ID   TPA_AMOLO               Reviewed;          64 AA.
AC   A0SN45;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Temporin-ALa {ECO:0000303|PubMed:17000029};
DE   AltName: Full=Amolopin-2a {ECO:0000312|EMBL:ABG72913.1};
DE   Flags: Precursor;
OS   Amolops loloensis (Lolokou Sucker Frog) (Staurois loloensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Amolops.
OX   NCBI_TaxID=318551;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-62, FUNCTION,
RP   SUBCELLULAR LOCATION, AND AMIDATION AT LEU-62.
RC   TISSUE=Skin, and Skin secretion;
RX   PubMed=17000029; DOI=10.1016/j.peptides.2006.08.017;
RA   Lu Y., Li J., Yu H., Xu X., Liang J., Tian Y., Ma D., Lin G., Huang G.,
RA   Lai R.;
RT   "Two families of antimicrobial peptides with multiple functions from skin
RT   of rufous-spotted torrent frog, Amolops loloensis.";
RL   Peptides 27:3085-3091(2006).
CC   -!- FUNCTION: Antimicrobial peptide with activity against Gram-positive and
CC       Gram-negative bacteria and against fungi (PubMed:17000029). Has been
CC       tested against S.aureus (MIC=2.0 ug/mL), E.coli (MIC=3.0 ug/mL),
CC       B.dysenteriae (MIC=1.5 ug/mL), and C.albicans (MIC=6.5 ug/mL)
CC       (PubMed:17000029). Can regulate or mediate antimicrobial response by
CC       stimulating mast cell degranulation (PubMed:17000029). Induces
CC       histamine release (PubMed:17000029). Shows cytotoxicity toward solid
CC       tumor cell line HepG2 (PubMed:17000029). Also shows a weak hemolytic
CC       activity (PubMed:17000029). {ECO:0000269|PubMed:17000029}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17000029}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:17000029}.
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=00863";
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DR   EMBL; DQ673116; ABG72913.1; -; mRNA.
DR   AlphaFoldDB; A0SN45; -.
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.
DR   GO; GO:0045087; P:innate immune response; 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; Cytolysis; Direct protein sequencing;
KW   Fungicide; Hemolysis; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000305|PubMed:17000029"
FT                   /id="PRO_0000449999"
FT   PEPTIDE         47..62
FT                   /note="Temporin-ALa"
FT                   /evidence="ECO:0000269|PubMed:17000029"
FT                   /id="PRO_5002630762"
FT   MOD_RES         62
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:17000029"
SQ   SEQUENCE   64 AA;  7307 MW;  BBD956837E67E243 CRC64;
     MFTLKKSLLL LFFLGTINLS LCEQERNAEE ERRDEPDERN AEVEKRFLPI VGKLLSGLSG
     LLGK