ID   KASSO_PHLMA             Reviewed;          65 AA.
AC   E4Z7G0;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Kassorin-M;
DE   AltName: Full=PreproKassorin-M;
DE   Flags: Precursor;
OS   Phlyctimantis maculatus (Red-legged running frog) (Hylambates maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Microhyloidea; Hyperoliidae; Kassina.
OX   NCBI_TaxID=2517390;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CBK52153.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AMIDATION AT
RP   LEU-64, AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000312|EMBL:CBK52153.1};
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: Induces contraction of smooth muscle in isolated guinea pig
CC       urinary bladder (EC50=4.66 nM). Has no antimicrobial activity against
CC       the Gram-positive bacterium S.aureus, the Gram-negative bacterium
CC       E.coli and the yeast C.albicans. Elicits histamine release from rat
CC       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=1388.82; 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; FN687445; CBK52153.1; -; mRNA.
DR   AlphaFoldDB; E4Z7G0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0006952; P:defense response; 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; Cleavage on pair of basic residues;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..51
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:21040978"
FT                   /id="PRO_0000421859"
FT   PEPTIDE         52..64
FT                   /note="Kassorin-M"
FT                   /id="PRO_5000666360"
FT   REGION          24..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         64
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:21040978"
SQ   SEQUENCE   65 AA;  7321 MW;  B2756200A42F50CB CRC64;
     MLTLKKSMLL LFFLGMVSFS LADDKREDEA EEGEDKRADE GEEKRAAEKK RFLEGLLNTV
     TGLLG