ID   PLS1_PITHY              Reviewed;          19 AA.
AC   P84566;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Phylloseptin-H1 {ECO:0000303|PubMed:18644413};
DE            Short=PLS-H1 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Phylloseptin-1 {ECO:0000303|PubMed:15752569};
DE            Short=PS-1 {ECO:0000303|PubMed:15752569};
GN   Name=psn1; Synonyms=psn-1;
OS   Pithecopus hypochondrialis (Orange-legged leaf frog) (Phyllomedusa
OS   hypochondrialis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Pithecopus.
OX   NCBI_TaxID=317381;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND AMIDATION AT ASN-19.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:15752569};
RX   PubMed=15752569; DOI=10.1016/j.peptides.2004.11.002;
RA   Leite J.R.S.A., Silva L.P., Rodrigues M.I.S., Prates M.V., Brand G.D.,
RA   Lacava B.M., Azevedo R.B., Bocca A.L., Albuquerque S., Bloch C. Jr.;
RT   "Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides
RT   from the Phyllomedusa genus.";
RL   Peptides 26:565-573(2005).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=18644413; DOI=10.1016/j.peptides.2008.06.017;
RA   Amiche M., Ladram A., Nicolas P.;
RT   "A consistent nomenclature of antimicrobial peptides isolated from frogs of
RT   the subfamily Phyllomedusinae.";
RL   Peptides 29:2074-2082(2008).
RN   [3]
RP   STRUCTURE BY NMR, AND AMIDATION AT ASN-19.
RX   PubMed=18656510; DOI=10.1016/j.peptides.2008.06.022;
RA   Resende J.M., Moraes C.M., Prates M.V., Cesar A., Almeida F.C.,
RA   Mundim N.C., Valente A.P., Bemquerer M.P., Pilo-Veloso D., Bechinger B.;
RT   "Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2,
RT   and -3 and biological activity: the role of charges and hydrogen bonding
RT   interactions in stabilizing helix conformations.";
RL   Peptides 29:1633-1644(2008).
CC   -!- FUNCTION: Has antibacterial activity against the Gram-positive bacteria
CC       S.aureus and E.faecalis and the Gram-negative bacteria E.coli and
CC       P.aeruginosa. No hemolytic activity. {ECO:0000269|PubMed:15752569}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15752569}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:15752569}.
CC   -!- MASS SPECTROMETRY: Mass=2015.25; Mass_error=0.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15752569};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Phylloseptin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00546";
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DR   PDB; 2JQ0; NMR; -; A=1-19.
DR   PDBsum; 2JQ0; -.
DR   AlphaFoldDB; P84566; -.
DR   SMR; P84566; -.
DR   EvolutionaryTrace; P84566; -.
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; Amphibian defense peptide; Antibiotic;
KW   Antimicrobial; Direct protein sequencing; Secreted.
FT   PEPTIDE         1..19
FT                   /note="Phylloseptin-H1"
FT                   /id="PRO_0000043822"
FT   MOD_RES         19
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:15752569,
FT                   ECO:0000269|PubMed:18656510"
FT   HELIX           5..18
FT                   /evidence="ECO:0007829|PDB:2JQ0"
SQ   SEQUENCE   19 AA;  2016 MW;  F921C707AE708FD1 CRC64;
     FLSLIPHAIN AVSAIAKHN