ID   B1PLA_LITPA             Reviewed;          44 AA.
AC   B6CPR5;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Brevinin-1PLa {ECO:0000312|EMBL:ACC78531.1};
DE   Flags: Precursor; Fragment;
OS   Lithobates palustris (Pickerel frog) (Rana palustris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=298395;
RN   [1] {ECO:0000312|EMBL:ACC78531.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18799711; DOI=10.1093/molbev/msn208;
RA   Tennessen J.A., Blouin M.S.;
RT   "Balancing selection at a frog antimicrobial peptide locus: fluctuating
RT   immune effector alleles?";
RL   Mol. Biol. Evol. 25:2669-2680(2008).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 21-44, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:11087945};
RX   PubMed=11087945; DOI=10.1016/s0167-4838(00)00191-6;
RA   Basir Y.J., Knoop F.C., Dulka J., Conlon J.M.;
RT   "Multiple antimicrobial peptides and peptides related to bradykinin and
RT   neuromedin N isolated from skin secretions of the pickerel frog, Rana
RT   palustris.";
RL   Biochim. Biophys. Acta 1543:95-105(2000).
CC   -!- FUNCTION: Antimicrobial peptide. {ECO:0000250|UniProtKB:Q8QFQ5}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11087945}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:11087945}.
CC   -!- MASS SPECTROMETRY: Mass=2623.2; Mass_error=0.5; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11087945};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; EU407159; ACC78531.1; -; Genomic_DNA.
DR   EMBL; EU407160; ACC78532.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6CPR5; -.
DR   SMR; B6CPR5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR012520; Antimicrobial_frog_1.
DR   Pfam; PF08018; Antimicrobial_1; 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.
FT   PROPEP          <1..18
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000413847"
FT   PEPTIDE         21..44
FT                   /note="Brevinin-1PLa"
FT                   /evidence="ECO:0000269|PubMed:11087945"
FT                   /id="PRO_5000405129"
FT   DISULFID        38..44
FT                   /evidence="ECO:0000269|PubMed:11087945"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ACC78531.1"
SQ   SEQUENCE   44 AA;  5053 MW;  5A6819385452278F CRC64;
     NAEEERRDEP DETDVEVEKR FFPNVASVPG QVLKKIFCAI SKKC