ID   TAC2_TACTR              Reviewed;          77 AA.
AC   P14214;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Tachyplesin-2;
DE   AltName: Full=Tachyplesin II;
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], AND AMIDATION AT ARG-40.
RX   PubMed=2250028; DOI=10.1016/s0021-9258(17)45367-1;
RA   Shigenaga T., Muta T., Toh Y., Tokunaga F., Iwanaga S.;
RT   "Antimicrobial tachyplesin peptide precursor. cDNA cloning and cellular
RT   localization in the horseshoe crab (Tachypleus tridentatus).";
RL   J. Biol. Chem. 265:21350-21354(1990).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-40.
RX   PubMed=2514185; DOI=10.1093/oxfordjournals.jbchem.a122913;
RA   Miyata T., Tokunaga F., Yonega T., Yoshikawa K., Iwanaga S., Niwa M.,
RA   Takao T., Shimonishi Y.;
RT   "Antimicrobial peptides, isolated from horseshoe crab hemocytes,
RT   tachyplesin II, and polyphemusins I and II: chemical structures and
RT   biological activity.";
RL   J. Biochem. 106:663-668(1989).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=8282718; DOI=10.1093/oxfordjournals.jbchem.a124173;
RA   Shigenaga T., Takayenoki Y., Kawasaki S., Seki N., Muta T., Toh Y., Ito A.,
RA   Iwanaga S.;
RT   "Separation of large and small granules from horseshoe crab (Tachypleus
RT   tridentatus) hemocytes and characterization of their components.";
RL   J. Biochem. 114:307-316(1993).
CC   -!- FUNCTION: Significantly inhibits the growth of Gram-negative and Gram-
CC       positive bacteria.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=S-granules.
CC   -!- TISSUE SPECIFICITY: Hemocytes.
CC   -!- SIMILARITY: Belongs to the tachyplesin/polyphemusin family.
CC       {ECO:0000305}.
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DR   PIR; B38345; B38345.
DR   PDB; 6PIO; NMR; -; A=24-41.
DR   PDBsum; 6PIO; -.
DR   AlphaFoldDB; P14214; -.
DR   BMRB; P14214; -.
DR   SMR; P14214; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:2514185"
FT   PEPTIDE         24..40
FT                   /note="Tachyplesin-2"
FT                   /id="PRO_0000033578"
FT   PROPEP          41..77
FT                   /id="PRO_0000033579"
FT   MOD_RES         40
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:2250028"
FT   DISULFID        26..39
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..35
FT                   /evidence="ECO:0000250"
FT   STRAND          25..31
FT                   /evidence="ECO:0007829|PDB:6PIO"
FT   STRAND          34..40
FT                   /evidence="ECO:0007829|PDB:6PIO"
SQ   SEQUENCE   77 AA;  9335 MW;  6EBE57A4A652AEFF CRC64;
     MKKLVIALCL MMVLAVMVEE AEARWCFRVC YRGICYRKCR GKRNEVRQYR DRGYDVRAIP
     DETFFTRQDE DEDDDEE