ID   ASCA1_ASCTR             Reviewed;          23 AA.
AC   P0CJ25;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Ascaphin-1;
OS   Ascaphus truei (Coastal tailed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Ascaphidae; Ascaphus.
OX   NCBI_TaxID=8439;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AMIDATION AT ASN-23, AND
RP   SYNTHESIS.
RC   TISSUE=Skin secretion;
RX   PubMed=15207717; DOI=10.1016/j.bbrc.2004.05.141;
RA   Conlon J.M., Sonnevend A., Davidson C., Smith D.D., Nielsen P.F.;
RT   "The ascaphins: a family of antimicrobial peptides from the skin secretions
RT   of the most primitive extant frog, Ascaphus truei.";
RL   Biochem. Biophys. Res. Commun. 320:170-175(2004).
CC   -!- FUNCTION: Antimicrobial peptide that shows higher potency against Gram-
CC       negative bacteria than against Gram-positive bacteria. Has a very week
CC       hemolytic activity. {ECO:0000269|PubMed:15207717}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- MASS SPECTROMETRY: Mass=2368.3; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15207717};
CC   -!- SIMILARITY: Belongs to the ascaphin family. {ECO:0000305}.
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DR   AlphaFoldDB; P0CJ25; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..23
FT                   /note="Ascaphin-1"
FT                   /id="PRO_0000406128"
FT   MOD_RES         23
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:15207717"
SQ   SEQUENCE   23 AA;  2371 MW;  49ED1D5E4CE5037F CRC64;
     GFRDVLKGAA KAFVKTVAGH IAN