ID   DRS5_AGAAN              Reviewed;          80 AA.
AC   O93226;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Dermaseptin-A5 {ECO:0000305|PubMed:18644413};
DE            Short=DRS-A5 {ECO:0000305|PubMed:18644413};
DE   AltName: Full=Dermaseptin AA-3-6 {ECO:0000303|PubMed:9774745};
DE   AltName: Full=Dermaseptin-A4 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-A4 {ECO:0000303|PubMed:18644413};
DE   Flags: Precursor;
OS   Agalychnis annae (Blue-sided leaf frog) (Phyllomedusa annae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=75990;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT VAL-77.
RC   TISSUE=Skin;
RX   PubMed=9774745; DOI=10.1016/s0167-4838(98)00202-7;
RA   Wechselberger C.;
RT   "Cloning of cDNAs encoding new peptides of the dermaseptin-family.";
RL   Biochim. Biophys. Acta 1388:279-283(1998).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=18644413; DOI=10.1016/j.peptides.2008.06.017;
RA   Amiche M., Ladram A., Nicolas P.;
RT   "A consistent nomenclature of antimicrobial peptides isolated from frogs of
RT   the subfamily Phyllomedusinae.";
RL   Peptides 29:2074-2082(2008).
CC   -!- FUNCTION: Possesses a potent antimicrobial activity against Gram-
CC       positive and Gram-negative bacteria. Probably acts by disturbing
CC       membrane functions with its amphipathic structure (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:9774745}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:9774745}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=0967";
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DR   EMBL; AJ005188; CAA06425.1; -; mRNA.
DR   AlphaFoldDB; O93226; -.
DR   SMR; O93226; -.
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; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..43
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000007073"
FT   PEPTIDE         46..77
FT                   /note="Dermaseptin-A5"
FT                   /evidence="ECO:0000305|PubMed:9774745"
FT                   /id="PRO_0000007074"
FT   PROPEP          79..80
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000007075"
FT   REGION          24..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         77
FT                   /note="Valine amide"
FT                   /evidence="ECO:0000305|PubMed:9774745"
SQ   SEQUENCE   80 AA;  8817 MW;  DB13FD831E7E2140 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEEEKRENE DEEEQEDDEQ SEMKRGMWST IRNVGKSAAK
     AANLPAKAAL GAISEAVGEQ