ASCA8_ASCTR
ID ASCA8_ASCTR Reviewed; 19 AA.
AC P0CJ32;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Ascaphin-8;
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, SYNTHESIS, AND AMIDATION AT
RP PHE-19.
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 similar potency against
CC Gram-negative bacteria and Gram-positive bacteria. Has a high hemolytic
CC activity. {ECO:0000269|PubMed:15207717}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- MASS SPECTROMETRY: Mass=2017.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15207717};
CC -!- SIMILARITY: Belongs to the ascaphin family. {ECO:0000305}.
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DR AlphaFoldDB; P0CJ32; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Hemolysis; Secreted.
FT PEPTIDE 1..19
FT /note="Ascaphin-8"
FT /id="PRO_0000406135"
FT MOD_RES 19
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:15207717"
SQ SEQUENCE 19 AA; 2020 MW; CFE8037F30DBE505 CRC64;
GFKDLLKGAA KALVKTVLF