APY_AEDAE
ID APY_AEDAE Reviewed; 562 AA.
AC P50635; Q176L2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Apyrase;
DE EC=3.6.1.5;
DE AltName: Full=ATP-diphosphatase;
DE Short=ADPase;
DE AltName: Full=ATP-diphosphohydrolase;
DE AltName: Full=Adenosine diphosphatase;
DE AltName: Allergen=Aed a 1;
DE Flags: Precursor;
GN Name=APY; ORFNames=AAEL006347;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 308-331 AND 498-521.
RC STRAIN=Rockefeller; TISSUE=Salivary gland;
RX PubMed=7846038; DOI=10.1073/pnas.92.3.694;
RA Champagne D.E., Smartt C.T., Ribeiro J.M.C., James A.A.;
RT "The salivary gland-specific apyrase of the mosquito Aedes aegypti is a
RT member of the 5'-nucleotidase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:694-698(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rockefeller; TISSUE=Salivary gland;
RX PubMed=7498420; DOI=10.1006/expr.1995.1114;
RA Smartt C.T., Kim A.P., Grossman G.L., James A.A.;
RT "The apyrase gene of the vector mosquito, Aedes aegypti, is expressed
RT specifically in the adult female salivary glands.";
RL Exp. Parasitol. 81:239-248(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: Facilitates hematophagy by preventing ADP-dependent platelet
CC aggregation in the host. May reduce probing time by facilitating the
CC speed of locating blood.
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};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Salivary gland specific.
CC -!- DEVELOPMENTAL STAGE: Not detectable in females on the first day after
CC eclosion, but is detectable on the second day. It is maximally
CC expressed by day 4.
CC -!- PTM: The N-terminus is blocked.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000305}.
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DR EMBL; L12389; AAC37218.1; -; mRNA.
DR EMBL; L41391; AAA99189.1; -; Genomic_DNA.
DR EMBL; CH477386; EAT42070.1; -; Genomic_DNA.
DR RefSeq; XP_001651910.1; XM_001651860.1.
DR AlphaFoldDB; P50635; -.
DR SMR; P50635; -.
DR STRING; 7159.AAEL006347-PA; -.
DR Allergome; 3; Aed a 1.
DR Allergome; 3539; Aed a 1.0101.
DR GeneID; 5567877; -.
DR KEGG; aag:5567877; -.
DR VEuPathDB; VectorBase:AAEL006347; -.
DR eggNOG; KOG4419; Eukaryota.
DR HOGENOM; CLU_005854_7_1_1; -.
DR InParanoid; P50635; -.
DR OMA; GRTNCLQ; -.
DR OrthoDB; 484599at2759; -.
DR PhylomeDB; P50635; -.
DR Proteomes; UP000008820; Unassembled WGS sequence.
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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..562
FT /note="Apyrase"
FT /id="PRO_0000000039"
FT BINDING 47
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 508..514
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 131
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 134
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 9
FT /note="E -> A (in strain: Rockefeller)"
FT VARIANT 30
FT /note="V -> P (in strain: Rockefeller)"
FT VARIANT 61
FT /note="V -> A (in strain: Rockefeller)"
FT VARIANT 224
FT /note="N -> K (in strain: Rockefeller)"
FT VARIANT 284
FT /note="L -> I (in strain: Rockefeller)"
FT VARIANT 314..315
FT /note="EE -> DT (in strain: Rockefeller)"
FT VARIANT 319..320
FT /note="KN -> QH (in strain: Rockefeller)"
FT VARIANT 347
FT /note="A -> E (in strain: Rockefeller)"
FT VARIANT 361
FT /note="M -> K (in strain: Rockefeller)"
FT VARIANT 472
FT /note="V -> I (in strain: Rockefeller)"
FT VARIANT 491
FT /note="K -> E (in strain: Rockefeller)"
FT VARIANT 498
FT /note="E -> Q (in strain: Rockefeller)"
FT CONFLICT 30
FT /note="V -> A (in Ref. 2; AAA99189)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="G -> GG (in Ref. 2; AAA99189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 62754 MW; EEC3C6BE34235EFD CRC64;
MAGRPGYSEV IFLYVVSVAV IARATDNMPV NKDVSKLFPL TLIHINDLHA RFEETNMKSN
VCTQKDQCIA GIARVYQKIK DLLKEYESKN PIYLNAGDNF QGTLWYNLLR WNVTADFIKK
LKPAAMTLGN HEFDHTPKGL APYLAELNKE GIPTIVANLV MNNDPDLKSS KIPKSIKLTV
GKRKIGIIGV LYDKTHEIAQ TGKVTLSNAV EAVRREAAAL KKDNIDIIVV LSHCSYEEDK
KIAAEAGDDI DVIVGAHSHS FLYSPDSKQP HDPKDKVEGP YPTLVESKNK RKIPIVQAKS
FGKYVGRLTL YFDEEGEVKN WEGYPVFIDH KVQQDPQILK DLVPWRAKVE AIGSTVVGET
MIELDRDSCR DQECTLGVLY ADGFADQYTN DTFRPFAIIQ AGNFRNPIKV GKITNGDIIE
AAPFGSTADL IRLKGADIWD VAEHSFALDD EGRTNCLQVS GLRIVIDISK PVRSRVKKIE
VMDYTNPKSD KLKPLDKEAE YYIVVPSYLA DGKDGFSAMK RATARRTGPL DSDVFKNYVE
KIKKVDNLKL GRVIVCKGSK CT
