TPI_AMOLO
ID TPI_AMOLO Reviewed; 61 AA.
AC C5H0E0;
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-ALi {ECO:0000303|PubMed:19843479};
DE AltName: Full=Amolopin-2i {ECO:0000312|EMBL:ACA09643.1};
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 LEU-59, AND SYNTHESIS OF
RP 47-59.
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 activity against Gram-positive and
CC Gram-negative bacteria and against fungi (PubMed:19843479). Has been
CC tested against S.aureus (MIC=7.5 ug/mL), B.pumilus (MIC=7.5 ug/mL),
CC B.cereus (MIC=75.0 ug/mL), E.coli (MIC=7.5 ug/mL), B.dysenteriae
CC (MIC=20.0 ug/mL), A.cacoaceticus (MIC=60.0 ug/mL), P.aeruginosa
CC (MIC=5.0 ug/mL) and C.albicans (MIC=5.0 ug/mL) (PubMed:19843479). Also
CC shows a weak hemolytic activity (PubMed:19843479).
CC {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=01936";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU311553; ACA09643.1; -; mRNA.
DR AlphaFoldDB; C5H0E0; -.
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_0000450009"
FT PEPTIDE 47..59
FT /note="Temporin-ALi"
FT /evidence="ECO:0000305|PubMed:19843479"
FT /id="PRO_5002950381"
FT MOD_RES 59
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:19843479"
SQ SEQUENCE 61 AA; 7093 MW; CC075176438C0AB3 CRC64;
MFPLKKSLLL LFFLATINLS LCEQERNAEE ERRDEPDERN AEVEKRFFPI VGKLLSGLLG
K