DRS3_AGADC
ID DRS3_AGADC Reviewed; 80 AA.
AC O93453;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Dermaseptin-DA3 {ECO:0000303|PubMed:18644413};
DE Short=DRS-DA3 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Dermaseptin PD-3-3 {ECO:0000303|PubMed:9774745};
DE Flags: Precursor;
OS Agalychnis dacnicolor (Giant mexican leaf frog) (Pachymedusa dacnicolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Agalychnis.
OX NCBI_TaxID=75988;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT LEU-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=0968";
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; AJ005191; CAA06428.1; -; mRNA.
DR AlphaFoldDB; O93453; -.
DR SMR; O93453; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF12121; DD_K; 1.
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..42
FT /evidence="ECO:0000305"
FT /id="PRO_0000007081"
FT PEPTIDE 45..77
FT /note="Dermaseptin-DA3"
FT /evidence="ECO:0000305|PubMed:9774745"
FT /id="PRO_0000007082"
FT PROPEP 79..80
FT /evidence="ECO:0000305"
FT /id="PRO_0000007083"
FT REGION 24..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Leucine amide"
FT /evidence="ECO:0000305|PubMed:9774745"
SQ SEQUENCE 80 AA; 8717 MW; 3664B33E58241EDA CRC64;
MAFLKKSLFL VLFLGLVSLS ICEEKRENED EEEQEDDEQS EEKRGMWSKI KNAGKAAAKA
SKKAAGKAAL GAVSEALGEQ