ID   DRSPH_PITHY             Reviewed;          70 AA.
AC   A0A2U8JCR5;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Dermaseptin-PH {ECO:0000303|PubMed:31635388};
DE            Short=DRS-PH {ECO:0000305|PubMed:31635388};
DE   Flags: Precursor;
GN   Name=DMP-PH {ECO:0000312|EMBL:AWK58821.1};
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 45-67, FUNCTION, SYNTHESIS
RP   OF 45-67, SUBCELLULAR LOCATION, AND AMIDATION AT GLN-67.
RC   TISSUE=Skin secretion;
RX   PubMed=31635388; DOI=10.3390/biom9100628;
RA   Li M., Xi X., Ma C., Chen X., Zhou M., Burrows J.F., Chen T., Wang L.;
RT   "A novel dermaseptin isolated from the skin secretion of phyllomedusa
RT   tarsius and its cationicity-enhanced analogue exhibiting effective
RT   antimicrobial and anti-proliferative activities.";
RL   Biomolecules 9:0-0(2019).
CC   -!- FUNCTION: Antimicrobial peptide which inhibits the growth of Gram-
CC       negative (MIC=16-64 uM) and Gram-positive bacteria (MIC=32 uM), and
CC       pathogenic yeast Candida albicans (MIC=16 uM) (PubMed:31635388). Shows
CC       a broad-spectrum of anticancer activities against several cancer cell
CC       lines (PubMed:31635388). Also shows slight cytotoxicity on human dermal
CC       microvascular endothelium cells (IC(50)=4.85 uM) (PubMed:31635388).
CC       Induces low hemolysis against horse erythrocytes (PubMed:31635388).
CC       {ECO:0000269|PubMed:31635388}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31635388}. Target
CC       cell membrane {ECO:0000305|PubMed:31635388}. Note=Forms a helical
CC       membrane channel in the prey. {ECO:0000305|PubMed:31635388}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:31635388}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       {ECO:0000305}.
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DR   EMBL; MF805718; AWK58821.1; -; mRNA.
DR   AlphaFoldDB; A0A2U8JCR5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Fungicide; Immunity; Innate immunity; Membrane;
KW   Secreted; Signal; Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..44
FT                   /evidence="ECO:0000269|PubMed:31635388"
FT                   /id="PRO_0000449597"
FT   PEPTIDE         45..67
FT                   /note="Dermaseptin-PH"
FT                   /evidence="ECO:0000269|PubMed:31635388"
FT                   /id="PRO_5016037295"
FT   PROPEP          68..70
FT                   /evidence="ECO:0000269|PubMed:31635388"
FT                   /id="PRO_0000449598"
FT   MOD_RES         67
FT                   /note="Glutamine amide"
FT                   /evidence="ECO:0000269|PubMed:31635388"
SQ   SEQUENCE   70 AA;  8024 MW;  D68D05AD7914F747 CRC64;
     MDILKKSLFL ILFLGVVSLS ICEEEKRENE EEMEQDDEQS EMKRALWKEV LKNAGKAALN
     EINNLVQGGQ