ID   TPK_AMOLO               Reviewed;          57 AA.
AC   C5H0E2;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Temporin-ALk {ECO:0000303|PubMed:19843479};
DE   AltName: Full=Amolopin-n1 {ECO:0000312|EMBL:ACA09645.1};
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], FUNCTION, AMIDATION AT SER-56, AND SYNTHESIS OF
RP   47-56.
RC   TISSUE=Skin;
RX   PubMed=19843479; DOI=10.1016/j.cbpb.2009.10.003;
RA   Wang M., Wang Y., Wang A., Song Y., Ma D., Yang H., Ma Y., Lai R.;
RT   "Five novel antimicrobial peptides from skin secretions of the frog,
RT   Amolops loloensis.";
RL   Comp. Biochem. Physiol. 155:72-76(2010).
CC   -!- FUNCTION: Antimicrobial peptide with weak activity against Gram-
CC       positive and Gram-negative bacteria and against fungi
CC       (PubMed:19843479). Has been tested against S.aureus (MIC=15.0 ug/mL),
CC       B.pumilus (no activity detected), B.cereus (no activity detected),
CC       E.coli (MIC=30.0 ug/mL), B.dysenteriae (MIC=60.0 ug/mL), A.cacoaceticus
CC       (MIC=75.0 ug/mL), P.aeruginosa (MIC=25.0 ug/mL) and C.albicans
CC       (MIC=15.0 ug/mL) (PubMed:19843479). Also shows a weak hemolytic
CC       activity (PubMed:19843479). {ECO:0000269|PubMed:19843479}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:19843479}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:19843479}.
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=01938";
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DR   EMBL; EU311555; ACA09645.1; -; mRNA.
DR   AlphaFoldDB; C5H0E2; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; 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; Fungicide; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000305|PubMed:19843479"
FT                   /id="PRO_0000450011"
FT   PEPTIDE         47..56
FT                   /note="Temporin-ALk"
FT                   /evidence="ECO:0000305|PubMed:19843479"
FT                   /id="PRO_5005668332"
FT   MOD_RES         56
FT                   /note="Serine amide"
FT                   /evidence="ECO:0000305|PubMed:19843479"
SQ   SEQUENCE   57 AA;  6630 MW;  729E65844C285462 CRC64;
     MFTLKKSLLL LFFLGTINLS LCEQERNAEE ERRDDLGERQ AEVEKRFFPI VGKLLSG