APY5_ARATH
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 03-AUG-2022, entry version 116.
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.AT1G14250.1; -.
DR iPTMnet; Q6NQA8; -.
DR PaxDb; Q6NQA8; -.
DR PRIDE; Q6NQA8; -.
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; locus:2035802; AT1G14250.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_5_1_1; -.
DR InParanoid; Q6NQA8; -.
DR OMA; CQRPWKQ; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q6NQA8; -.
DR BioCyc; ARA:AT1G14250-MON; -.
DR BRENDA; 3.6.1.5; 399.
DR PRO; PR:Q6NQA8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q6NQA8; baseline and differential.
DR Genevisible; Q6NQA8; 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:0000325; C:plant-type vacuole; 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: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.
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
