KASSO_KASSE
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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