DRS2_PHYTS
ID DRS2_PHYTS Reviewed; 28 AA.
AC P84922;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Dermaseptin-2 {ECO:0000303|Ref.1};
DE Short=DStar 02 {ECO:0000303|Ref.1};
OS Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=306084;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, AND AMIDATION AT GLN-28.
RC TISSUE=Skin secretion;
RA Prates M.V., Jardim D.P., Silva L.P., Gordo M., Leite J.R.S.A.,
RA Figueredo R.C.R., Amaral A.C., Felipe M.S.S., Bloch C. Jr.;
RT "Dermaseptins and phylloseptins from Phyllomedusa tarsius (Amphibia).";
RL Submitted (AUG-2006) to UniProtKB.
CC -!- FUNCTION: Antimicrobial peptide with activity against the Gram-positive
CC bacterium S.aureus, and the Gram-negative bacteria E.coli and
CC P.aeruginosa (Ref.1). Probably acts by disturbing membrane functions
CC with its amphipathic structure (By similarity). Has an activity of
CC stimulation of insulin release, which may protect the species from
CC being eaten by predators by causing fatal hypoglycemia (By similarity).
CC Has hemolytic activity (60% hemolysis at 128 ug/ml) (Ref.1).
CC {ECO:0000250|UniProtKB:C0HLC4, ECO:0000250|UniProtKB:P81486,
CC ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=2996.67; Mass_error=0.1; Method=MALDI;
CC Evidence={ECO:0000269|Ref.1};
CC -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC that of Insulin-releasing peptide from Phyllomedusa trinitatis (AC
CC C0HLC4), and Dermaseptin-B4 from Phyllomedusa bicolor (AC P81486).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000255}.
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DR AlphaFoldDB; P84922; -.
DR SMR; P84922; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR022731; Dermaseptin.
DR Pfam; PF12121; DD_K; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW Direct protein sequencing; Hemolysis; Secreted.
FT PEPTIDE 1..28
FT /note="Dermaseptin-2"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000376034"
FT MOD_RES 28
FT /note="Glutamine amide"
FT /evidence="ECO:0000269|Ref.1"
SQ SEQUENCE 28 AA; 2999 MW; C1F70922D9A57A69 CRC64;
ALWKDILKNV GKAAGKAVLN TVTDMVNQ