APY_TABYA
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 03-AUG-2022, entry version 29.
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: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.
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
