ID   ES1VB_ODOVE             Reviewed;          84 AA.
AC   Q1JS87;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Esculentin-1Vb {ECO:0000312|EMBL:CAJ34610.1};
DE            Short=esc1Vb {ECO:0000312|EMBL:CAJ34610.1};
DE   AltName: Full=Esculentin 1VEb {ECO:0000303|PubMed:16621152};
DE   Flags: Precursor;
OS   Odorrana versabilis (Chinese bamboo leaf odorous frog) (Rana versabilis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Odorrana.
OX   NCBI_TaxID=326940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=16621152; DOI=10.1016/j.peptides.2006.02.009;
RA   Chen T., Zhou M., Rao P., Walker B., Shaw C.;
RT   "The Chinese bamboo leaf odorous frog (Rana (odorrana) versabilis) and
RT   north american rana frogs share the same families of skin antimicrobial
RT   peptides.";
RL   Peptides 27:1738-1744(2006).
CC   -!- FUNCTION: Antimicrobial peptide. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16621152}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:16621152}.
CC   -!- MASS SPECTROMETRY: Mass=4938.20; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16621152};
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=00650";
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DR   EMBL; AM113514; CAJ34610.1; -; mRNA.
DR   AlphaFoldDB; Q1JS87; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR012521; Antimicrobial_frog_2.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08023; Antimicrobial_2; 1.
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; Disulfide bond; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..36
FT                   /id="PRO_0000268211"
FT   PEPTIDE         39..84
FT                   /note="Esculentin-1Vb"
FT                   /id="PRO_0000268212"
FT   DISULFID        78..84
SQ   SEQUENCE   84 AA;  9298 MW;  9BF46BDBE60DF165 CRC64;
     MFTLKKPLLL IVLLGIISLS LCEQERNADE DEESETKRGI FTKINKKKAK TGVFNIIKTI
     GKEAGMDVIR AGIDTISCKI KGEC