DMS4_PHYBU
ID DMS4_PHYBU Reviewed; 28 AA.
AC P86279;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Dermaseptin DRS-DI4-like peptide {ECO:0000303|Ref.1};
OS Phyllomedusa burmeisteri (Brazilian common walking leaf frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=39413;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RC TISSUE=Skin secretion {ECO:0000269|Ref.1};
RA Conceicao K., Klitzke C.F., Brito R.C., Andrade D.F., Junca F.A.,
RA Biondi I., Lopes-Ferreira M.;
RT "Identification of peptides from Phyllomedusa burmesteri skin secretomics
RT by nano LC MS/MS.";
RL Submitted (APR-2009) to UniProtKB.
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|UniProtKB:P81485}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands. {ECO:0000269|Ref.1}.
CC -!- MASS SPECTROMETRY: Mass=2778.47; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000255}.
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DR AlphaFoldDB; P86279; -.
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 Pfam; PF12121; DD_K; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..28
FT /note="Dermaseptin DRS-DI4-like peptide"
FT /evidence="ECO:0000269|Ref.1"
FT /id="PRO_0000378910"
SQ SEQUENCE 28 AA; 2780 MW; 390C3DCBBEB5ED1B CRC64;
ALWKNMLKGI GKLAGQAALG AVKTLVGA