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PLS3_PITNO
ID   PLS3_PITNO              Reviewed;          19 AA.
AC   C0HKQ0;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Phylloseptin-N3 {ECO:0000305};
DE            Short=PLS-N3 {ECO:0000305};
DE   AltName: Full=Phylloseptin-8 {ECO:0000303|PubMed:24113627};
DE            Short=PS-8 {ECO:0000250|UniProtKB:P85883};
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:0000303|PubMed:24113627};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   AMIDATION AT PHE-19.
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)=0.46 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:P85882, ECO:0000269|PubMed:24113627}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24113627}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000305|PubMed:24113627}.
CC   -!- MASS SPECTROMETRY: Mass=2012.44; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:24113627};
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=00954";
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DR   AlphaFoldDB; C0HKQ0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted.
FT   PEPTIDE         1..19
FT                   /note="Phylloseptin-N3"
FT                   /evidence="ECO:0000269|PubMed:24113627"
FT                   /id="PRO_0000441009"
FT   MOD_RES         19
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:24113627"
SQ   SEQUENCE   19 AA;  2013 MW;  F4A1C707B26C8FD1 CRC64;
     FLSLIPTAIN AVSALAKHF
 
 
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