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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...

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.