KASSO_PHLMA
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