APY_AEDAL
ID APY_AEDAL Reviewed; 564 AA.
AC E0D877; Q5MIX3;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Apyrase {ECO:0000303|PubMed:21842387};
DE EC=3.6.1.5 {ECO:0000303|PubMed:21842387};
DE AltName: Full=ATP-diphosphatase {ECO:0000250|UniProtKB:P50635};
DE Short=ADPase {ECO:0000250|UniProtKB:P50635};
DE AltName: Full=ATP-diphosphohydrolase {ECO:0000250|UniProtKB:P50635};
DE AltName: Full=Adenosine diphosphatase {ECO:0000250|UniProtKB:P50635, ECO:0000303|PubMed:21842387};
DE AltName: Allergen=Aed al 1 {ECO:0000303|PubMed:17244540};
DE Flags: Precursor;
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAJ14796.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Salivary gland {ECO:0000312|EMBL:BAJ14796.1};
RX PubMed=21842387; DOI=10.1007/s00436-011-2579-x;
RA Dong F., Fu Y., Li X., Jiang J., Sun J., Cheng X.;
RT "Cloning, expression, and characterization of salivary apyrase from Aedes
RT albopictus.";
RL Parasitol. Res. 110:931-937(2012).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAV90659.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-45, TISSUE SPECIFICITY,
RP AND ALLERGEN.
RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAV90659.1};
RX PubMed=17244540; DOI=10.1016/j.ibmb.2006.10.007;
RA Arca B., Lombardo F., Francischetti I.M., Pham V.M., Mestres-Simon M.,
RA Andersen J.F., Ribeiro J.M.;
RT "An insight into the sialome of the adult female mosquito Aedes
RT albopictus.";
RL Insect Biochem. Mol. Biol. 37:107-127(2007).
CC -!- FUNCTION: Facilitates hematophagy by inhibiting ADP-dependent platelet
CC aggregation in the host. May reduce probing time by facilitating the
CC speed of locating blood. Platelet aggregation was inhibited by 6% when
CC 0.4 uM recombinant apyrase was added and by 9.5% when the concentration
CC of recombinant apyrase was 0.8 uM. {ECO:0000269|PubMed:21842387}.
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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q9USP2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.6 uM for the recombinant enzyme {ECO:0000269|PubMed:21842387};
CC Vmax=1.02 nmol/sec/ug enzyme toward ATP
CC {ECO:0000269|PubMed:21842387};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21842387}.
CC -!- TISSUE SPECIFICITY: Salivary gland specific.
CC {ECO:0000269|PubMed:17244540, ECO:0000269|PubMed:21842387}.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:17244540}.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000255}.
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DR EMBL; AB576780; BAJ14796.1; -; mRNA.
DR EMBL; AY826087; AAV90659.1; -; mRNA.
DR AlphaFoldDB; E0D877; -.
DR SMR; E0D877; -.
DR Allergome; 1345; Aed al 1.
DR PRIDE; E0D877; -.
DR VEuPathDB; VectorBase:AALC636_027329; -.
DR VEuPathDB; VectorBase:AALF004988; -.
DR VEuPathDB; VectorBase:AALFPA_079132; -.
DR BRENDA; 3.6.1.5; 8486.
DR SABIO-RK; E0D877; -.
DR Proteomes; UP000069940; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; -; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR11575; PTHR11575; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; SSF55816; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 1: Evidence at protein level;
KW Allergen; ATP-binding; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Metal-binding; Nucleotide-binding; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:17244540"
FT CHAIN 26..564
FT /note="Apyrase"
FT /evidence="ECO:0000269|PubMed:21842387"
FT /id="PRO_5000623950"
FT BINDING 48
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 99
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 99
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 131
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 234
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 258
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT BINDING 509..515
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT SITE 132
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT SITE 135
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P50635"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="L -> I (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..26
FT /note="AM -> TT (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="M -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="N -> S (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="L -> F (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..473
FT /note="SV -> KI (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> K (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="E -> K (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
FT CONFLICT 551..552
FT /note="LD -> WG (in Ref. 2; AAV90659)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 62751 MW; 15B9F0F2D3BD0825 CRC64;
MAGKPGIQLF VIFLLLSSFA AVVWAMDNMP ADKDVSKLFP LTLIHINDLH ARFDETNMKS
NACTAKDQCI AGIARVYQKI QDLLKEYKSK NAIYLNAGDN FQGTLWYNLL RWQVTADFIT
KLKPTAMTLG NHEFDHTPKG LAPYLAELDK AGIPTLVANL VMNDDPDLKS SKIQKSIKVT
VGGKTIGIIG VLYDKTHEIA QTGKVTLSNA VETVKREAAA LKKDKVDIIV VLSHCSYDED
KKIAKEAGQD IDVIVGAHSH SFLYSKESNK PYDQKDKIEG PYPTIVESNN KRKIPIVQAK
SFGKYVGRLT LYFDNEGEVK HWEGYPEFID NKVKQDPKIL EALIPWRKKV QEIGSTKVGE
TTIELDRDSC RDKECTLGVL YADAFADHYT NSSFRPFAII QAGNFRNPIK VGKITNGDII
EAAPFGSTAD LIRLKGDNLW AVAEHSLALD DENRTNCLQV SGLRIVIDPS KSVGSRVVKI
DVMDNRNPKS EDLKPLDRNA EYFIALPSYL ADGKDGFSAM KEATARWTGP LDSDVFKSYV
EKIKKVDKLK LDRVIVCKAG SPCT
