APY2_ARATH
ID APY2_ARATH Reviewed; 472 AA.
AC Q9SPM5; F4JWK7; I1VCB1; Q8L704; Q9M7B3;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Apyrase 2;
DE Short=AtAPY2;
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 2;
GN Name=APY2; OrderedLocusNames=At5g18280; ORFNames=MRG7.24;
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].
RC STRAIN=cv. No-0;
RX PubMed=10517321; DOI=10.1007/s004380051082;
RA Roberts N.J., Brigham J., Wu B., Murphy J.B., Volpin H., Phillips D.A.,
RA Etzler M.E.;
RT "A Nod factor-binding lectin is a member of a distinct class of apyrases
RT that may be unique to the legumes.";
RL Mol. Gen. Genet. 262:261-267(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX DOI=10.1016/S0981-9428(00)01209-2;
RA Steinebrunner I.A., Jeter C.R., Song C., Roux S.J.;
RT "Molecular and biochemical comparison of two different apyrases from
RT Arabidopsis thaliana.";
RL Plant Physiol. Biochem. 38:913-922(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22430844; DOI=10.1104/pp.111.193151;
RA Parsons H.T., Christiansen K., Knierim B., Carroll A., Ito J., Batth T.S.,
RA Smith-Moritz A.M., Morrison S., McInerney P., Hadi M.Z., Auer M.,
RA Mukhopadhyay A., Petzold C.J., Scheller H.V., Loque D., Heazlewood J.L.;
RT "Isolation and proteomic characterization of the Arabidopsis Golgi defines
RT functional and novel components involved in plant cell wall biosynthesis.";
RL Plant Physiol. 159:12-26(2012).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [5]
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 [6]
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12692323; DOI=10.1104/pp.102.014308;
RA Steinebrunner I., Wu J., Sun Y., Corbett A., Roux S.J.;
RT "Disruption of apyrases inhibits pollen germination in Arabidopsis.";
RL Plant Physiol. 131:1638-1647(2003).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=17534719; DOI=10.1007/s11103-007-9184-5;
RA Wolf C., Hennig M., Romanovicz D., Steinebrunner I.;
RT "Developmental defects and seedling lethality in apyrase AtAPY1 and AtAPY2
RT double knockout mutants.";
RL Plant Mol. Biol. 64:657-672(2007).
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC nucleoside tri- and di-phosphates. Substrate preference is ATP > ADP.
CC Functions with APY1 to reduce extracellular ATP level which is
CC essential for pollen germination and normal plant development. Plays a
CC role in the regulation of stomatal function by modulating extracellular
CC ATP levels in guard cells. {ECO:0000269|PubMed:12692323,
CC ECO:0000269|PubMed:17534719, ECO:0000269|Ref.2}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for ATP {ECO:0000269|Ref.2};
CC Vmax=26 umol/min/mg enzyme {ECO:0000269|Ref.2};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:22430844}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:22430844}. Membrane {ECO:0000305|PubMed:22430844};
CC Single-pass type II membrane protein {ECO:0000305|PubMed:22430844}.
CC Note=As cell membrane protein, the functional domain could be at the
CC extracellular side.
CC -!- TISSUE SPECIFICITY: Expressed in roots, root hairs, root cap, leaves,
CC stems, trichomes, phloem throughout the plant, guard cells, filaments
CC of young stamens, stipules, papillae of stigmas, pollen, pollen tubes
CC and the abscission zone of siliques. {ECO:0000269|PubMed:12692323,
CC ECO:0000269|PubMed:17534719, ECO:0000269|Ref.2}.
CC -!- INDUCTION: By hypertonic stress.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. Apy1 and apy2 double mutant displays developmental defects
CC including the lack of functional root and shoot meristems, and
CC morphogenetic and patterning abnormalities of the cotyledons. Double
CC mutant exhibits a complete inhibition of pollen germination.
CC {ECO:0000269|PubMed:12692323, ECO:0000269|PubMed:17534719}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AF156783; AAF00612.1; -; mRNA.
DR EMBL; AF141671; AAF66599.1; -; mRNA.
DR EMBL; JQ937238; AFI41206.1; -; mRNA.
DR EMBL; AB012246; BAB09486.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92532.2; -; Genomic_DNA.
DR EMBL; AY099866; AAM20717.1; -; mRNA.
DR EMBL; AY140045; AAM98186.1; -; mRNA.
DR EMBL; BT000329; AAN15648.1; -; mRNA.
DR RefSeq; NP_197329.5; NM_121833.7.
DR AlphaFoldDB; Q9SPM5; -.
DR SMR; Q9SPM5; -.
DR STRING; 3702.AT5G18280.2; -.
DR PRIDE; Q9SPM5; -.
DR ProteomicsDB; 244416; -.
DR EnsemblPlants; AT5G18280.1; AT5G18280.1; AT5G18280.
DR GeneID; 831946; -.
DR Gramene; AT5G18280.1; AT5G18280.1; AT5G18280.
DR KEGG; ath:AT5G18280; -.
DR Araport; AT5G18280; -.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_0_0_1; -.
DR InParanoid; Q9SPM5; -.
DR OMA; DKPIVQY; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q9SPM5; -.
DR BioCyc; ARA:AT5G18280-MON; -.
DR BRENDA; 3.6.1.5; 399.
DR BRENDA; 3.6.1.6; 399.
DR PRO; PR:Q9SPM5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SPM5; baseline and differential.
DR Genevisible; Q9SPM5; AT.
DR GO; GO:0000139; C:Golgi 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: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 1: Evidence at protein level;
KW ATP-binding; Calcium; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="Apyrase 2"
FT /id="PRO_0000419906"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..472
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 195
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 219..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 20
FT /note="H -> N (in Ref. 3; AFI41206)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> V (in Ref. 2; AAF66599)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="R -> Q (in Ref. 6; AAM98186)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="M -> T (in Ref. 2; AAF66599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 472 AA; 51599 MW; FA0C280456D51224 CRC64;
MTAKRGIGRH ESLADKIQRH RGIILVISVP IVLIGLVLLL MPGRSISDSV VEEYSVHNRK
GGPNSRGPKN YAVIFDAGSS GSRVHVYCFD QNLDLIPLGN ELELFLQLKP GLSAYPTDPR
QAANSLVSLL DKAEASVPRE LRPKTHVRVG ATAGLRTLGH DASENILQAV RELLRDRSML
KTEANAVTVL DGTQEGSYQW VTINYLLRNL GKPYSDTVGV VDLGGGSVQM AYAISEEDAA
SAPKPLEGED SYVREMYLKG RKYFLYVHSY LHYGLLAARA EILKVSEDSE NPCIVAGYDG
MYKYGGKEFK APASQSGASL DECRRITINA LKVNDTLCTH MKCTFGGVWN GGRGGGQKNM
FVASFFFDRA AEAGFVDPKQ PVATVRPMDF EKAAKKACSM KLEEGKSTFP LVEEENLPYL
CMDLVYQYTL LIDGFGLEPS QTITLVKKVK YGDQAVEAAW PLGSAIEAVS SP
