BR1SC_LITSH
ID BR1SC_LITSH Reviewed; 24 AA.
AC P82906;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Brevinin-1Sc;
OS Lithobates sphenocephalus (Southern leopard frog) (Rana sphenocephala).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=146672;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RX PubMed=10604597; DOI=10.1034/j.1399-3011.1999.00123.x;
RA Conlon J.M., Halverson T., Dulka J., Platz J.E., Knoop F.C.;
RT "Peptides with antimicrobial activity of the brevinin-1 family isolated
RT from skin secretions of the southern leopard frog, Rana sphenocephala.";
RL J. Pept. Res. 54:522-527(1999).
CC -!- FUNCTION: Antibacterial activity against Gram-negative bacterium
CC E.coli. {ECO:0000269|PubMed:10604597}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- MASS SPECTROMETRY: Mass=2612; Mass_error=0.02; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10604597};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Brevinin subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P82906; -.
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 Direct protein sequencing; Disulfide bond; Secreted.
FT PEPTIDE 1..24
FT /note="Brevinin-1Sc"
FT /id="PRO_0000043548"
FT DISULFID 18..24
SQ SEQUENCE 24 AA; 2614 MW; 435347E4371C4515 CRC64;
FFPIVAGVAG QVLKKIYCTI SKKC