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P17726 (TAP_ORNMO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Tick anticoagulant peptide

Short name=TAP
OrganismOrnithodoros moubata (Soft tick) (Argasid tick)
Taxonomic identifier6938 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaChelicerataArachnidaAcariParasitiformesIxodidaIxodoideaArgasidaeOrnithodoros

Protein attributes

Sequence length60 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

TAP is a slow, tight-binding inhibitor of blood coagulation, specific for factor Xa.

Miscellaneous

The inhibition of factor Xa seems to be reversible and stoichiometric.

Sequence similarities

Contains 1 BPTI/Kunitz inhibitor domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6060Tick anticoagulant peptide
PRO_0000155457

Regions

Domain5 – 5955BPTI/Kunitz inhibitor

Amino acid modifications

Disulfide bond5 ↔ 59 Ref.2
Disulfide bond15 ↔ 39 Ref.2
Disulfide bond33 ↔ 55 Ref.2

Secondary structure

............... 60
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17726 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 700D3D1245E83099

FASTA606,985
        10         20         30         40         50         60 
YNRLCIKPRD WIDECDSNEG GERAYFRNGK GGCDSFWICP EDHTGADYYS SYRDCFNACI 

« Hide

References

[1]"Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa."
Waxman L., Smith D.E., Arcuri K.E., Vlasuk G.P.
Science 248:593-596(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Determination of disulfide bond pairs and stability in recombinant tick anticoagulant peptide."
Sardana M., Sardana V., Rodkey J., Wood T., Ng A., Vlasuk G.P., Waxman L.
J. Biol. Chem. 266:13560-13563(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[3]"NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata."
Antuch W., Guntert P., Billeter M., Hawthorne T., Grossenbacher H., Wuethrich K.
FEBS Lett. 352:251-257(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[4]"NMR structure determination of tick anticoagulant peptide (TAP)."
Lim-Wilby M.S.L., Hallenga K., de Maeyer M., Lasters I., Vlasuk G.P., Brunck T.K.
Protein Sci. 4:178-186(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA41212.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D0DX-ray1.62A1-60[»]
1KIGX-ray3.00I1-60[»]
1TAPNMR-A1-60[»]
1TCPNMR-A1-60[»]
ProteinModelPortalP17726.
SMRP17726. Positions 1-60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-124564.

Protein family/group databases

MEROPSI52.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D4.10.410.10. 1 hit.
InterProIPR002223. Prot_inh_Kunz-m.
[Graphical view]
PfamPF00014. Kunitz_BPTI. 1 hit.
[Graphical view]
SUPFAMSSF57362. SSF57362. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP17726.

Entry information

Entry nameTAP_ORNMO
AccessionPrimary (citable) accession number: P17726
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 71 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references