ID   KASSO_KASSE             Reviewed;          78 AA.
AC   E6ZBE2;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Kassorin-S;
DE   AltName: Full=PreproKassorin-S;
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:CBL43005.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP   SUBCELLULAR LOCATION, AMIDATION AT LEU-77, AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000312|EMBL:CBL43005.1};
RX   PubMed=21040978; DOI=10.1016/j.molimm.2010.09.018;
RA   Chen H., Wang L., Zeller M., Hornshaw M., Wu Y., Zhou M., Li J., Hang X.,
RA   Cai J., Chen T., Shaw C.;
RT   "Kassorins: novel innate immune system peptides from skin secretions of the
RT   African hyperoliid frogs, Kassina maculata and Kassina senegalensis.";
RL   Mol. Immunol. 48:442-451(2011).
CC   -!- FUNCTION: Antimicrobial peptide. Active against the Gram-positive
CC       bacterium S.aureus (MIC=30 uM) and the yeast C.albicans (MIC=100 uM).
CC       Not effective against the Gram-negative bacterium E.coli at
CC       concentrations up to 250 uM. Lacks ability to induce contraction of
CC       smooth muscle in isolated guinea pig urinary bladder. Elicits histamine
CC       release from rat peritoneal mast cells. {ECO:0000269|PubMed:21040978}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21040978}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:21040978}.
CC   -!- MASS SPECTROMETRY: Mass=1330.81; Method=MALDI; Note=With amidation.;
CC       Evidence={ECO:0000269|PubMed:21040978};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000250|UniProtKB:P82269}.
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DR   EMBL; FN691480; CBL43005.1; -; mRNA.
DR   AlphaFoldDB; E6ZBE2; -.
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; Fungicide; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..64
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:21040978"
FT                   /id="PRO_0000421860"
FT   PEPTIDE         65..77
FT                   /note="Kassorin-S"
FT                   /id="PRO_5000683059"
FT   REGION          24..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         77
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:21040978"
SQ   SEQUENCE   78 AA;  8732 MW;  17929E94BBB54C64 CRC64;
     MLTLKKSMLL LFFLGMVSLS LANSKRADEE GEDKRADEEG EDKRADEEGE DKRADEEGEE
     KRKRFLGGIL NTITGLLG