MDS1_PHYSA
ID MDS1_PHYSA Reviewed; 67 AA.
AC F7UI88;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Medusin-S1 {ECO:0000305};
DE Short=MDS-S1 {ECO:0000305};
DE AltName: Full=Phylloseptin-S5 {ECO:0000303|PubMed:23967105};
DE Short=PLS-S6 {ECO:0000303|PubMed:23967105};
DE Flags: Precursor;
OS Phyllomedusa sauvagei (Sauvage's leaf frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC Phyllomedusa.
OX NCBI_TaxID=8395;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-66, FUNCTION, AMIDATION
RP AT LEU-66, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Skin secretion;
RX PubMed=23967105; DOI=10.1371/journal.pone.0070782;
RA Raja Z., Andre S., Piesse C., Sereno D., Nicolas P., Foulon T., Oury B.,
RA Ladram A.;
RT "Structure, antimicrobial activities and mode of interaction with membranes
RT of novel [corrected] phylloseptins from the painted-belly leaf frog,
RT Phyllomedusa sauvagii.";
RL PLoS ONE 8:E70782-E70782(2013).
CC -!- FUNCTION: Antibacterial peptide with moderate activity against the
CC Gram-positive bacteria (S.aureus ATCC 25923, MIC=25 uM), but not
CC against all other bacteria (both Gram-positive and Gram-negative)
CC tested. Does not show activity against fungi, and against Leishmania
CC species (PubMed:23967105). It adopts an alpha-helical structure with
CC very low amphipathicity in membrane environments (Probable).
CC {ECO:0000269|PubMed:23967105, ECO:0000305|PubMed:23967105}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23967105}. Target
CC cell membrane {ECO:0000269|PubMed:23967105}. Note=Forms a helical
CC membrane channel in the target. {ECO:0000305|PubMed:23967105}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000250|UniProtKB:L0P402}.
CC -!- MASS SPECTROMETRY: Mass=1796.14; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:23967105};
CC -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC that of Medusin-PH from Phyllomedusa hypochondrialis (AC L0P402).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Medusin subfamily. {ECO:0000255}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=02176";
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DR EMBL; AM903081; CAP17494.1; -; mRNA.
DR AlphaFoldDB; F7UI88; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Direct protein sequencing; Immunity;
KW Innate immunity; Membrane; Secreted; Signal; Target cell membrane;
KW Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..48
FT /evidence="ECO:0000305|PubMed:23967105"
FT /id="PRO_0000449586"
FT PEPTIDE 49..66
FT /note="Medusin-S1"
FT /evidence="ECO:0000269|PubMed:23967105"
FT /id="PRO_5003362865"
FT REGION 26..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Leucine amide"
FT /evidence="ECO:0000269|PubMed:23967105"
SQ SEQUENCE 67 AA; 7678 MW; D89F6A5D872A7BC8 CRC64;
MSFLKKSLFL VLFLGFVSLS ICEEEKRETE EKENEQEDDR EERSEEKRLL GMIPVAISAI
SALSKLG
