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Protein

Tachystatin-A2

Gene
N/A
Organism
Tachypleus tridentatus (Japanese horseshoe crab)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits stronger antimicrobial activity against the Gram-positive bacteria (S.aureus (IC50 is 4.2 µg/ml)) and fungi (C.albicans (IC50 is 3.0 µg/ml) and P.pastoris (IC50 is 0.5 µg/ml)) than Gram-negative bacteria (E.coli (IC50 is 25 µg/ml)). Binds to chitin (8.4 µM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei32 – 321May be important for binding to chitin

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Fungicide

Names & Taxonomyi

Protein namesi
Recommended name:
Tachystatin-A2
OrganismiTachypleus tridentatus (Japanese horseshoe crab)
Taxonomic identifieri6853 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaChelicerataMerostomataXiphosuraLimulidaeTachypleus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Peptidei24 – 6744Tachystatin-A2PRO_0000256690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 471 Publication
Disulfide bondi34 ↔ 521 Publication
Disulfide bondi46 ↔ 641 Publication

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Granular hemocytes, small secretory granules.1 Publication

Structurei

Secondary structure

1
67
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343Combined sources
Beta strandi51 – 566Combined sources
Beta strandi62 – 654Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIXNMR-A24-67[»]
ProteinModelPortaliQ9U8X3.
SMRiQ9U8X3. Positions 24-67.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U8X3.

Family & Domainsi

Domaini

The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.

Keywords - Domaini

Knottin, Signal

Family and domain databases

InterProiIPR022717. Antimicrobial_tachystatin_A.
[Graphical view]
PfamiPF11406. Tachystatin_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9U8X3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLQNTLILI GCLFLMGAMI GDAYSRCQLQ GFNCVVRSYG LPTIPCCRGL
60
TCRSYFPGST YGRCQRY
Length:67
Mass (Da):7,511
Last modified:May 1, 2000 - v1
Checksum:i6477DF0556E91310
GO

Mass spectrometryi

Molecular mass is 5055.5 Da from positions 24 - 67. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023783 mRNA. Translation: BAA85250.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023783 mRNA. Translation: BAA85250.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CIXNMR-A24-67[»]
ProteinModelPortaliQ9U8X3.
SMRiQ9U8X3. Positions 24-67.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9U8X3.

Family and domain databases

InterProiIPR022717. Antimicrobial_tachystatin_A.
[Graphical view]
PfamiPF11406. Tachystatin_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins."
    Osaki T., Omotezako M., Nagayama R., Hirata M., Iwanaga S., Kasahara J., Hattori J., Ito I., Sugiyama H., Kawabata S.
    J. Biol. Chem. 274:26172-26178(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-67, MASS SPECTROMETRY, TISSUE SPECIFICITY.
    Tissue: Hemocyte.
  2. Cited for: STRUCTURE BY NMR OF 24-67, DISULFIDE BONDS.

Entry informationi

Entry nameiTACA2_TACTR
AccessioniPrimary (citable) accession number: Q9U8X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 1, 2000
Last modified: January 20, 2016
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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 one 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.