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O96559 (APY_CIMLE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits platlet aggregation by the calcium-dependent hydrolysis of ATP and ADP. Ref.1

Catalytic activity

A nucleoside 5'-triphosphate + 2 H2O = a nucleoside 5'-phosphate + 2 phosphate. Ref.1

Cofactor

Calcium. Ref.1

Sequence similarities

Belongs to the apyrase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Ref.1
Chain36 – 364329Apyrase Ref.1
PRO_0000234527

Regions

Compositional bias21 – 288Poly-Leu

Sequences

Sequence LengthMass (Da)Tools
O96559 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C398CB6D29A882DE

FASTA36441,474
        10         20         30         40         50         60 
MRSSYRVGNP IRFQPTNVVG LLLLSLVLSF MLVQSYELGH ASGETNANSK YPLTTPVEEN 

        70         80         90        100        110        120 
LKVRFKIGVI SDDDKNAVSK DESNTWVSTY LTGTLEWEKS TDKITVQWDK GNEKKVKSKY 

       130        140        150        160        170        180 
SYGGRGMELS ELVTFNGNLL TFDDRTGLVY ILKDDKVYPW VVLADGDGKN SKGFKSEWAT 

       190        200        210        220        230        240 
EKAGNLYVGS SGKEWTTKEG TIENYNPMWV KMINKNGEVT SLNWQTNYEK IRSSMNITFP 

       250        260        270        280        290        300 
GYMWHEAACW SDKYNKWFFL PRALSQEAYD SKKFETQGAN VIISCDDKFE KCEPTQIQGK 

       310        320        330        340        350        360 
TEDKRGFSNF KFVPTSEDKI IVGLKTVEAD DTTETYFTAF DLEGKVLLEE TKIDDHKYEG 


VDFV 

« Hide

References

[1]"Purification, cloning, and expression of an apyrase from the bed bug Cimex lectularius. A new type of nucleotide-binding enzyme."
Valenzuela J.G., Charlab R., Galperin M.Y., Ribeiro J.M.C.
J. Biol. Chem. 273:30583-30590(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-85; 263-284 AND 326-345, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
Tissue: Salivary gland.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF085499 mRNA. Translation: AAD09177.1.

3D structure databases

ProteinModelPortalO96559.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR009283. Apyrase.
[Graphical view]
PANTHERPTHR13023. PTHR13023. 1 hit.
PfamPF06079. Apyrase. 1 hit.
[Graphical view]
SUPFAMSSF101887. SSF101887. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAPY_CIMLE
AccessionPrimary (citable) accession number: O96559
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 40 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