ID   ES1_PELSA               Reviewed;          46 AA.
AC   P84840;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Esculentin-1 {ECO:0000303|PubMed:16394170};
OS   Pelophylax saharicus (Sahara frog) (Rana saharica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=70019;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:16394170};
RX   PubMed=16394170; DOI=10.1677/joe.1.06293;
RA   Marenah L., Flatt P.R., Orr D.F., Shaw C., Abdel-Wahab Y.H.A.;
RT   "Skin secretions of Rana saharica frogs reveal antimicrobial peptides
RT   esculentins-1 and -1B and brevinins-1E and -2EC with novel insulin
RT   releasing activity.";
RL   J. Endocrinol. 188:1-9(2006).
CC   -!- FUNCTION: Antimicrobial peptide (By similarity). Stimulates insulin
CC       release by BRIN-BD11 cells in vitro. {ECO:0000250,
CC       ECO:0000269|PubMed:16394170}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16394170}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:16394170}.
CC   -!- MASS SPECTROMETRY: Mass=4920.4; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16394170};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Esculentin subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P84840; -.
DR   SMR; P84840; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IDA:UniProtKB.
DR   InterPro; IPR012521; Antimicrobial_frog_2.
DR   Pfam; PF08023; Antimicrobial_2; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   PEPTIDE         1..46
FT                   /note="Esculentin-1"
FT                   /evidence="ECO:0000269|PubMed:16394170"
FT                   /id="PRO_0000233922"
FT   DISULFID        40..46
FT                   /evidence="ECO:0000250|UniProtKB:P32414"
SQ   SEQUENCE   46 AA;  4922 MW;  F271DB3776AF855C CRC64;
     GIFSKFGRKK IKNLLISGLK NVGKEVGMDV VRTGIDIAGC KIKGEC