ID   TACA1_TACTR             Reviewed;          44 AA.
AC   P0C1Z7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Tachystatin-A1;
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, MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC   TISSUE=Hemocyte;
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: Exhibits stronger antimicrobial activity against the Gram-
CC       positive bacteria (S.aureus (IC(50) is 4.2 ug/ml)) and fungi
CC       (C.albicans (IC(50) is 3.0 ug/ml) and P.pastoris (IC(50) is 0.5 ug/ml))
CC       than Gram-negative bacteria (E.coli (IC(50) is 25 ug/ml)). Binds to
CC       chitin (8.4 uM are required to obtain 50% of binding). Does not cause
CC       hemolysis on sheep erythrocytes. Has no blocking activity on the P-type
CC       calcium channel.
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}.
CC   -!- MASS SPECTROMETRY: Mass=5039.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10473569};
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DR   AlphaFoldDB; P0C1Z7; -.
DR   SMR; P0C1Z7; -.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR022717; Antimicrobial_tachystatin_A.
DR   Pfam; PF11406; Tachystatin_A; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW   Fungicide; Knottin; Secreted.
FT   PEPTIDE         1..44
FT                   /note="Tachystatin-A1"
FT                   /id="PRO_0000256689"
FT   SITE            9
FT                   /note="May be important for binding to chitin"
FT   DISULFID        4..24
FT                   /evidence="ECO:0000250"
FT   DISULFID        11..29
FT                   /evidence="ECO:0000250"
FT   DISULFID        23..41
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   44 AA;  5046 MW;  A6ADC38EB2814B50 CRC64;
     YSRCQLQGFN CVVRSYGLPT IPCCRGLTCR SYFPGSTYGR CQRF