ID   TP1A_RANIT              Reviewed;          16 AA.
AC   C0HL49;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2017, sequence version 1.
DT   25-MAY-2022, entry version 6.
DE   RecName: Full=Temporin-1ITa {ECO:0000303|PubMed:28699258};
OS   Rana italica (Italian stream frog) (Rana graeca italica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Rana.
OX   NCBI_TaxID=147302 {ECO:0000303|PubMed:28699258};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT LEU-16.
RC   TISSUE=Skin secretion {ECO:0000303|PubMed:28699258};
RX   PubMed=28699258; DOI=10.1002/psc.3025;
RA   Conlon J.M., Musale V., Attoub S., Mangoni M.L., Leprince J., Coquet L.,
RA   Jouenne T., Abdel-Wahab Y.H.A., Flatt P.R., Rinaldi A.C.;
RT   "Cytotoxic peptides with insulin-releasing activities from skin secretions
RT   of the Italian stream frog Rana italica (Ranidae).";
RL   J. Pept. Sci. 23:769-776(2017).
CC   -!- FUNCTION: Antimicrobial peptide active against Gram-positive bacterium
CC       S.epidermidis ATCC 12228 (MIC=8 uM) and against yeast C.parapsilosis
CC       ATCC 22019 (MIC=64 uM) but not against Gram-negative bacterium E.coli
CC       ATCC 25922. Has hemolytic and cytotoxic activity.
CC       {ECO:0000269|PubMed:28699258}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28699258}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:28699258}.
CC   -!- MASS SPECTROMETRY: Mass=1614.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:28699258};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Temporin subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; C0HL49; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Fungicide; Hemolysis; Secreted.
FT   PEPTIDE         1..16
FT                   /note="Temporin-1ITa"
FT                   /evidence="ECO:0000269|PubMed:28699258"
FT                   /id="PRO_0000442264"
FT   MOD_RES         16
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:28699258"
SQ   SEQUENCE   16 AA;  1616 MW;  FC423D285A67648D CRC64;
     FLGAIAQALT SLLGKL