TACA2_TACTR
ID TACA2_TACTR Reviewed; 67 AA.
AC Q9U8X3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Tachystatin-A2 {ECO:0000303|PubMed:10473569};
DE Flags: Precursor;
OS Tachypleus tridentatus (Japanese horseshoe crab).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC Xiphosura; Limulidae; Tachypleus.
OX NCBI_TaxID=6853;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-67, FUNCTION, MASS
RP 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).
RN [2]
RP FUNCTION, AND SYNTHESIS OF 24-67.
RX PubMed=29483648; DOI=10.1038/s41594-018-0033-9;
RA Correnti C.E., Gewe M.M., Mehlin C., Bandaranayake A.D., Johnsen W.A.,
RA Rupert P.B., Brusniak M.Y., Clarke M., Burke S.E., De Van Der Schueren W.,
RA Pilat K., Turnbaugh S.M., May D., Watson A., Chan M.K., Bahl C.D.,
RA Olson J.M., Strong R.K.;
RT "Screening, large-scale production and structure-based classification of
RT cystine-dense peptides.";
RL Nat. Struct. Mol. Biol. 25:270-278(2018).
RN [3]
RP STRUCTURE BY NMR OF 24-67, AND DISULFIDE BONDS.
RX PubMed=11959852; DOI=10.1074/jbc.m111120200;
RA Fujitani N., Kawabata S., Osaki T., Kumaki Y., Demura M., Nitta K.,
RA Kawano K.;
RT "Structure of the antimicrobial peptide tachystatin A.";
RL J. Biol. Chem. 277:23651-23657(2002).
CC -!- FUNCTION: Exhibits stronger antimicrobial activity against the Gram-
CC positive bacteria (S.aureus (IC(50)=4.2 ug/ml)) and fungi (C.albicans
CC (IC(50)=3.0 ug/ml) and P.pastoris (IC(50)=0.5 ug/ml)) than Gram-
CC negative bacteria (E.coli (IC(50)=25 ug/ml)) (PubMed:10473569). Binds
CC to chitin (8.4 uM are required to obtain 50% of binding)
CC (PubMed:10473569). Does not cause hemolysis on sheep erythrocytes
CC (PubMed:10473569). Has no blocking activity on the P-type calcium
CC channel (PubMed:10473569). Has also been shown to weakly inhibit
CC Kv1.2/KCNA2 voltage-gated potassium channels and TRPV1 receptors
CC (PubMed:29483648). {ECO:0000269|PubMed:10473569,
CC ECO:0000269|PubMed:29483648}.
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.
CC {ECO:0000269|PubMed:11959852}.
CC -!- MASS SPECTROMETRY: Mass=5055.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10473569};
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DR EMBL; AB023783; BAA85250.1; -; mRNA.
DR PDB; 1CIX; NMR; -; A=24-67.
DR PDBsum; 1CIX; -.
DR AlphaFoldDB; Q9U8X3; -.
DR SMR; Q9U8X3; -.
DR EvolutionaryTrace; Q9U8X3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
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 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Disulfide bond; Fungicide; Ion channel impairing toxin; Knottin;
KW Potassium channel impairing toxin; Secreted; Signal; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10473569"
FT PEPTIDE 24..67
FT /note="Tachystatin-A2"
FT /evidence="ECO:0000269|PubMed:10473569"
FT /id="PRO_0000256690"
FT SITE 32
FT /note="May be important for binding to chitin"
FT DISULFID 27..47
FT /evidence="ECO:0000269|PubMed:11959852,
FT ECO:0000312|PDB:1CIX"
FT DISULFID 34..52
FT /evidence="ECO:0000269|PubMed:11959852,
FT ECO:0000312|PDB:1CIX"
FT DISULFID 46..64
FT /evidence="ECO:0000269|PubMed:11959852,
FT ECO:0000312|PDB:1CIX"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1CIX"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1CIX"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1CIX"
SQ SEQUENCE 67 AA; 7511 MW; 6477DF0556E91310 CRC64;
MKLQNTLILI GCLFLMGAMI GDAYSRCQLQ GFNCVVRSYG LPTIPCCRGL TCRSYFPGST
YGRCQRY
