ID   ES1IA_ODOIS             Reviewed;          84 AA.
AC   F1T149;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 1.
DT   25-MAY-2022, entry version 26.
DE   RecName: Full=Esculentin-1SIa {ECO:0000303|PubMed:21193000};
DE   Flags: Precursor;
OS   Odorrana ishikawae (Ishikawa's frog) (Rana ishikawae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Odorrana.
OX   NCBI_TaxID=310659 {ECO:0000303|PubMed:21193000};
RN   [1] {ECO:0000312|EMBL:BAK08581.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-84, FUNCTION, SYNTHESIS,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000303|PubMed:21193000};
RX   PubMed=21193000; DOI=10.1016/j.peptides.2010.12.013;
RA   Iwakoshi-Ukena E., Ukena K., Okimoto A., Soga M., Okada G., Sano N.,
RA   Fujii T., Sugawara Y., Sumida M.;
RT   "Identification and characterization of antimicrobial peptides from the
RT   skin of the endangered frog Odorrana ishikawae.";
RL   Peptides 32:670-676(2011).
CC   -!- FUNCTION: Has antimicrobial activity against Gram-negative bacterium
CC       E.coli ATCC 8739 (MIC=6.3 ug), against Gram positive bacteria S.aureus
CC       ATCC 6538 (MIC=3.1 ug), methicillin-resistant S.aureus ATCC 43300
CC       (MIC=25 ug) and B.subtilis ATCC 6633 (MIC=25 ug). Has no activity
CC       against fungus C.albicans ATCC 90028. {ECO:0000269|PubMed:21193000}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21193000}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:21193000}.
CC   -!- MASS SPECTROMETRY: Mass=4805.0; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:21193000};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Esculentin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=01703";
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DR   EMBL; AB602051; BAK08581.1; -; mRNA.
DR   AlphaFoldDB; F1T149; -.
DR   SMR; F1T149; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..36
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:21193000"
FT                   /id="PRO_0000439607"
FT   PEPTIDE         39..84
FT                   /note="Esculentin-1SIa"
FT                   /evidence="ECO:0000269|PubMed:21193000"
FT                   /id="PRO_0000439608"
FT   DISULFID        78..84
FT                   /evidence="ECO:0000250|UniProtKB:B3A0M9"
SQ   SEQUENCE   84 AA;  9062 MW;  369DA466DB53E36A CRC64;
     MFTLKKPLLL IVLLGIISLS LCEQERAADE DEGSEIKRGI FSKFAGKGIK NLLVKGVKNI
     GKEVGMDVIR TGIDIAGCKI KGEC