APY_SOLTU
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 03-AUG-2022, entry version 92.
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 InParanoid; P80595; -.
DR BioCyc; MetaCyc:MON-16862; -.
DR BRENDA; 3.6.1.5; 5757.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; P80595; baseline and differential.
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; 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