ID   XT7_XENTR               Reviewed;          18 AA.
AC   P84381;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Antimicrobial peptide 7;
DE   AltName: Full=XT-7;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, CIRCULAR DICHROISM ANALYSIS, AMIDATION AT LEU-18, MUTAGENESIS
RP   OF LYS-8, AND SYNTHESIS.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:11738090};
RX   PubMed=11738090; DOI=10.1016/s0167-4838(01)00272-2;
RA   Ali M.F., Soto A., Knoop F.C., Conlon J.M.;
RT   "Antimicrobial peptides isolated from skin secretions of the diploid frog,
RT   Xenopus tropicalis (Pipidae).";
RL   Biochim. Biophys. Acta 1550:81-89(2001).
CC   -!- FUNCTION: Has very strong antibacterial activity against many Gram-
CC       negative bacteria and the Gram-positive bacteria S.pneumoniae and
CC       Enterococcus sp. There is moderate antimicrobial activity against the
CC       Gram-negative bacterium P.aeruginosa and yeast C.albicans and weaker
CC       activity against the Streptococcal strains and E.coli. Has hemolytic
CC       activity against human red blood cells. Seems to disrupt the membranes
CC       by adopting an alpha-helical conformation.
CC       {ECO:0000269|PubMed:11738090}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11738090}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:11738090}.
CC   -!- PTM: Amidation on Leu-18 is required to adopt an alpha-helical
CC       conformation in a hydrophobic solvent. The absence of amidation leads
CC       to a decrease in cationicity leading to a more than a 10-fold decrease
CC       in antimicrobial activities. {ECO:0000269|PubMed:11738090}.
CC   -!- MASS SPECTROMETRY: Mass=1776.0; Mass_error=0.4; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11738090};
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DR   AlphaFoldDB; P84381; -.
DR   BMRB; P84381; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; 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; Fungicide; Hemolysis; Reference proteome;
KW   Secreted.
FT   PEPTIDE         1..18
FT                   /note="Antimicrobial peptide 7"
FT                   /id="PRO_0000043869"
FT   MOD_RES         18
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:11738090"
FT   MUTAGEN         8
FT                   /note="Missing: Induces a decrease in cationicity leading
FT                   to a more than a 10-fold decrease in antimicrobial
FT                   activities."
FT                   /evidence="ECO:0000269|PubMed:11738090"
SQ   SEQUENCE   18 AA;  1777 MW;  F721CDFC9A5B84F8 CRC64;
     GLLGPLLKIA AKVGSNLL