ID   E2ALB_AMOLO             Reviewed;          76 AA.
AC   C5H0D5;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=Esculentin-2-ALb {ECO:0000303|PubMed:19843479};
DE   AltName: Full=Amolopin-9b {ECO:0000312|EMBL:ACA09638.1};
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 40-76, FUNCTION, MASS
RP   SPECTROMETRY, DISULFIDE BOND, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin, and Skin secretion;
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=1.25 ug/mL), B.pumilus (MIC=2.5 ug/mL),
CC       B.cereus (MIC=7.5 ug/mL), E.coli (MIC=12.5 ug/mL), B.dysenteriae
CC       (MIC=7.5 ug/mL), A.cacoaceticus (MIC=12.5 ug/mL), P.aeruginosa
CC       (MIC=50.0 ug/mL) and C.albicans (MIC=2.5 ug/mL) (PubMed:19843479). Also
CC       shows a weak hemolytic activity (PubMed:19843479).
CC       {ECO:0000269|PubMed:19843479}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19843479}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:19843479}.
CC   -!- MASS SPECTROMETRY: Mass=3868.57; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19843479};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Esculentin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=01930";
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DR   EMBL; EU311548; ACA09638.1; -; mRNA.
DR   AlphaFoldDB; C5H0D5; -.
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; IPR012521; Antimicrobial_frog_2.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF08023; Antimicrobial_2; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Immunity; Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..39
FT                   /evidence="ECO:0000305|PubMed:19843479"
FT                   /id="PRO_0000450002"
FT   CHAIN           40..76
FT                   /note="Esculentin-2-ALb"
FT                   /evidence="ECO:0000269|PubMed:19843479"
FT                   /id="PRO_5002950379"
FT   DISULFID        70..76
FT                   /evidence="ECO:0000269|PubMed:19843479"
SQ   SEQUENCE   76 AA;  8293 MW;  6D541EA9DBA96DCA CRC64;
     MFTMKKSLLL LFFLGTISLS LCEEERSADE DDGEKGVKRG IFSLIKTAAK FVGKNLLKQA
     GKAGVEHLAC KANNQC