TP1A_RANBO
ID TP1A_RANBO Reviewed; 13 AA.
AC P84116;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 17-JUN-2020, entry version 32.
DE RecName: Full=Temporin-1BYa;
OS Rana boylii (Foothill yellow-legged frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX NCBI_TaxID=160499;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, AMIDATION AT LEU-13, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000269|PubMed:14531844};
RX PubMed=14531844; DOI=10.1034/j.1399-3011.2003.00090.x;
RA Conlon J.M., Sonnevend A., Patel M., Davidson C., Nielsen P.F., Pal T.,
RA Rollins-Smith L.A.;
RT "Isolation of peptides of the brevinin-1 family with potent candidacidal
RT activity from the skin secretions of the frog Rana boylii.";
RL J. Pept. Res. 62:207-213(2003).
CC -!- FUNCTION: Antibacterial activity against Gram-positive bacterium
CC S.aureus. {ECO:0000269|PubMed:14531844}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14531844}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC -!- MASS SPECTROMETRY: Mass=1381.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:14531844};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Temporin subfamily. {ECO:0000269|PubMed:14531844}.
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..13
FT /note="Temporin-1BYa"
FT /id="PRO_0000043569"
FT MOD_RES 13
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:14531844"
FT UNSURE 13
FT /note="L or I"
FT /evidence="ECO:0000269|PubMed:14531844"
SQ SEQUENCE 13 AA; 1384 MW; C850402B9DECC33D CRC64;
FLPIIAKVLS GLL