ID   TACHC_TACTR             Reviewed;          41 AA.
AC   P0C200;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Tachystatin-C;
OS   Tachypleus tridentatus (Japanese horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Tachypleus.
OX   NCBI_TaxID=6853;
RN   [1]
RP   PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RX   PubMed=10473569; DOI=10.1074/jbc.274.37.26172;
RA   Osaki T., Omotezako M., Nagayama R., Hirata M., Iwanaga S., Kasahara J.,
RA   Hattori J., Ito I., Sugiyama H., Kawabata S.;
RT   "Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins,
RT   with sequence similarity to spider neurotoxins.";
RL   J. Biol. Chem. 274:26172-26178(1999).
CC   -!- FUNCTION: Binds to chitin. Shows strong activity against E.coli (IC(50)
CC       is 1.2 ug/ml). Is also very active against S.aureus (IC(50) is 0.8
CC       ug/ml), C.albicans (IC(50) is 0.9 ug/ml) and P.pastoris (IC(50) is 0.3
CC       ug/ml). Binds to chitin (5.2 uM are required to obtain 50% of binding).
CC       Causes hemolysis on sheep erythrocytes, probably by forming ion-
CC       permeable pores.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Granular hemocytes, small secretory granules.
CC       {ECO:0000269|PubMed:10473569}.
CC   -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC       structurally defines this protein as a knottin. {ECO:0000250}.
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DR   AlphaFoldDB; P0C200; -.
DR   SMR; P0C200; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Hemolysis; Knottin; Secreted.
FT   PEPTIDE         1..41
FT                   /note="Tachystatin-C"
FT                   /id="PRO_0000256693"
FT   DISULFID        12..28
FT                   /evidence="ECO:0000250"
FT   DISULFID        19..33
FT                   /evidence="ECO:0000250"
FT   DISULFID        27..38
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   41 AA;  4922 MW;  A1E5C4082D64713D CRC64;
     DYDWSLRGPP KCATYGQKCR TWSPPNCCWN LRCKAFRCRP R