APY3_ARATH
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 03-AUG-2022, entry version 138.
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.AT1G14240.2; -.
DR PaxDb; Q9XI62; -.
DR PRIDE; Q9XI62; -.
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; locus:2035786; AT1G14240.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_5_1_1; -.
DR InParanoid; Q9XI62; -.
DR OMA; QTWAELQ; -.
DR PhylomeDB; Q9XI62; -.
DR BioCyc; ARA:AT1G14240-MON; -.
DR BRENDA; 3.6.1.5; 399.
DR PRO; PR:Q9XI62; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI62; baseline and differential.
DR Genevisible; Q9XI62; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
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 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
