ID   SENEG_KASSE             Reviewed;          76 AA.
AC   L0P323;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Senegalin {ECO:0000312|EMBL:CCI74234.1};
DE   Flags: Precursor;
OS   Kassina senegalensis (Senegal running frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Microhyloidea; Hyperoliidae; Kassina.
OX   NCBI_TaxID=8415;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CCI74234.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-75, FUNCTION, SYNTHESIS,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION
RP   AT LEU-75.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:23430307};
RX   PubMed=23430307; DOI=10.1007/s00726-013-1470-8;
RA   Wang H., Li R., Xi X., Meng T., Zhou M., Wang L., Zhang Y., Chen T.,
RA   Shaw C.;
RT   "Senegalin: a novel antimicrobial/myotropic hexadecapeptide from the skin
RT   secretion of the African running frog, Kassina senegalensis.";
RL   Amino Acids 44:1347-1355(2013).
CC   -!- FUNCTION: Antimicrobial peptide with activity against the Gram-positive
CC       bacterium S.aureus NCTC 10788 (MIC=50 um) and the yeast C.albicans NCPF
CC       1467 (MIC=150 uM). Ineffective against the Gram-negative bacterium
CC       E.coli NCTC 10418. Induces a dose-dependent contraction of rat urinary
CC       bladder smooth muscle (EC50=2.9 nM) and a dose-dependent relaxation of
CC       rat tail artery smooth muscle (EC50=37.7 nM).
CC       {ECO:0000269|PubMed:23430307}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23430307}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:23430307}.
CC   -!- MASS SPECTROMETRY: Mass=1733.12; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:23430307};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; HE863807; CCI74234.1; -; mRNA.
DR   AlphaFoldDB; L0P323; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Fungicide;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..55
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:23430307"
FT                   /id="PRO_5001105169"
FT   PEPTIDE         60..75
FT                   /note="Senegalin"
FT                   /evidence="ECO:0000269|PubMed:23430307"
FT                   /id="PRO_5001105170"
FT   REGION          24..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         75
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:23430307"
SQ   SEQUENCE   76 AA;  8565 MW;  345F26EDBB5BDA99 CRC64;
     MLSLKKSMLL LFFLGMVSFS LANKRSDGKR ADEEGEDKRA DEEGEDKRAD EEGEDKRKRF
     LPFLIPALTS LISSLG