ID   ES2L_RANLU              Reviewed;          37 AA.
AC   P82827;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Esculentin-2L {ECO:0000303|PubMed:10651828};
OS   Rana luteiventris (Columbia spotted frog) (Rana pretiosa luteiventris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=58176;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=10651828; DOI=10.1046/j.1432-1327.2000.01074.x;
RA   Goraya J., Wang Y., Li Z., O'Flaherty M., Knoop F.C., Platz J.E.,
RA   Conlon J.M.;
RT   "Peptides with antimicrobial activity from four different families isolated
RT   from the skins of the North American frogs Rana luteiventris, Rana
RT   berlandieri and Rana pipiens.";
RL   Eur. J. Biochem. 267:894-900(2000).
CC   -!- FUNCTION: Antibacterial activity against Gram-positive bacterium
CC       S.aureus and Gram-negative bacterium E.coli. Has activity against
CC       C.albicans. {ECO:0000269|PubMed:10651828}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10651828}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:10651828}.
CC   -!- MASS SPECTROMETRY: Mass=3748.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10651828};
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=00661";
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DR   AlphaFoldDB; P82827; -.
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.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Disulfide bond; Fungicide; Secreted.
FT   PEPTIDE         1..37
FT                   /note="Esculentin-2L"
FT                   /evidence="ECO:0000269|PubMed:10651828"
FT                   /id="PRO_0000044650"
FT   DISULFID        31..37
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   37 AA;  3750 MW;  A96DDDAC236494B4 CRC64;
     GILSLFTGGI KALGKTLFKM AGKAGAEHLA CKATNQC