DRS1_PHYBI
ID DRS1_PHYBI Reviewed; 78 AA.
AC P80282;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Dermaseptin-B1 {ECO:0000303|PubMed:18644413};
DE Short=DRS-B1 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Dermaseptin BI;
DE Flags: Precursor;
OS Phyllomedusa bicolor (Two-colored leaf frog) (Rana bicolor).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=8393;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND AMIDATION AT GLN-75.
RC TISSUE=Skin;
RX PubMed=8074751; DOI=10.1016/s0021-9258(17)32386-4;
RA Amiche M., Ducancel F., Mor A., Boulain J.-C., Menez A., Nicolas P.;
RT "Precursors of vertebrate peptide antibiotics dermaseptin b and
RT adenoregulin have extensive sequence identities with precursors of opioid
RT peptides dermorphin, dermenkephalin, and deltorphins.";
RL J. Biol. Chem. 269:17847-17852(1994).
RN [2]
RP PROTEIN SEQUENCE OF 45-75, AND SUBCELLULAR LOCATION.
RC TISSUE=Skin secretion;
RX PubMed=8306981; DOI=10.1111/j.1432-1033.1994.tb19924.x;
RA Mor A., Nicolas P.;
RT "Isolation and structure of novel defensive peptides from frog skin.";
RL Eur. J. Biochem. 219:145-154(1994).
RN [3]
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 bacteria,
CC fungi and protozoa. Probably acts by disturbing membrane functions with
CC its amphipathic structure.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8306981}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:8306981}.
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=0293";
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DR EMBL; X72387; CAA51080.1; -; mRNA.
DR PIR; A53727; A53727.
DR PIR; B54897; B54897.
DR AlphaFoldDB; P80282; -.
DR TCDB; 1.C.52.1.1; the dermaseptin (dermaseptin) family.
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:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF12121; DD_K; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing; Fungicide;
KW Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..42
FT /evidence="ECO:0000269|PubMed:8306981"
FT /id="PRO_0000007089"
FT PEPTIDE 45..75
FT /note="Dermaseptin-B1"
FT /evidence="ECO:0000269|PubMed:8306981"
FT /id="PRO_0000007090"
FT PROPEP 76..78
FT /evidence="ECO:0000269|PubMed:8306981"
FT /id="PRO_0000007091"
FT MOD_RES 75
FT /note="Glutamine amide"
FT /evidence="ECO:0000305|PubMed:8074751"
SQ SEQUENCE 78 AA; 8707 MW; EB3B6F03058FEC6F CRC64;
MDILKKSLFL VLFLGLVSLS ICEEEKRENE DEEKQDDEQS EMKRAMWKDV LKKIGTVALH
AGKAALGAVA DTISQGEQ
