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B3A0N5 (APY_TABYA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 12. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apyrase

EC=3.6.1.5
Alternative name(s):
ATP-diphosphatase
Short name=ADPase
ATP-diphosphohydrolase
Adenosine diphosphatase
Allergen=Tab y 1
OrganismTabanus yao (Horsefly)
Taxonomic identifier485572 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraTabanomorphaTabanoideaTabanidaeTabanus

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Facilitates hematophagy by inhibiting ADP-dependent platelet aggregation in the host. Shows potential for antithrombotic activity. May reduce probing time by facilitating the speed of locating blood. Ref.1

Catalytic activity

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate.

Cofactor

Divalent metal cations By similarity. UniProtKB Q9USP2

Subcellular location

Secreted Ref.1.

Tissue specificity

Salivary gland specific. Ref.1

Allergenic properties

Causes an allergic reaction in human. Binds to IgE. Ref.1

Sequence similarities

Belongs to the 5'-nucleotidase family.

Ontologies

Keywords
   Cellular componentSecreted
   DiseaseAllergen
   DomainSignal
   LigandATP-binding
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processnucleotide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 554533Apyrase
PRO_0000414929

Regions

Region504 – 5107Substrate binding By similarity UniProtKB P50635

Sites

Metal binding431Divalent metal cation 1 By similarity UniProtKB P50635
Metal binding451Divalent metal cation 1 By similarity UniProtKB P50635
Metal binding921Divalent metal cation 1 By similarity UniProtKB P50635
Metal binding921Divalent metal cation 2 By similarity UniProtKB P50635
Metal binding1241Divalent metal cation 2 By similarity UniProtKB P50635
Metal binding2241Divalent metal cation 2 By similarity UniProtKB P50635
Metal binding2481Divalent metal cation 2 By similarity UniProtKB P50635
Binding site4181Substrate By similarity UniProtKB P50635
Site1251Transition state stabilizer By similarity UniProtKB P50635
Site1281Transition state stabilizer By similarity UniProtKB P50635

Experimental info

Sequence conflict4441N → K AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
B3A0N5 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: 99E4B3B04F38EF59

FASTA55461,880
        10         20         30         40         50         60 
MFKITVFIYV LQLILPSKVH SSPVPDSDNG LREFPLSIVH INDFHARFEQ TDELGGQCKP 

        70         80         90        100        110        120 
TAKCVGGYAR LVTTVKKLKE EGQNTIFLNA ADNYQGTLWY NLGKWNVTAY FMNLLPADAM 

       130        140        150        160        170        180 
TLGNHEFDDK IEGIVPFLEV IKTPIVVANI DDSLEPTFKG KYTKSVVLER GGRKIGIVGV 

       190        200        210        220        230        240 
IAQNTDNISS PGKLRFLDEI QSVKNESKRL REEEKVDIVI VLSHIGLDHD YDLAEQAGDY 

       250        260        270        280        290        300 
IDAIIGGHSH SFLWTGDNPP GKEKVVDAYP VEIVQTSGKK VLIVQASAFA RYVGNITLYF 

       310        320        330        340        350        360 
GENNNLIRYA GAPVYLDSDV PEVPQIVEEM KAWEEFVHEK GNEIIAESRV VLSRENCRVS 

       370        380        390        400        410        420 
DCNIGNFFTD AYVHEYVTSH TGPYWTPVSV GLMNVGGIRA SVDRGNITFS QLITMAPFEN 

       430        440        450        460        470        480 
TVDTFDLSGK HLLEAFEHAV TVPNRLGFNG QNMLQVSGVK LVYDVTKCEG QRVVSAKIRC 

       490        500        510        520        530        540 
QKCDIPKYEP LDPEETYRIV TASFLANGGD GFTMIRDNKK NYKVGRKDYD VLINYAKYSS 

       550 
PITIGEEGRI RIIQ 

« Hide

References

[1]"A novel allergen Tab y 1 with inhibitory activity of platelet aggregation from salivary glands of horseflies."
An S., Ma D., Wei J.F., Yang X., Yang H.W., Yang H., Xu X., He S., Lai R.
Allergy 66:1420-1427(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-104; 143-159; 175-192; 292-308; 431-444 AND 538-549, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALLERGEN.
Tissue: Salivary gland.

Cross-references

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome9494. Tab y 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.780.10. 1 hit.
InterProIPR008334. 5'-Nucleotdase_C.
IPR006146. 5'-Nucleotdase_CS.
IPR006179. 5_nucleotidase/apyrase.
IPR004843. Calcineurin-like_PHP_apaH.
[Graphical view]
PANTHERPTHR11575. PTHR11575. 1 hit.
PfamPF02872. 5_nucleotid_C. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR01607. APYRASEFAMLY.
SUPFAMSSF55816. SSF55816. 1 hit.
PROSITEPS00785. 5_NUCLEOTIDASE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAPY_TABYA
AccessionPrimary (citable) accession number: B3A0N5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: January 25, 2012
Last modified: April 16, 2014
This is version 12 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families