ID   APY_SOLTU               Reviewed;         454 AA.
AC   P80595; Q43164;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=Apyrase;
DE            EC=3.6.1.5;
DE   AltName: Full=ATP-diphosphatase;
DE   AltName: Full=ATP-diphosphohydrolase;
DE   AltName: Full=Adenosine diphosphatase;
DE            Short=ADPase;
GN   Name=RROP1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 59-160; 236-253 AND
RP   332-345.
RC   TISSUE=Tuber;
RX   PubMed=8579614; DOI=10.1006/bbrc.1996.0162;
RA   Handa M., Guidotti G.;
RT   "Purification and cloning of a soluble ATP-diphosphohydrolase (apyrase)
RT   from potato tubers (Solanum tuberosum).";
RL   Biochem. Biophys. Res. Commun. 218:916-923(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 42-54; 68-95 AND 236-253.
RC   STRAIN=cv. Desiree;
RX   PubMed=8703025; DOI=10.1074/jbc.271.36.22139;
RA   Vasconcelos E.G., Ferreira S.T., de Carvalho T.M.U., de Souza W.,
RA   Kettlun A.M., Mancilla M., Valenzuela M.A., Verjovski-Almeida S.;
RT   "Partial purification and immunohistochemical localization of ATP
RT   diphosphohydrolase from Schistosoma mansoni. Immunological cross-
RT   reactivities with potato apyrase and Toxoplasma gondii nucleoside
RT   triphosphate hydrolase.";
RL   J. Biol. Chem. 271:22139-22145(1996).
CC   -!- FUNCTION: Catalyzes the hydrolysis of phosphoanhydride bonds of
CC       nucleoside tri- and di-phosphates.
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;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR   EMBL; U58597; AAB02720.1; -; mRNA.
DR   PIR; JC4616; JC4616.
DR   AlphaFoldDB; P80595; -.
DR   SMR; P80595; -.
DR   STRING; 4113.P80595; -.
DR   GlyCosmos; P80595; 2 sites, No reported glycans.
DR   InParanoid; P80595; -.
DR   BioCyc; MetaCyc:MONOMER-16862; -.
DR   BRENDA; 3.6.1.5; 5757.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; P80595; baseline and differential.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IBA:GO_Central.
DR   GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
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:SF87; APYRASE; 1.
DR   Pfam; PF01150; GDA1_CD39; 1.
DR   PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Membrane; Nucleotide-binding; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..454
FT                   /note="Apyrase"
FT                   /id="PRO_0000019904"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..454
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         194..204
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   454 AA;  50041 MW;  9D9EFE431DA2F52F CRC64;
     MLNQNSHFIF IILAIFLVLP LSLLSKNVNA QIPLRRHLLS HESEHYAVIF DAGSTGSRVH
     VFRFDEKLGL LPIGNNIEYF MATEPGLSSY AEDPKAAANS LEPLLDGAEG VVPQELQSET
     PLELGATAGL RMLKGDAAEK ILQAVRNLVK NQSTFHSKDQ WVTILDGTQE GSYMWAAINY
     LLGNLGKDYK STTATIDLGG GSVQMAYAIS NEQFAKAPQN EDGEPYVQQK HLMSKDYNLY
     VHSYLNYGQL AGRAEIFKAS RNESNPCALE GCDGYYSYGG VDYKVKAPKK GSSWKRCRRL
     TRHALKINAK CNIEECTFNG VWNGGGGDGQ KNIHASSFFY DIGAQVGIVD TKFPSALAKP
     IQYLNAAKVA CQTNVADIKS IFPKTQDRNI PYLCMDLIYE YTLLVDGFGL NPHKEITVIH
     DVQYKNYLVG AAWPLGCAID LVSSTTNKIR VASS
//