ID   APY3_ARATH              Reviewed;         483 AA.
AC   Q9XI62; Q3EDC8;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Probable apyrase 3;
DE            Short=AtAPY3;
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 3;
GN   Name=APY3; OrderedLocusNames=At1g14240; ORFNames=F7A19.34;
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, AND TISSUE SPECIFICITY.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia; TISSUE=Root;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9XI62-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in the initiation zone of lateral root
CC       and in the lateral root tip, the adaxial junction of lateral shoots
CC       with the stems, and in the abscission zone of flower organs. Not
CC       expressed in the rosette leaves. {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; JF830008; AEJ38084.1; -; mRNA.
DR   EMBL; AC007576; AAD39311.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29127.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29128.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29130.1; -; Genomic_DNA.
DR   EMBL; BT006000; AAO64935.1; -; mRNA.
DR   EMBL; AK227399; BAE99403.1; -; mRNA.
DR   EMBL; AK317332; BAH20006.1; -; mRNA.
DR   PIR; D86276; D86276.
DR   RefSeq; NP_001117284.1; NM_001123812.2. [Q9XI62-1]
DR   RefSeq; NP_172876.1; NM_101290.5. [Q9XI62-1]
DR   RefSeq; NP_973822.2; NM_202093.4. [Q9XI62-1]
DR   AlphaFoldDB; Q9XI62; -.
DR   SMR; Q9XI62; -.
DR   STRING; 3702.Q9XI62; -.
DR   GlyCosmos; Q9XI62; 4 sites, No reported glycans.
DR   PaxDb; 3702-AT1G14240-2; -.
DR   EnsemblPlants; AT1G14240.1; AT1G14240.1; AT1G14240. [Q9XI62-1]
DR   EnsemblPlants; AT1G14240.2; AT1G14240.2; AT1G14240. [Q9XI62-1]
DR   EnsemblPlants; AT1G14240.4; AT1G14240.4; AT1G14240. [Q9XI62-1]
DR   GeneID; 837985; -.
DR   Gramene; AT1G14240.1; AT1G14240.1; AT1G14240. [Q9XI62-1]
DR   Gramene; AT1G14240.2; AT1G14240.2; AT1G14240. [Q9XI62-1]
DR   Gramene; AT1G14240.4; AT1G14240.4; AT1G14240. [Q9XI62-1]
DR   KEGG; ath:AT1G14240; -.
DR   Araport; AT1G14240; -.
DR   TAIR; AT1G14240; APY3.
DR   eggNOG; KOG1386; Eukaryota.
DR   HOGENOM; CLU_010246_5_1_1; -.
DR   InParanoid; Q9XI62; -.
DR   OMA; FMLNFTN; -.
DR   OrthoDB; 180318at2759; -.
DR   PhylomeDB; Q9XI62; -.
DR   BioCyc; ARA:AT1G14240-MONOMER; -.
DR   BRENDA; 3.6.1.5; 399.
DR   PRO; PR:Q9XI62; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9XI62; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
DR   Genevisible; Q9XI62; AT.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Calcium; Glycoprotein; Hydrolase;
KW   Membrane; Nucleotide-binding; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..483
FT                   /note="Probable apyrase 3"
FT                   /id="PRO_0000420341"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        195
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         219..229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   483 AA;  53426 MW;  4E31D13830F1C8F9 CRC64;
     MTPETDALKV QILPKHQSLP YTVTKAKSKS LILLVVVSVT ITLGLLLYVF NSNSVISSGS
     LLSRRCKLRY SVLIDAGSSG TRVHVFGYWF ESGKPVFDFG EKHYANLKLT PGLSSYADNP
     EGASVSVTKL VEFAKQRIPK RMFRRSDIRL MATAGMRLLE VPVQEQILEV TRRVLRSSGF
     MFRDEWANVI SGSDEGIYSW ITANYALGSL GTDPLETTGI VELGGASAQV TFVSSEHVPP
     EYSRTIAYGN ISYTIYSHSF LDYGKDAALK KLLEKLQNSA NSTVDGVVED PCTPKGYIYD
     TNSKNYSSGF LADESKLKGS LQAAGNFSKC RSATFALLKE GKENCLYEHC SIGSTFTPDL
     QGSFLATASF YYTAKFFELE EKGWLSELIP AGKRYCGEEW SKLILEYPTT DEEYLRGYCF
     SAAYTISMLH DSLGIALDDE SITYASKAGE KHIPLDWALG AFILDVVTPN SDYNGKSRKY
     LGF
//