ID   APY_CIMLE               Reviewed;         364 AA.
AC   O96559;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=Apyrase;
DE            EC=3.6.1.5;
DE   Flags: Precursor;
GN   Name=APY {ECO:0000312|EMBL:AAD09177.1};
OS   Cimex lectularius (Bed bug) (Acanthia lectularia).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Cimicidae; Cimex.
OX   NCBI_TaxID=79782;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAD09177.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-85; 263-284 AND 326-345,
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   TISSUE=Salivary gland {ECO:0000312|EMBL:AAD09177.1};
RX   PubMed=9804829; DOI=10.1074/jbc.273.46.30583;
RA   Valenzuela J.G., Charlab R., Galperin M.Y., Ribeiro J.M.C.;
RT   "Purification, cloning, and expression of an apyrase from the bed bug Cimex
RT   lectularius. A new type of nucleotide-binding enzyme.";
RL   J. Biol. Chem. 273:30583-30590(1998).
CC   -!- FUNCTION: Inhibits platelet aggregation by the calcium-dependent
CC       hydrolysis of ATP and ADP. {ECO:0000269|PubMed:9804829}.
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         Evidence={ECO:0000269|PubMed:9804829};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:9804829};
CC   -!- SIMILARITY: Belongs to the apyrase family. {ECO:0000255}.
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DR   EMBL; AF085499; AAD09177.1; -; mRNA.
DR   RefSeq; NP_001303629.1; NM_001316700.1.
DR   AlphaFoldDB; O96559; -.
DR   SMR; O96559; -.
DR   GeneID; 106669828; -.
DR   KEGG; clec:106669828; -.
DR   CTD; 106669828; -.
DR   VEuPathDB; VectorBase:LOC106669828; -.
DR   InParanoid; O96559; -.
DR   OrthoDB; 1242at2759; -.
DR   Proteomes; UP000494040; Unplaced.
DR   GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030899; F:calcium-dependent ATPase activity; IDA:UniProtKB.
DR   GO; GO:0017110; F:nucleoside diphosphate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; NAS:UniProtKB.
DR   Gene3D; 2.120.10.100; Apyrase; 1.
DR   InterPro; IPR009283; Apyrase.
DR   InterPro; IPR036258; Apyrase_sf.
DR   PANTHER; PTHR13023; APYRASE; 1.
DR   PANTHER; PTHR13023:SF3; SOLUBLE CALCIUM-ACTIVATED NUCLEOTIDASE 1; 1.
DR   Pfam; PF06079; Apyrase; 1.
DR   SUPFAM; SSF101887; Apyrase; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Direct protein sequencing; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:9804829"
FT   CHAIN           36..364
FT                   /note="Apyrase"
FT                   /evidence="ECO:0000269|PubMed:9804829"
FT                   /id="PRO_0000234527"
SQ   SEQUENCE   364 AA;  41474 MW;  C398CB6D29A882DE CRC64;
     MRSSYRVGNP IRFQPTNVVG LLLLSLVLSF MLVQSYELGH ASGETNANSK YPLTTPVEEN
     LKVRFKIGVI SDDDKNAVSK DESNTWVSTY LTGTLEWEKS TDKITVQWDK GNEKKVKSKY
     SYGGRGMELS ELVTFNGNLL TFDDRTGLVY ILKDDKVYPW VVLADGDGKN SKGFKSEWAT
     EKAGNLYVGS SGKEWTTKEG TIENYNPMWV KMINKNGEVT SLNWQTNYEK IRSSMNITFP
     GYMWHEAACW SDKYNKWFFL PRALSQEAYD SKKFETQGAN VIISCDDKFE KCEPTQIQGK
     TEDKRGFSNF KFVPTSEDKI IVGLKTVEAD DTTETYFTAF DLEGKVLLEE TKIDDHKYEG
     VDFV
//