ID   APY_TABYA               Reviewed;         554 AA.
AC   B3A0N5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Apyrase {ECO:0000303|PubMed:21848516};
DE            EC=3.6.1.5 {ECO:0000250|UniProtKB:P50635};
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};
DE   AltName: Allergen=Tab y 1 {ECO:0000303|PubMed:21848516};
DE   Flags: Precursor;
OS   Tabanus yao (Horsefly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Tabanomorpha; Tabanoidea;
OC   Tabanidae; Tabanus.
OX   NCBI_TaxID=485572;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-104; 143-159; 175-192;
RP   292-308; 431-444 AND 538-549, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND ALLERGEN.
RC   TISSUE=Salivary gland {ECO:0000269|PubMed:21848516};
RX   PubMed=21848516; DOI=10.1111/j.1398-9995.2011.02683.x;
RA   An S., Ma D., Wei J.F., Yang X., Yang H.W., Yang H., Xu X., He S., Lai R.;
RT   "A novel allergen Tab y 1 with inhibitory activity of platelet aggregation
RT   from salivary glands of horseflies.";
RL   Allergy 66:1420-1427(2011).
CC   -!- FUNCTION: Facilitates hematophagy by inhibiting ADP-dependent platelet
CC       aggregation in the host. Shows potential for antithrombotic activity.
CC       May reduce probing time by facilitating the speed of locating blood.
CC       {ECO:0000269|PubMed:21848516}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21848516}.
CC   -!- TISSUE SPECIFICITY: Salivary gland specific.
CC       {ECO:0000269|PubMed:21848516}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:21848516}.
CC   -!- SIMILARITY: Belongs to the 5'-nucleotidase family. {ECO:0000255}.
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DR   AlphaFoldDB; B3A0N5; -.
DR   SMR; B3A0N5; -.
DR   Allergome; 9494; Tab y 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004050; F:apyrase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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   CDD; cd07409; MPP_CD73_N; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 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:SF24; 5'-NUCLEOTIDASE; 1.
DR   PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR   Pfam; PF02872; 5_nucleotid_C; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR01607; APYRASEFAMLY.
DR   SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
PE   1: Evidence at protein level;
KW   Allergen; ATP-binding; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..554
FT                   /note="Apyrase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000414929"
FT   BINDING         43
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         45
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         92
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         92
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         124
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         224
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         248
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         418
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   BINDING         504..510
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   SITE            125
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   SITE            128
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P50635"
FT   CONFLICT        444
FT                   /note="N -> K (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000269|PubMed:21848516"
SQ   SEQUENCE   554 AA;  61880 MW;  99E4B3B04F38EF59 CRC64;
     MFKITVFIYV LQLILPSKVH SSPVPDSDNG LREFPLSIVH INDFHARFEQ TDELGGQCKP
     TAKCVGGYAR LVTTVKKLKE EGQNTIFLNA ADNYQGTLWY NLGKWNVTAY FMNLLPADAM
     TLGNHEFDDK IEGIVPFLEV IKTPIVVANI DDSLEPTFKG KYTKSVVLER GGRKIGIVGV
     IAQNTDNISS PGKLRFLDEI QSVKNESKRL REEEKVDIVI VLSHIGLDHD YDLAEQAGDY
     IDAIIGGHSH SFLWTGDNPP GKEKVVDAYP VEIVQTSGKK VLIVQASAFA RYVGNITLYF
     GENNNLIRYA GAPVYLDSDV PEVPQIVEEM KAWEEFVHEK GNEIIAESRV VLSRENCRVS
     DCNIGNFFTD AYVHEYVTSH TGPYWTPVSV GLMNVGGIRA SVDRGNITFS QLITMAPFEN
     TVDTFDLSGK HLLEAFEHAV TVPNRLGFNG QNMLQVSGVK LVYDVTKCEG QRVVSAKIRC
     QKCDIPKYEP LDPEETYRIV TASFLANGGD GFTMIRDNKK NYKVGRKDYD VLINYAKYSS
     PITIGEEGRI RIIQ
//