ID   BR1T_RANTE              Reviewed;          20 AA.
AC   P82232;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Brevinin-1T;
OS   Rana temporaria (European common frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=8407;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Skin secretion;
RX   PubMed=10333736;
RX   DOI=10.1002/(sici)1097-0282(1998)47:6<435::aid-bip3>3.0.co;2-8;
RA   Simmaco M., Mignogna G., Barra D.;
RT   "Antimicrobial peptides from amphibian skin: what do they tell us?";
RL   Biopolymers 47:435-450(1998).
CC   -!- FUNCTION: Antibacterial activity against representative Gram-negative
CC       and Gram-positive bacteria and exhibits a very high hemolytic activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P82232; -.
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; IPR012520; Antimicrobial_frog_1.
DR   Pfam; PF08018; Antimicrobial_1; 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..20
FT                   /note="Brevinin-1T"
FT                   /id="PRO_0000043550"
FT   DISULFID        14..20
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   20 AA;  2199 MW;  937236DC8EAEEB84 CRC64;
     VNPIILGVLP KFVCLITKKC