TAC1_TACTR
ID TAC1_TACTR Reviewed; 77 AA.
AC P14213;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Tachyplesin-1;
DE AltName: Full=Tachyplesin I;
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].
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, AMIDATION AT ARG-40, AND DISULFIDE BONDS.
RX PubMed=3141410; DOI=10.1016/s0021-9258(18)37448-9;
RA Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S.,
RA Niwa M., Takao T., Shimonishi Y.;
RT "Tachyplesin, a class of antimicrobial peptide from the hemocytes of the
RT horseshoe crab (Tachypleus tridentatus). Isolation and chemical
RT structure.";
RL J. Biol. Chem. 263:16709-16713(1988).
RN [3]
RP STRUCTURE BY NMR OF 24-40.
RX PubMed=2394727; DOI=10.1016/s0021-9258(18)55402-8;
RA Kawano K., Yoneya T., Miyata T., Yoshikawa K., Tokunaga F., Terada Y.,
RA Iwanaga S.;
RT "Antimicrobial peptide, tachyplesin I, isolated from hemocytes of the
RT horseshoe crab (Tachypleus tridentatus). NMR determination of the beta-
RT sheet structure.";
RL J. Biol. Chem. 265:15365-15367(1990).
RN [4]
RP STRUCTURE BY NMR OF 24-40.
RX PubMed=8490053; DOI=10.1016/0167-4838(93)90183-r;
RA Tamamura H., Kuroda M., Masuda M., Otaka A., Funakoshi S., Nakashima H.,
RA Yamamoto N., Waki M., Matsumoto A., Lancelin J.-M., Kohda D., Tate S.,
RA Inagaki F., Fujii N.;
RT "A comparative study of the solution structures of tachyplesin I and a
RT novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II),
RT determined by nuclear magnetic resonance.";
RL Biochim. Biophys. Acta 1163:209-216(1993).
RN [5]
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 EMBL; M57242; AAA63538.1; -; mRNA.
DR PIR; A38345; A38345.
DR PDB; 1MA2; NMR; -; A=24-40.
DR PDB; 1MA4; NMR; -; A=24-40.
DR PDB; 1MA5; NMR; -; A=24-40.
DR PDB; 1MA6; NMR; -; A=24-40.
DR PDB; 1WO0; NMR; -; A=24-40.
DR PDB; 1WO1; NMR; -; A=24-40.
DR PDB; 2MDB; NMR; -; A=24-40.
DR PDB; 2RTV; NMR; -; A=24-40.
DR PDB; 6PIN; NMR; -; A=24-41.
DR PDBsum; 1MA2; -.
DR PDBsum; 1MA4; -.
DR PDBsum; 1MA5; -.
DR PDBsum; 1MA6; -.
DR PDBsum; 1WO0; -.
DR PDBsum; 1WO1; -.
DR PDBsum; 2MDB; -.
DR PDBsum; 2RTV; -.
DR PDBsum; 6PIN; -.
DR AlphaFoldDB; P14213; -.
DR BMRB; P14213; -.
DR SMR; P14213; -.
DR TCDB; 1.C.34.1.1; the tachyplesin (tachyplesin) family.
DR EvolutionaryTrace; P14213; -.
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:3141410"
FT PEPTIDE 24..40
FT /note="Tachyplesin-1"
FT /id="PRO_0000033576"
FT PROPEP 41..77
FT /id="PRO_0000033577"
FT MOD_RES 40
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:3141410"
FT DISULFID 26..39
FT /evidence="ECO:0000269|PubMed:3141410"
FT DISULFID 30..35
FT /evidence="ECO:0000269|PubMed:3141410"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1MA2"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1MA2"
SQ SEQUENCE 77 AA; 9349 MW; B940CAA4A641335F CRC64;
MKKLVIALCL MMVLAVMVEE AEAKWCFRVC YRGICYRRCR GKRNEVRQYR DRGYDVRAIP
EETFFTRQDE DEDDDEE
