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 07-APR-2021, entry version 15. 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}. 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; FN687445; CBK52153.1; -; mRNA. 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 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 //