ID   APY6_ARATH              Reviewed;         555 AA.
AC   O80612; Q56WA2; Q94EZ2;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Probable apyrase 6;
DE            Short=AtAPY6;
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 6;
GN   Name=APY6; OrderedLocusNames=At2g02970; ORFNames=T17M13.14;
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, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND FUNCTION.
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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] OF 442-555.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC       nucleoside tri- and di-phosphates (By similarity). Involved in the
CC       regulation of pollen and anther development. {ECO:0000250,
CC       ECO:0000269|Ref.1}.
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: Cytoplasmic vesicle membrane {ECO:0000269|Ref.1};
CC       Multi-pass membrane protein {ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Detected in mature pollen grains (at the protein
CC       level). Also expressed in the veins and hydathode regions of rosette
CC       leaves. {ECO:0000269|Ref.1}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Apy6 and dapy7 double
CC       mutant exhibits late anther dehiscence and low male fertility. Pollen
CC       grains of double mutant are largely deformed in shape and in most
CC       cases, the cell walls of the pollen grains are interconnected.
CC       {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; JF830011; AEJ38087.1; -; mRNA.
DR   EMBL; AC004138; AAC32915.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05650.1; -; Genomic_DNA.
DR   EMBL; AF387012; AAK62457.1; -; mRNA.
DR   EMBL; AK222142; BAD95196.1; -; mRNA.
DR   PIR; G84442; G84442.
DR   RefSeq; NP_565293.1; NM_126349.3.
DR   AlphaFoldDB; O80612; -.
DR   SMR; O80612; -.
DR   STRING; 3702.O80612; -.
DR   GlyCosmos; O80612; 2 sites, No reported glycans.
DR   PaxDb; 3702-AT2G02970-1; -.
DR   ProteomicsDB; 244442; -.
DR   EnsemblPlants; AT2G02970.1; AT2G02970.1; AT2G02970.
DR   GeneID; 814826; -.
DR   Gramene; AT2G02970.1; AT2G02970.1; AT2G02970.
DR   KEGG; ath:AT2G02970; -.
DR   Araport; AT2G02970; -.
DR   TAIR; AT2G02970; APY6.
DR   eggNOG; KOG1386; Eukaryota.
DR   HOGENOM; CLU_010246_5_1_1; -.
DR   InParanoid; O80612; -.
DR   OMA; MISAGKS; -.
DR   OrthoDB; 180318at2759; -.
DR   PhylomeDB; O80612; -.
DR   BioCyc; ARA:AT2G02970-MONOMER; -.
DR   BRENDA; 3.6.1.5; 399.
DR   PRO; PR:O80612; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80612; baseline and differential.
DR   GO; GO:0030659; C:cytoplasmic vesicle 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   GO; GO:0009901; P:anther dehiscence; IGI:TAIR.
DR   GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
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:SF3; APYRASE 6-RELATED; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   Genevisible; O80612; AT.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Cytoplasmic vesicle; Glycoprotein; Hydrolase;
KW   Membrane; Nucleotide-binding; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..555
FT                   /note="Probable apyrase 6"
FT                   /id="PRO_0000420344"
FT   TOPO_DOM        1..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..512
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        534..555
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        212
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         89..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         236..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        267
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        348
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        254
FT                   /note="P -> Q (in Ref. 4; AAK62457)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   555 AA;  61288 MW;  10DBE86621323927 CRC64;
     MRRSHARSRV KNSSSSKSDM DPIKFQIRSG NRAPSSSSTY TLTKPNSKHA KSNLLLTVGS
     ISVVLGVLFL CYSILFSGGN LRGSLRYSVV IDGGSTGTRI HVFGYRIESG KPVFEFRGAN
     YASLKLHPGL SAFADDPDGA SVSLTELVEF AKGRVPKGMW IETEVRLMAT AGMRLLELPV
     QEKILGVARR VLKSSGFLFR DEWASVISGS DEGVYAWVVA NFALGSLGGD PLKTTGIVEL
     GGASAQVTFV SSEPMPPEFS RTISFGNVTY NLYSHSFLHF GQNAAHDKLW GSLLSRDHNS
     AVEPTREKIF TDPCAPKGYN LDANTQKHLS GLLAEESRLS DSFQAGGNYS QCRSAALTIL
     QDGNEKCSYQ HCSIGSTFTP KLRGRFLATE NFFYTSKFFG LGEKAWLSNM ISAGERFCGE
     DWSKLRVKDP SLHEEDLLRY CFSSAYIVSL LHDTLGIPLD DERIGYANQA GDIPLDWALG
     AFIQQTATET SQHAASGNLH WFHALFSNHP KTLHYLIGIP ILMTVLVYLV TKWRKPQLKT
     IYDLEKGRYI VTRIR
//