ID   KASST_PHLMA             Reviewed;          68 AA.
AC   G0LWV9;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   25-MAY-2022, entry version 17.
DE   RecName: Full=Kasstasin {ECO:0000312|EMBL:CCA30519.1};
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:CCA30519.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-67, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AMIDATION AT LYS-67, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:21624426};
RX   PubMed=21624426; DOI=10.1016/j.biochi.2011.05.009;
RA   Li X., Feng W., Zhou M., Ma C., Chen T., Zeller M., Hornshaw M., Wang L.,
RA   Shaw C.;
RT   "Kasstasin: A novel potent vasoconstrictor peptide from the skin secretion
RT   of the African red-legged running frog, Kassina maculata.";
RL   Biochimie 93:1537-1542(2011).
CC   -!- FUNCTION: Peptide with potent vasoconstrictor properties (EC50=25 pM).
CC       Has moderate antimicrobial activity against Gram-positive bacterium
CC       S.aureus (MIC=55 uM) and against Gram-negative bacterium E.coli
CC       (MIC=110 uM). Not active against fungus C.albicans. Has weak hemolytic
CC       activity against horse erythrocytes. {ECO:0000269|PubMed:21624426}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21624426}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC       {ECO:0000269|PubMed:21624426}.
CC   -!- MASS SPECTROMETRY: Mass=2279.76; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:21624426};
CC   -!- MISCELLANEOUS: Kasstasin is a derivation of Kassina, the taxon of
CC       origin, and the Ancient Greek word 'stasis' meaning 'stoppage of flow'.
CC       {ECO:0000269|PubMed:21624426}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; FR837931; CCA30519.1; -; mRNA.
DR   AlphaFoldDB; G0LWV9; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0042310; P:vasoconstriction; 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; Cytolysis; Direct protein sequencing;
KW   Hemolysis; Secreted; Signal; Vasoactive; Vasoconstrictor.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..44
FT                   /evidence="ECO:0000255, ECO:0000303|PubMed:21624426"
FT                   /id="PRO_5000783568"
FT   PEPTIDE         47..67
FT                   /note="Kasstasin"
FT                   /evidence="ECO:0000269|PubMed:21624426"
FT                   /id="PRO_5000783569"
FT   REGION          22..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         67
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:21624426"
SQ   SEQUENCE   68 AA;  7700 MW;  66E1932A5BE2ED7E CRC64;
     MMKKSMLLLF FLGMVSFSLA DDKREDEGEE KRADEGEEKR AAEEKRFIKE LLPHLSGIID
     SVANAIKG