DRS1_PHYDS
ID DRS1_PHYDS Reviewed; 33 AA.
AC P83638;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Dermaseptin-DI1 {ECO:0000303|PubMed:18644413};
DE Short=DRS-DI1 {ECO:0000303|PubMed:18644413};
DE AltName: Full=Dermadistinctin-K {ECO:0000303|PubMed:10477123};
DE Short=DD-K {ECO:0000303|PubMed:10477123};
OS Phyllomedusa distincta (Monkey frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=164618;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP SPECTROMETRY, CIRCULAR DICHROISM ANALYSIS, AND SYNTHESIS.
RC TISSUE=Skin secretion;
RX PubMed=10477123; DOI=10.1016/s0196-9781(99)00050-9;
RA Batista C.V.F., da Silva L.R., Sebben A., Scaloni A., Ferrara L.,
RA Paiva G.R., Olamendi-Portugal T., Possani L.D., Bloch C. Jr.;
RT "Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta.";
RL Peptides 20:679-686(1999).
RN [2]
RP SYNTHESIS, AND FUNCTION AS AN ANTIPROTOZOAN PROTEIN.
RX PubMed=12379643; DOI=10.1074/jbc.m209289200;
RA Brand G.D., Leite J.R.S.A., Silva L.P., Albuquerque S., Prates M.V.,
RA Azevedo R.B., Carregaro V., Silva J.S., Sa V.C.L., Brandao R.A.,
RA Bloch C. Jr.;
RT "Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta. Anti-
RT Trypanosoma cruzi activity without cytotoxicity to mammalian cells.";
RL J. Biol. Chem. 277:49332-49340(2002).
RN [3]
RP FUNCTION, AND SYNTHESIS.
RX PubMed=17409003; DOI=10.1016/j.cbpa.2007.02.031;
RA Silva L.P., Leite J.R.S.A., Brand G.D., Regis W.B., Tedesco A.C.,
RA Azevedo R.B., Freitas S.M., Bloch C. Jr.;
RT "Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta:
RT liposomes fusion and/or lysis investigated by fluorescence and atomic force
RT microscopy.";
RL Comp. Biochem. Physiol. 151A:329-335(2008).
RN [4]
RP FUNCTION, AND SYNTHESIS.
RX PubMed=17442605; DOI=10.1016/j.cbpa.2007.03.016;
RA Leite J.R.S.A., Brand G.D., Silva L.P., Kuckelhaus S.A.S., Bento W.R.C.,
RA Araujo A.L.T., Martins G.R., Lazzari A.M., Bloch C. Jr.;
RT "Dermaseptins from Phyllomedusa oreades and Phyllomedusa distincta:
RT Secondary structure, antimicrobial activity, and mammalian cell toxicity.";
RL Comp. Biochem. Physiol. 151A:336-343(2008).
RN [5]
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).
RN [6]
RP STRUCTURE BY NMR, AND AMIDATION AT VAL-33.
RX PubMed=19289046; DOI=10.1016/j.bpj.2008.11.063;
RA Verly R.M., de Moraes C.M., Resende J.M., Aisenbrey C., Bemquerer M.P.,
RA Pilo-Veloso D., Valente A.P., Almeida F.C., Bechinger B.;
RT "Structure and membrane interactions of the antibiotic peptide
RT dermadistinctin K by multidimensional solution and oriented 15N and 31P
RT solid-state NMR spectroscopy.";
RL Biophys. J. 96:2194-2203(2009).
CC -!- FUNCTION: Has antibacterial activity against the Gram-positive bacteria
CC S.aureus and E.faecalis, and the Gram-negative bacteria P.aeruginosa
CC and E.coli. Has antiprotozoal activity against T.cruzi. Has antifungal
CC activity against the yeasts C.tropicalis (MIC=10.1 uM),
CC C.guilliermondii (MIC=20.3 uM), C.albicans (MIC=20.3 uM) and C.albicans
CC ATCC 1023 (MIC=10.1 uM). Decreases viability of murine peritoneal
CC cells. Fuses to, and disrupts liposomes. {ECO:0000269|PubMed:10477123,
CC ECO:0000269|PubMed:12379643, ECO:0000269|PubMed:17409003,
CC ECO:0000269|PubMed:17442605}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10477123}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:10477123}.
CC -!- MASS SPECTROMETRY: Mass=3154.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10477123};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000255}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=0966";
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DR PDB; 2JX6; NMR; -; A=1-33.
DR PDB; 2K9B; NMR; -; A=1-33.
DR PDBsum; 2JX6; -.
DR PDBsum; 2K9B; -.
DR AlphaFoldDB; P83638; -.
DR SMR; P83638; -.
DR EvolutionaryTrace; P83638; -.
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 3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW Antimicrobial; Direct protein sequencing; Secreted.
FT PEPTIDE 1..33
FT /note="Dermaseptin-DI1"
FT /evidence="ECO:0000269|PubMed:10477123"
FT /id="PRO_0000044730"
FT MOD_RES 33
FT /note="Valine amide"
FT /evidence="ECO:0000269|PubMed:19289046"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:2JX6"
FT HELIX 8..32
FT /evidence="ECO:0007829|PDB:2JX6"
SQ SEQUENCE 33 AA; 3153 MW; 2A6A282029A47547 CRC64;
GLWSKIKAAG KEAAKAAAKA AGKAALNAVS EAV
