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MDS_PHYTS
ID   MDS_PHYTS               Reviewed;          67 AA.
AC   A0A1M4BLT1;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   25-MAY-2022, entry version 13.
DE   RecName: Full=Medusin-PT {ECO:0000303|PubMed:28469603, ECO:0000312|EMBL:SBO46661.1};
DE   Flags: Precursor;
OS   Phyllomedusa tarsius (Brownbelly leaf frog) (Phyllomedusa tarsia).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=306084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-66, FUNCTION, SYNTHESIS
RP   OF 49-66, AMIDATION AT LEU-66, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   PRO-54 AND THR-58.
RC   TISSUE=Skin secretion;
RX   PubMed=28469603; DOI=10.3389/fmicb.2017.00628;
RA   Gao Y., Wu D., Wang L., Lin C., Ma C., Xi X., Zhou M., Duan J.,
RA   Bininda-Emonds O.R.P., Chen T., Shaw C.;
RT   "Targeted modification of a novel amphibian antimicrobial peptide from
RT   Phyllomedusa tarsius to enhance its activity against MRSA and microbial
RT   biofilm.";
RL   Front. Microbiol. 8:628-628(2017).
CC   -!- FUNCTION: Antimicrobial peptide with activity against Gram-positive
CC       bacteria S.epidermidis ATCC 12228 (MIC=50 uM) and S.aureus (MIC=64
CC       ug/ml and MBC=128 ug/ml) (PubMed:28469603) (By similarity). Not active
CC       against some Gram-positive bacteria (methicillin-resistant S.aureus
CC       (MRSA), E.faecalis), Gram-negative bacterium E.coli ATCC 25922 and
CC       fungus C.albicans at concentrations up to 100 uM (PubMed:28469603) (By
CC       similarity). Can only slightly inhibit the formation of biofilm by
CC       S.aureus (minimal biofilm inhibitionconcentration MBIC=512 ug/ml,
CC       minimal biofilm eradication concentration MBEC>512 ug/ml)
CC       (PubMed:28469603). Has an anti-inflammatory effect, since it inhibits
CC       the production of the pro-inflammatory cytokines TNF-alpha and IL-1beta
CC       (By similarity). Has high activity of stimulation of insulin release,
CC       which may protect the species from being eaten by predators by causing
CC       fatal hypoglycemia (By similarity). Is not cytotoxic to cancer line
CC       cells (By similarity). Shows very low hemolysis on horse erythrocytes
CC       and moderate hemolysis on mouse erythrocytes (PubMed:28469603) (By
CC       similarity). {ECO:0000250|UniProtKB:C0HLE1,
CC       ECO:0000269|PubMed:28469603}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28469603}. Target
CC       cell membrane.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:28469603}.
CC   -!- PTM: In the synthetic mutant medusin-PT1a [T58K], the Leu-50 has been
CC       modified in a D-amino acid. In medusin-PT1a, there is an increase in
CC       antimicrobial activity, and an increase in hemolytic activity. It is
CC       more potent against S.aureus and gains activity against MRSA,
CC       E.faecalis, E.coli, P.aeruginosa and C.albicans. There is an important
CC       increase in both biofilm inhibition and biofilm eradication.
CC       {ECO:0000269|PubMed:28469603}.
CC   -!- MISCELLANEOUS: The primary structure of this peptide is identical to
CC       that of Medusin-TR1 (AC C0HLE1). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Medusin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=02995";
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DR   EMBL; LT591889; SBO46661.1; -; mRNA.
DR   AlphaFoldDB; A0A1M4BLT1; -.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; 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; Fungicide;
KW   Immunity; Innate immunity; Membrane; Secreted; Signal;
KW   Target cell membrane; Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..48
FT                   /evidence="ECO:0000305|PubMed:28469603"
FT                   /id="PRO_0000449998"
FT   PEPTIDE         49..66
FT                   /note="Medusin-PT"
FT                   /evidence="ECO:0000269|PubMed:28469603"
FT                   /id="PRO_5012815711"
FT   REGION          25..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         66
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:28469603"
FT   MUTAGEN         54
FT                   /note="P->K: In medusin-PT2; increase in antimicrobial
FT                   activity against Gram-positive bacteria and fungi, and
FT                   increase in hemolytic activity (is more potent against
FT                   S.aureus and gains activity against MRSA, E.faecalis, and
FT                   C.albicans. No change against E.coli and P.aeruginosa.
FT                   Important increase in biofilm inhibition and small increase
FT                   in biofilm eradication)."
FT   MUTAGEN         58
FT                   /note="T->K: In medusin-PT1; increase in antimicrobial
FT                   activity, and increase in hemolytic activity (is more
FT                   potent against S.aureus and gains activity against MRSA,
FT                   E.faecalis, E.coli and C.albicans. No change against
FT                   P.aeruginosa. Important increase in both biofilm inhibition
FT                   and biofilm eradication). In medusin-PT1a; increase in
FT                   antimicrobial activity, and increase in hemolytic activity
FT                   (is more potent against S.aureus and gains activity against
FT                   MRSA, E.faecalis, E.coli, P.aeruginosa and C.albicans.
FT                   Important increase in both biofilm inhibition and biofilm
FT                   eradication)."
SQ   SEQUENCE   67 AA;  7696 MW;  D781C3379F53B0DF CRC64;
     MAFLKKSLFL VFFLGFVSLS ICEEEKRETD EKENEQEDDR EERSEEKRLL GMIPVAITAI
     SALSKLG
 
 
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