ID   ES1AB_PELRI             Reviewed;          46 AA.
AC   P86155;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Esculentin-1a/b {ECO:0000303|PubMed:18855342};
DE   Contains:
DE     RecName: Full=Esculentin-1a/b(19-46) {ECO:0000303|PubMed:18855342};
DE   Contains:
DE     RecName: Full=Esculentin-1a/b(21-46) {ECO:0000303|PubMed:18855342};
OS   Pelophylax ridibundus (Marsh frog) (Rana ridibunda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=8406;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND DISULFIDE
RP   BOND.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:18855342};
RX   PubMed=18855342; DOI=10.1002/rcm.3759;
RA   Samgina T.Y., Artemenko K.A., Gorshkov V.A., Ogourtsov S.V., Zubarev R.A.,
RA   Lebedev A.T.;
RT   "De novo sequencing of peptides secreted by the skin glands of the
RT   caucasian green frog Rana ridibunda.";
RL   Rapid Commun. Mass Spectrom. 22:3517-3525(2008).
RN   [2]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, DISULFIDE BOND, MASS SPECTROMETRY,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:28012108};
RX   PubMed=28012108; DOI=10.1007/s00216-016-0143-3;
RA   Samgina T.Y., Artemenko K.A., Bergquist J., Trebse P., Torkar G.,
RA   Tolpina M.D., Lebedev A.T.;
RT   "Differentiation of frogs from two populations belonging to the Pelophylax
RT   esculentus complex by LC-MS/MS comparison of their skin peptidomes.";
RL   Anal. Bioanal. Chem. 409:1951-1961(2017).
CC   -!- FUNCTION: Antimicrobial peptide (By similarity). Stimulates insulin
CC       secretion by BRIN-BD11 cells in vitro (By similarity). Shows hemolytic
CC       activity (By similarity). {ECO:0000250|UniProtKB:P84841}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18855342,
CC       ECO:0000269|PubMed:28012108}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:28012108}.
CC   -!- MASS SPECTROMETRY: [Esculentin-1a/b]: Mass=4795; Method=Electrospray;
CC       Note=Esculentin-1a/b.; Evidence={ECO:0000269|PubMed:18855342};
CC   -!- MASS SPECTROMETRY: [Esculentin-1a/b(19-46)]: Mass=2928;
CC       Method=Electrospray; Note=Esculentin-1a/b(19-46).;
CC       Evidence={ECO:0000269|PubMed:18855342};
CC   -!- MASS SPECTROMETRY: [Esculentin-1a/b(21-46)]: Mass=2688;
CC       Method=Electrospray; Note=Esculentin-1a/b(21-46).;
CC       Evidence={ECO:0000269|PubMed:18855342};
CC   -!- MASS SPECTROMETRY: [Esculentin-1a/b]: Mass=4797.7; Method=Electrospray;
CC       Note=Esculentin-1a/b.; Evidence={ECO:0000269|PubMed:28012108};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Esculentin subfamily. {ECO:0000255}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00082";
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DR   AlphaFoldDB; P86155; -.
DR   SMR; P86155; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   InterPro; IPR012521; Antimicrobial_frog_2.
DR   Pfam; PF08023; Antimicrobial_2; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Disulfide bond; Hemolysis; Secreted.
FT   PEPTIDE         1..46
FT                   /note="Esculentin-1a/b"
FT                   /evidence="ECO:0000269|PubMed:18855342,
FT                   ECO:0000269|PubMed:28012108"
FT                   /id="PRO_0000361070"
FT   PEPTIDE         19..46
FT                   /note="Esculentin-1a/b(19-46)"
FT                   /evidence="ECO:0000269|PubMed:18855342"
FT                   /id="PRO_0000361071"
FT   PEPTIDE         21..46
FT                   /note="Esculentin-1a/b(21-46)"
FT                   /evidence="ECO:0000269|PubMed:18855342"
FT                   /id="PRO_0000361072"
FT   DISULFID        40..46
FT                   /evidence="ECO:0000269|PubMed:18855342,
FT                   ECO:0000269|PubMed:28012108"
FT   UNSURE          11
FT                   /note="L or I"
FT                   /evidence="ECO:0000269|PubMed:18855342"
SQ   SEQUENCE   46 AA;  4803 MW;  CDD607B271DFE8EF CRC64;
     GIFSKLAGKK LKNLLISGLK NVGKEVGMDV VRTGIDIAGC KIKGEC