ID   DRS2_PHYDS              Reviewed;          28 AA.
AC   P83639;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Dermaseptin-DI2 {ECO:0000303|PubMed:18644413};
DE            Short=DRS-DI2 {ECO:0000303|PubMed:18644413};
DE   AltName: Full=Dermadistinctin-L {ECO:0000303|PubMed:10477123};
DE            Short=DD L {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).
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=10.9 uM),
CC       C.guilliermondii (MIC=21.8 uM), C.albicans (MIC=21.8 uM) and C.albicans
CC       ATCC 1023 (MIC=10.9 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=2926.6; 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=0958";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P83639; -.
DR   SMR; P83639; -.
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-DI2"
FT                   /evidence="ECO:0000269|PubMed:10477123"
FT                   /id="PRO_0000043637"
SQ   SEQUENCE   28 AA;  2926 MW;  84E71BA9D9A57CDE CRC64;
     ALWKTLLKNV GKAAGKAALN AVTDMVNQ