APY6_ARATH
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 03-AUG-2022, entry version 121.
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.AT2G02970.1; -.
DR PaxDb; O80612; -.
DR PRIDE; O80612; -.
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; locus:2056725; AT2G02970.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_5_1_1; -.
DR InParanoid; O80612; -.
DR OMA; YPFNFQG; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; O80612; -.
DR BioCyc; ARA:AT2G02970-MON; -.
DR BRENDA; 3.6.1.5; 399.
DR PRO; PR:O80612; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80612; baseline and differential.
DR Genevisible; O80612; AT.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
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:0009901; P:anther dehiscence; IGI:TAIR.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
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; 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
