ID   TP1A_LITPA              Reviewed;          62 AA.
AC   A7WNV7;
DT   16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Temporin-1PLa {ECO:0000303|PubMed:11087945, ECO:0000303|PubMed:17698247};
DE   Flags: Precursor;
OS   Lithobates palustris (Pickerel frog) (Rana palustris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=298395;
RN   [1] {ECO:0000312|EMBL:CAN87013.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:17698247};
RX   PubMed=17698247; DOI=10.1016/j.peptides.2007.07.019;
RA   Zhou M., Wang L., Owens D.E., Chen T., Walker B., Shaw C.;
RT   "Rapid identification of precursor cDNAs encoding five structural classes
RT   of antimicrobial peptides from pickerel frog (Rana palustris) skin
RT   secretion by single step 'shotgun' cloning.";
RL   Peptides 28:1605-1610(2007).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 48-60, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, AND AMIDATION AT ILE-60.
RC   TISSUE=Skin secretion {ECO:0000269|PubMed:11087945};
RX   PubMed=11087945; DOI=10.1016/s0167-4838(00)00191-6;
RA   Basir Y.J., Knoop F.C., Dulka J., Conlon J.M.;
RT   "Multiple antimicrobial peptides and peptides related to bradykinin and
RT   neuromedin N isolated from skin secretions of the pickerel frog, Rana
RT   palustris.";
RL   Biochim. Biophys. Acta 1543:95-105(2000).
CC   -!- FUNCTION: Antimicrobial activity against the Gram-positive bacterium
CC       S.aureus. {ECO:0000269|PubMed:11087945}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11087945}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:11087945}.
CC   -!- MASS SPECTROMETRY: Mass=1368.8; Mass_error=0.3; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11087945};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Temporin subfamily. {ECO:0000255}.
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DR   EMBL; AM745091; CAN87013.1; -; mRNA.
DR   AlphaFoldDB; A7WNV7; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5000271602"
FT   PEPTIDE         48..60
FT                   /note="Temporin-1PLa"
FT                   /evidence="ECO:0000312|EMBL:CAN87013.1"
FT                   /id="PRO_5000271603"
FT   MOD_RES         60
FT                   /note="Isoleucine amide"
FT                   /evidence="ECO:0000269|PubMed:11087945"
SQ   SEQUENCE   62 AA;  7129 MW;  F542112628E6FC46 CRC64;
     MFTSKKSLLL LFFLGTINLS LCEEERDADE EERRDDPDEM NVEVEKRFLP LVGKILSGLI
     GK