ID   DRS5_AGASP              Reviewed;          75 AA.
AC   A0A5P9K5G4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   25-MAY-2022, entry version 9.
DE   RecName: Full=Dermaseptin-SP5 {ECO:0000303|PubMed:31671555};
DE            Short=DRS-SP5 {ECO:0000303|PubMed:31671555};
DE   Flags: Precursor;
OS   Agalychnis spurrelli (Gliding leaf frog) (Agalychnis litodryas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Agalychnis.
OX   NCBI_TaxID=317303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP   SYNTHESIS OF 46-72, SUBCELLULAR LOCATION, AND AMIDATION AT PRO-72.
RC   TISSUE=Skin secretion;
RX   PubMed=31671555; DOI=10.3390/biom9110667;
RA   Proano-Bolanos C., Blasco-Zuniga A., Almeida J.R., Wang L.,
RA   Llumiquinga M.A., Rivera M., Zhou M., Chen T., Shaw C.;
RT   "Unravelling the skin secretion peptides of the gliding leaf frog,
RT   Agalychnis spurrelli (Hylidae).";
RL   Biomolecules 9:1-20(2019).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SYNTHESIS OF 46-73, IDENTIFICATION BY
RP   MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Skin secretion;
RX   PubMed=31422479; DOI=10.1007/s00894-019-4141-1;
RA   Cuesta S., Gallegos F., Arias J., Pilaquinga F., Blasco-Zuniga A.,
RA   Proano-Bolanos C., Rivera M., Meneses L.;
RT   "Molecular modeling of four dermaseptin-related peptides of the gliding
RT   tree frog Agalychnis spurrelli.";
RL   J. Mol. Model. 25:260-260(2019).
CC   -!- FUNCTION: Antimicrobial peptide with weak activity against Gram-
CC       positive and Gram-negative bacteria and fungi (PubMed:31671555,
CC       PubMed:31422479). Has been tested against E.coli (MIC=96.06-256 uM),
CC       S.aureus (MIC>192.12 uM), K.pneumoniae (MIC>189.00 uM) and C.albicans
CC       (MIC=384.24-1024 uM) (PubMed:31671555, PubMed:31422479). Probably acts
CC       by disturbing membrane functions with its alpha-helical amphipathic
CC       structure (Probable). May penetrate bacterial membranes, but stay at
CC       the mammalian membrane surface (Probable). Does not show hemolytic
CC       activity (PubMed:31671555). Does not interact at all with cardiolipin
CC       (Probable). {ECO:0000269|PubMed:31422479, ECO:0000269|PubMed:31671555,
CC       ECO:0000305|PubMed:31422479}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31422479,
CC       ECO:0000269|PubMed:31671555}. Target cell membrane
CC       {ECO:0000250|UniProtKB:P31107}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:31671555}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Dermaseptin subfamily. {ECO:0000305}.
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DR   EMBL; MK532483; QFU19633.1; -; mRNA.
DR   AlphaFoldDB; A0A5P9K5G4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; 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; Cleavage on pair of basic residues; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..45
FT                   /evidence="ECO:0000305|PubMed:31671555"
FT                   /id="PRO_0000449992"
FT   PEPTIDE         46..72
FT                   /note="Dermaseptin-SP5"
FT                   /evidence="ECO:0000305|PubMed:31671555"
FT                   /id="PRO_0000449993"
FT   PROPEP          74..75
FT                   /evidence="ECO:0000305|PubMed:31671555"
FT                   /id="PRO_0000449994"
FT   REGION          26..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="Proline amide"
FT                   /evidence="ECO:0000305|PubMed:31671555"
SQ   SEQUENCE   75 AA;  8342 MW;  E2D21630E906B36C CRC64;
     MAFLKKSLFL VLFLGLVSLS MCEEEKRENE VEEEQEDDEQ SELRRSLRSS IKDMAAAAGR
     AALNAVNGIV NPGEQ