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Protein

Apyrase

Gene

APY

Organism
Cimex lectularius (Bed bug) (Acanthia lectularia)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Ca2+1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium-dependent ATPase activity Source: UniProtKB
  3. calcium ion binding Source: InterPro
  4. nucleoside-diphosphatase activity Source: UniProtKB

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. metabolic process Source: GOC
  3. negative regulation of blood coagulation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Apyrase (EC:3.6.1.5)
Gene namesi
Name:APYImported
OrganismiCimex lectularius (Bed bug) (Acanthia lectularia)
Taxonomic identifieri79782 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraParaneopteraHemipteraEuhemipteraHeteropteraPanheteropteraCimicomorphaCimicidaeCimex

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 35351 PublicationAdd
BLAST
Chaini36 – 364329Apyrase1 PublicationPRO_0000234527Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliO96559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi21 – 288Poly-LeuSequence Analysis

Sequence similaritiesi

Belongs to the apyrase family.Sequence Analysis

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR009283. Apyrase.
[Graphical view]
PANTHERiPTHR13023. PTHR13023. 1 hit.
PfamiPF06079. Apyrase. 1 hit.
[Graphical view]
SUPFAMiSSF101887. SSF101887. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O96559-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSSYRVGNP IRFQPTNVVG LLLLSLVLSF MLVQSYELGH ASGETNANSK
60 70 80 90 100
YPLTTPVEEN LKVRFKIGVI SDDDKNAVSK DESNTWVSTY LTGTLEWEKS
110 120 130 140 150
TDKITVQWDK GNEKKVKSKY SYGGRGMELS ELVTFNGNLL TFDDRTGLVY
160 170 180 190 200
ILKDDKVYPW VVLADGDGKN SKGFKSEWAT EKAGNLYVGS SGKEWTTKEG
210 220 230 240 250
TIENYNPMWV KMINKNGEVT SLNWQTNYEK IRSSMNITFP GYMWHEAACW
260 270 280 290 300
SDKYNKWFFL PRALSQEAYD SKKFETQGAN VIISCDDKFE KCEPTQIQGK
310 320 330 340 350
TEDKRGFSNF KFVPTSEDKI IVGLKTVEAD DTTETYFTAF DLEGKVLLEE
360
TKIDDHKYEG VDFV
Length:364
Mass (Da):41,474
Last modified:May 1, 1999 - v1
Checksum:iC398CB6D29A882DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085499 mRNA. Translation: AAD09177.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF085499 mRNA. Translation: AAD09177.1.

3D structure databases

ProteinModelPortaliO96559.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR009283. Apyrase.
[Graphical view]
PANTHERiPTHR13023. PTHR13023. 1 hit.
PfamiPF06079. Apyrase. 1 hit.
[Graphical view]
SUPFAMiSSF101887. SSF101887. 1 hit.
ProtoNetiSearch...

Publicationsi

  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 glandImported.

Entry informationi

Entry nameiAPY_CIMLE
AccessioniPrimary (citable) accession number: O96559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.