TPE_RANTE
ID TPE_RANTE Reviewed; 13 AA.
AC P56920;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Temporin-1Te {ECO:0000250|UniProtKB:P56917};
DE Short=TE {ECO:0000250|UniProtKB:P56917};
DE AltName: Full=Temporin-E {ECO:0000303|PubMed:9022710};
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, AMIDATION AT LEU-13, AND SUBCELLULAR LOCATION.
RC TISSUE=Skin secretion;
RX PubMed=9022710; DOI=10.1111/j.1432-1033.1996.0788r.x;
RA Simmaco M., Mignogna G., Canofeni S., Miele R., Mangoni M.L., Barra D.;
RT "Temporins, antimicrobial peptides from the European red frog Rana
RT temporaria.";
RL Eur. J. Biochem. 242:788-792(1996).
CC -!- FUNCTION: Has no antibacterial activity. Has hemolytic activity.
CC {ECO:0000250|UniProtKB:P56919}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9022710}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:9022710}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Temporin subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=00097";
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DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Cytolysis; Direct protein sequencing;
KW Hemolysis; Immunity; Innate immunity; Secreted.
FT PEPTIDE 1..13
FT /note="Temporin-1Te"
FT /evidence="ECO:0000269|PubMed:9022710"
FT /id="PRO_0000043582"
FT MOD_RES 13
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:9022710"
SQ SEQUENCE 13 AA; 1379 MW; 26505DFA79A92448 CRC64;
VLPIIGNLLN SLL