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   16-JUN-2009, entry version 29.
DE   RecName: Full=Apyrase;
DE            EC=3.6.1.5;
DE   Flags: Precursor;
GN   Name=APY;
OS   Cimex lectularius (Bed bug).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Euhemiptera; Heteroptera;
OC   Panheteroptera; Cimicomorpha; Cimicidae; Cimex.
OX   NCBI_TaxID=79782;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-85; 263-284 AND
RP   326-345, FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   TISSUE=Salivary gland;
RX   MEDLINE=99023990; 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
RT   Cimex lectularius. A new type of nucleotide-binding enzyme.";
RL   J. Biol. Chem. 273:30583-30590(1998).
CC   -!- FUNCTION: Inhibits platlet aggregation by the calcium-dependent
CC       hydrolysis of ATP and ADP.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 H(2)O = AMP + 2 phosphate.
CC   -!- COFACTOR: Calcium.
CC   -!- SIMILARITY: Belongs to the apyrase family.
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DR   EMBL; AF085499; AAD09177.1; -; mRNA.
DR   BRENDA; 3.6.1.5; 142462.
DR   GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030899; F:calcium-dependent ATPase activity; IDA:UniProtKB.
DR   GO; GO:0017110; F:nucleoside-diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0030195; P:negative regulation of blood coagulation; NAS:UniProtKB.
DR   InterPro; IPR009283; Apyrase.
DR   PANTHER; PTHR13023; Apyrase; 1.
DR   Pfam; PF06079; Apyrase; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Direct protein sequencing; Hydrolase;
KW   Nucleotide-binding; Signal.
FT   SIGNAL        1     35
FT   CHAIN        36    364       Apyrase.
FT                                /FTId=PRO_0000234527.
FT   COMPBIAS     21     28       Poly-Leu.
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
//