ID   APY5_ARATH              Reviewed;         488 AA.
AC   Q6NQA8; Q9M9T7;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Probable apyrase 5;
DE            Short=AtAPY5;
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 5;
GN   Name=APY5; OrderedLocusNames=At1g14250; ORFNames=F14L17.1, F7A19;
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, AND
RP   INDUCTION.
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC       nucleoside tri- and di-phosphates. {ECO:0000250}.
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}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in young rosette leaves but only
CC       weakly in roots. {ECO:0000269|Ref.1}.
CC   -!- INDUCTION: By wounding and drought stress. {ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; JF830010; AEJ38086.1; -; mRNA.
DR   EMBL; AC007576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC012188; AAF43924.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29131.1; -; Genomic_DNA.
DR   EMBL; BT010550; AAQ65173.1; -; mRNA.
DR   EMBL; AK175135; BAD42898.1; -; mRNA.
DR   EMBL; AK175519; BAD43282.1; -; mRNA.
DR   PIR; E86276; E86276.
DR   RefSeq; NP_172877.1; NM_101291.3.
DR   AlphaFoldDB; Q6NQA8; -.
DR   SMR; Q6NQA8; -.
DR   BioGRID; 23226; 1.
DR   IntAct; Q6NQA8; 1.
DR   STRING; 3702.Q6NQA8; -.
DR   GlyCosmos; Q6NQA8; 1 site, No reported glycans.
DR   iPTMnet; Q6NQA8; -.
DR   PaxDb; 3702-AT1G14250-1; -.
DR   ProteomicsDB; 246595; -.
DR   EnsemblPlants; AT1G14250.1; AT1G14250.1; AT1G14250.
DR   GeneID; 837986; -.
DR   Gramene; AT1G14250.1; AT1G14250.1; AT1G14250.
DR   KEGG; ath:AT1G14250; -.
DR   Araport; AT1G14250; -.
DR   TAIR; AT1G14250; -.
DR   eggNOG; KOG1386; Eukaryota.
DR   HOGENOM; CLU_010246_5_1_1; -.
DR   InParanoid; Q6NQA8; -.
DR   OMA; CAVSNFV; -.
DR   OrthoDB; 180318at2759; -.
DR   PhylomeDB; Q6NQA8; -.
DR   BioCyc; ARA:AT1G14250-MONOMER; -.
DR   BRENDA; 3.6.1.5; 399.
DR   PRO; PR:Q6NQA8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q6NQA8; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:SF100; APYRASE 3-RELATED; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   Genevisible; Q6NQA8; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Glycoprotein; Hydrolase; Membrane;
KW   Nucleotide-binding; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..488
FT                   /note="Probable apyrase 5"
FT                   /id="PRO_0000420343"
FT   TOPO_DOM        1..32
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        54..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         73..83
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         220..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   488 AA;  53505 MW;  75D5ED11E61F786A CRC64;
     MDALKVQILP DNQSSPSSTH MLTKPKSKKA TKSIAMLIVA SLAITLGLLF VFSSNSVMFS
     ASFLRRSSLH YSVIIDAGSS GTRIHVFGYW FESGKPVFDF GEEHYASLKL SPGLSSYADN
     PEGASVSVTK LVEFAKGRIP KGKLKKSDIR LMATAGMRLL DVPVQEQILD VTRRVLRSSG
     FKFQDEWATV ISGTDEGIYA WVVANHALGS LGGDPLKTTG IVELGGASAQ VTFVPSEHVP
     PEFSRTISYG NVSYTIYSHS FLDFGQDAAE DKLLESLQNS VAASTGDGIV EDPCTPKGYI
     YDTHSQKDSS GFLSEESKFK ASLQVQAAGD FTKCRSATLA MLQEGKENCA YKHCSIGSTF
     TPNIQGSFLA TENFFHTSKF FGLGEKEWLS EMILAGKRFC GEEWSKLKEK YPTTKDKYLH
     RYCFSSAYII SMLHDSLGVA LDDERIKYAS KAGKENIPLD WALGAFILNT DTPTSDYNGK
     SRKMIGFK
//