APY3_ORYSJ
ID APY3_ORYSJ Reviewed; 451 AA.
AC Q2QYE1; A0A0P0Y6G6;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable apyrase 3;
DE Short=OsAPY3;
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 Flags: Precursor;
GN Name=APY3; OrderedLocusNames=Os12g0123500, LOC_Os12g02980;
GN ORFNames=OsJ_35056;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
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: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; DP000011; ABA95698.2; -; Genomic_DNA.
DR EMBL; AP008218; BAF29051.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT15669.1; -; Genomic_DNA.
DR EMBL; CM000149; EEE52674.1; -; Genomic_DNA.
DR EMBL; AK072692; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; Q2QYE1; -.
DR SMR; Q2QYE1; -.
DR STRING; 4530.OS12T0123500-01; -.
DR PaxDb; Q2QYE1; -.
DR PRIDE; Q2QYE1; -.
DR EnsemblPlants; Os12t0123500-01; Os12t0123500-01; Os12g0123500.
DR Gramene; Os12t0123500-01; Os12t0123500-01; Os12g0123500.
DR eggNOG; KOG1385; Eukaryota.
DR HOGENOM; CLU_010246_0_0_1; -.
DR InParanoid; Q2QYE1; -.
DR OMA; KICRMSL; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR Genevisible; Q2QYE1; OS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 ATP-binding; Calcium; Glycoprotein; Hydrolase; Nucleotide-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..451
FT /note="Probable apyrase 3"
FT /id="PRO_0000419909"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 47..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 193..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 225
FT /note="P -> S (in Ref. 6; AK072692)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 451 AA; 48901 MW; A4DCE9410897E241 CRC64;
MAADHLVVAM LLLLALSPPA VADDTAVLGR KGGVVEGQAA GPGRYAVILD AGSTGTRVHV
FRFDNKLDLL KVGDNIELFA KVDPGLSSYA GRPQDAANSI LPLLDKANTV VPARLMNKTP
LKLGATAGLR LIGDEKANQI LEAVRDVVHT KSKYQYNPNW INVLEGSQEG SYIWVALNYL
LDKLGGDYSK TVGVVDLGGG SVQMAYAISS NTAATAPKVP EGKDPYVVKE YLKGKDYNIY
VHSYLHYGGF ASRAHILERK DGPFSNCMLR GFSGNFTYNG KQYDATAAPQ GADYHKCREE
VVKLLKVNAP CETKNCSFNG VWNGGGGAGQ DDLYVASAFY YIASHVGFIN SDAPSAKSTP
ATFKAVAEKV CKLSVKEAKV EYPNVRDHAY LCMDLIYEYS LLVDGFGLHP SKEITLVDKV
KHGEYYIDAA WPLGTAIEAV SPKKRLREIY K
