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PLS31_PHYTB
ID   PLS31_PHYTB             Reviewed;          19 AA.
AC   C0HLD8;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Phylloseptin-3.1TR {ECO:0000303|PubMed:29980138};
DE            Short=PLS-3.1TR {ECO:0000305};
DE   AltName: Full=Phylloseptin-3.3TR {ECO:0000303|PubMed:29980138};
OS   Phyllomedusa trinitatis (Trinidad leaf frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Phyllomedusinae;
OC   Phyllomedusa.
OX   NCBI_TaxID=332092;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SYNTHESIS, SUBCELLULAR LOCATION, MASS
RP   SPECTROMETRY, AND AMIDATION AT LEU-19.
RC   TISSUE=Skin secretion;
RX   PubMed=29980138; DOI=10.1016/j.cbd.2018.06.006;
RA   Mechkarska M., Coquet L., Leprince J., Auguste R.J., Jouenne T.,
RA   Mangoni M.L., Conlon J.M.;
RT   "Peptidomic analysis of the host-defense peptides in skin secretions of the
RT   Trinidadian leaf frog Phyllomedusa trinitatis (Phyllomedusidae).";
RL   Comp. Biochem. Physiol. 28:72-79(2018).
RN   [2]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=30734396; DOI=10.1002/psc.3153;
RA   Pantic J., Guilhaudis L., Musale V., Attoub S., Lukic M.L., Mechkarska M.,
RA   Conlon J.M.;
RT   "Immunomodulatory, insulinotropic, and cytotoxic activities of
RT   phylloseptins and plasticin-TR from the Trinidanian leaf frog Phyllomedusa
RT   trinitatis.";
RL   J. Pept. Sci. 25:E3153-E3153(2019).
CC   -!- FUNCTION: The amidated Phylloseptin-3.1TR has weak antimicrobial
CC       activity against Gram-negative bacterium E.coli ATCC 25922 (MIC=100
CC       uM), Gram-positive bacterium S.epidermidis ATCC 12228 (MIC=12.5 uM) and
CC       against fungus C.albicans ATCC 24433 (MIC=25 uM) (PubMed:29980138). Has
CC       an anti-inflammatory effect, since it inhibits the production of the
CC       pro-inflammatory cytokines TNF-alpha, and induces the production of the
CC       anti-inflammatory cytokine IL-10 (PubMed:30734396). Has an activity of
CC       stimulation of insulin release, which may protect the species from
CC       being eaten by predators by causing fatal hypoglycemia
CC       (PubMed:30734396). Is cytotoxic to cancer line cells (PubMed:30734396).
CC       Shows moderate hemolysis on mouse erythrocytes (LC(50)=12 uM)
CC       (PubMed:30734396). {ECO:0000269|PubMed:29980138,
CC       ECO:0000269|PubMed:30734396}.
CC   -!- FUNCTION: The non-amidated Phylloseptin-3.3TR has weak antimicrobial
CC       activity against fungus C.albicans ATCC 24433 (MIC=100 uM). Not active
CC       against Gram-negative bacterium E.coli ATCC 25922 and Gram-positive
CC       bacterium S.epidermidis ATCC 12228 at concentrations up to 100 uM
CC       (PubMed:29980138). Has an anti-inflammatory effect, since it inhibits
CC       the production of the pro-inflammatory cytokines TNF-alpha and IL-1
CC       beta, and induces the production of the anti-inflammatory cytokine IL-
CC       10 (PubMed:30734396). Has high activity of stimulation of insulin
CC       release, which may protect the species from being eaten by predators by
CC       causing fatal hypoglycemia (PubMed:30734396). Is not cytotoxic to
CC       cancer line cells (PubMed:30734396). Shows very low hemolysis on mouse
CC       erythrocytes (LC(50)=340 uM) (PubMed:30734396).
CC       {ECO:0000269|PubMed:29980138, ECO:0000269|PubMed:30734396}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:29980138}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:29980138}.
CC   -!- PTM: Phylloseptin-3.1TR is amidated, whereas Phylloseptin-3.3TR is the
CC       name given to the non-amidated form. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=2049.3; Method=MALDI; Note=amidated
CC       Phylloseptin-3.1TR.; Evidence={ECO:0000269|PubMed:29980138};
CC   -!- MASS SPECTROMETRY: Mass=2050.1; Method=MALDI; Note=non-amidated
CC       Phylloseptin-3.3TR.; Evidence={ECO:0000269|PubMed:29980138};
CC   -!- PHARMACEUTICAL: Phylloseptin-3.3TR may represent a template for the
CC       design of potent anti-inflammatory agents for use in the control
CC       hyperinflammatory phase of sepsis, since it has the ability to inhibit
CC       production of TNF-alpha and IL-1 beta and to stimulate IL-10 production
CC       by peritoneal cells coupled with very low toxicity against mouse
CC       erythrocytes and A549 human lung adenocarcinoma cells.
CC       {ECO:0000305|PubMed:30734396}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Phylloseptin subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=02992";
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=02994";
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DR   AlphaFoldDB; C0HLD8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial; Cytolysis;
KW   Direct protein sequencing; Fungicide; Hemolysis; Immunity; Innate immunity;
KW   Pharmaceutical; Secreted.
FT   PEPTIDE         1..19
FT                   /note="Phylloseptin-3.1TR"
FT                   /evidence="ECO:0000269|PubMed:29980138"
FT                   /id="PRO_0000445198"
FT   MOD_RES         19
FT                   /note="Leucine amide; in form Phylloseptin-3.1TR"
FT                   /evidence="ECO:0000269|PubMed:29980138"
SQ   SEQUENCE   19 AA;  2051 MW;  55BBF25A92D7F7A2 CRC64;
     FFSMIPKIAT GIASLVKNL
 
 
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