DMS1_PITNO
ID DMS1_PITNO Reviewed; 73 AA.
AC J7H8J4;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 26.
DE RecName: Full=Dermaseptin-1 {ECO:0000303|PubMed:24113627};
DE Flags: Precursor;
OS Pithecopus nordestinus (Northeastern Brazilian leaf frog) (Phyllomedusa
OS nordestina).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Pithecopus.
OX NCBI_TaxID=2034992 {ECO:0000312|EMBL:AFP89761.1};
RN [1] {ECO:0000312|EMBL:AFP89761.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin {ECO:0000303|PubMed:23159791};
RX PubMed=23159791; DOI=10.1016/j.toxicon.2012.10.016;
RA Neiva M., Vargas D.C., Conceicao K., Radis-Baptista G., Assakura M.T.,
RA Jared C., Hayashi M.A.;
RT "Gene expression analysis by ESTs sequencing of the Brazilian frog
RT Phyllomedusa nordestina skin glands.";
RL Toxicon 61:139-150(2013).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 46-70, FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND AMIDATION AT LEU-70.
RC TISSUE=Skin secretion {ECO:0000303|PubMed:24113627};
RX PubMed=24113627; DOI=10.1016/j.exppara.2013.09.016;
RA Pinto E.G., Pimenta D.C., Antoniazzi M.M., Jared C., Tempone A.G.;
RT "Antimicrobial peptides isolated from Phyllomedusa nordestina (Amphibia)
RT alter the permeability of plasma membrane of Leishmania and Trypanosoma
RT cruzi.";
RL Exp. Parasitol. 135:655-660(2013).
CC -!- FUNCTION: Has antiparasitic activity against trypomastigote form of
CC T.cruzi (IC(50)=0.68 uM) in vitro but not against L.infantum
CC (PubMed:24113627). Probably acts by permeabilizing cell membranes
CC (PubMed:24113627). In vitro, shows no cytotoxicity against macrophages
CC (PubMed:24113627). Has antibacterial activity (By similarity).
CC {ECO:0000250|UniProtKB:Q1EJP5, ECO:0000269|PubMed:24113627}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC ECO:0000269|PubMed:24113627}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:23159791}.
CC -!- MASS SPECTROMETRY: Mass=2410.88; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:24113627};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Dermaseptin subfamily. {ECO:0000305}.
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DR EMBL; JX127159; AFP89761.1; -; mRNA.
DR AlphaFoldDB; J7H8J4; -.
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 InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF12121; DD_K; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..43
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:24113627"
FT /id="PRO_0000441004"
FT PEPTIDE 46..70
FT /note="Dermaseptin-1"
FT /evidence="ECO:0000269|PubMed:24113627"
FT /id="PRO_0000441005"
FT PROPEP 72..73
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:24113627"
FT /id="PRO_0000441006"
FT REGION 25..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:24113627"
SQ SEQUENCE 73 AA; 8005 MW; 8A33590B26E8B137 CRC64;
MAFLKKSIFL ALFLGMVSLS ICEEEKRENE GEEEQEDDEQ SEMKRGLWST IKNVGKEAAI
AAGKAALGAL GEQ