DRS1_PHYTB
ID DRS1_PHYTB Reviewed; 28 AA.
AC C0HLC4;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 25-MAY-2022, entry version 9.
DE RecName: Full=Dermaseptin-TR1 {ECO:0000303|PubMed:18644413};
DE Short=DRS-TR1 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Dermaseptin-2.1TR {ECO:0000303|PubMed:29980138};
DE AltName: Full=Insulin-releasing peptide {ECO:0000303|PubMed:15257102};
DE Short=IRP {ECO:0000303|PubMed:15257102};
OS Phyllomedusa trinitatis (Trinidad leaf frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=332092;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RX PubMed=15257102; DOI=10.1097/00006676-200408000-00005;
RA Marenah L., McClean S., Flatt P.R., Orr D.F., Shaw C., Abdel-Wahab Y.H.;
RT "Novel insulin-releasing peptides in the skin of Phyllomedusa trinitatis
RT frog include 28 amino acid peptide from dermaseptin BIV precursor.";
RL Pancreas 29:110-115(2004).
RN [2]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RX PubMed=29980138; DOI=10.1016/j.cbd.2018.06.006;
RA Mechkarska M., Coquet L., Leprince J., Auguste R.J., Jouenne T.,
RA Mangoni M.L., Conlon J.M.;
RT "Peptidomic analysis of the host-defense peptides in skin secretions of the
RT Trinidadian leaf frog Phyllomedusa trinitatis (Phyllomedusidae).";
RL Comp. Biochem. Physiol. 28:72-79(2018).
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: Stimulates insulin release (PubMed:15257102). This activity
CC may protect the species from being eaten by predators by causing fatal
CC hypoglycemia (PubMed:15257102). Possesses a potent antimicrobial
CC activity against Gram-positive and Gram-negative bacteria (By
CC similarity). Probably acts by disturbing membrane functions with its
CC amphipathic structure (By similarity). Has hemolytic activity (By
CC similarity). {ECO:0000250|UniProtKB:P81486,
CC ECO:0000250|UniProtKB:P84922, ECO:0000269|PubMed:15257102}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15257102,
CC ECO:0000269|PubMed:29980138}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:15257102, ECO:0000305|PubMed:29980138}.
CC -!- MASS SPECTROMETRY: Mass=2996.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15257102};
CC -!- MASS SPECTROMETRY: Mass=2997.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:29980138};
CC -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC that of Dermaseptin-B4 from Phyllomedusa bicolor (AC P81486), and
CC Dermaseptin-2 from P.tarsius (AC P84922). However, this peptide is not
CC amidated, in contrast to the two mentionned peptides. {ECO:0000305}.
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=00163";
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DR AlphaFoldDB; C0HLC4; -.
DR SMR; C0HLC4; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR Pfam; PF12121; DD_K; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antimicrobial; Direct protein sequencing;
KW Immunity; Innate immunity; Secreted.
FT PEPTIDE 1..28
FT /note="Dermaseptin-TR1"
FT /evidence="ECO:0000269|PubMed:29980138"
FT /id="PRO_0000445211"
SQ SEQUENCE 28 AA; 2999 MW; C1F70922D9A57A69 CRC64;
ALWKDILKNV GKAAGKAVLN TVTDMVNQ