F:dUTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102489; F:GTP phosphohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004382; F:guanosine-diphosphatase activity; IDA:TAIR.
GO; GO:0045134; F:uridine-diphosphatase activity; IDA:TAIR.
GO; GO:0009846; P:pollen germination; IGI:TAIR.
InterPro; IPR000407; GDA1_CD39_NTPase.
PANTHER; PTHR11782; PTHR11782; 1.
Pfam; PF01150; GDA1_CD39; 1.
PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
1: Evidence at protein level;
ATP-binding; Calcium; Complete proteome; Glycoprotein;
Golgi apparatus; Hydrolase; Membrane; Nucleotide-binding;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 471 Apyrase 1.
/FTId=PRO_0000419905.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 43 471 Lumenal. {ECO:0000255}.
NP_BIND 72 82 ATP-binding. {ECO:0000305}.
NP_BIND 218 228 ATP-binding. {ECO:0000305}.
COMPBIAS 350 355 Poly-Gly.
ACT_SITE 194 194 Proton acceptor. {ECO:0000250}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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