ID   PPM2_LIMPO              Reviewed;          18 AA.
AC   P14216;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Polyphemusin-2;
DE   AltName: Full=Polyphemusin II;
OS   Limulus polyphemus (Atlantic horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Limulus.
OX   NCBI_TaxID=6850;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT ARG-18.
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).
CC   -!- FUNCTION: Significantly inhibits the growth of Gram-negative and Gram-
CC       positive bacteria.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemocytes.
CC   -!- SIMILARITY: Belongs to the tachyplesin/polyphemusin family.
CC       {ECO:0000305}.
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DR   PIR; JU0125; JU0125.
DR   AlphaFoldDB; P14216; -.
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   Amidation; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Secreted.
FT   PEPTIDE         1..18
FT                   /note="Polyphemusin-2"
FT                   /id="PRO_0000044453"
FT   MOD_RES         18
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000269|PubMed:2514185"
FT   DISULFID        4..17
FT                   /evidence="ECO:0000250"
FT   DISULFID        8..13
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   18 AA;  2431 MW;  E402A109D2923504 CRC64;
     RRWCFRVCYK GFCYRKCR