PLEA1_NIDPL
ID PLEA1_NIDPL Reviewed; 69 AA.
AC A8DY01; A8DY00; A8DY02; A8DY03; A8DY04; A8DY09; A8DY10; A8DY15;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Pleurain-A1;
DE Flags: Precursor;
OS Nidirana pleuraden (Yunnan pond frog) (Babina pleuraden).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Nidirana.
OX NCBI_TaxID=369511;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 44-69, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND VARIANT
RP SER-7.
RC TISSUE=Skin, and Skin secretion;
RX PubMed=17764786; DOI=10.1016/j.peptides.2007.07.020;
RA Wang X., Song Y., Li J., Liu H., Xu X., Lai R., Zhang K.;
RT "A new family of antimicrobial peptides from skin secretions of Rana
RT pleuraden.";
RL Peptides 28:2069-2074(2007).
CC -!- FUNCTION: Antimicrobial peptide. Has activity against the Gram-positive
CC bacterium S.aureus ATCC2592 (MIC=15 ug/ml), the Gram-negative bacteria
CC E.coli ATCC25922 (MIC=60 ug/ml), B.dysenteriae (MIC=120 ug/ml),
CC H.pylori NTCT11637 (MIC=30 ug/ml), and the fungus C.albicans ATCC2002
CC (MIC=30 ug/ml). Has little hemolytic activity on rabbit red blood
CC cells. {ECO:0000269|PubMed:17764786}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17764786}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000269|PubMed:17764786}.
CC -!- MASS SPECTROMETRY: Mass=3048.5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:17764786};
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC Pleurain subfamily. {ECO:0000305}.
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DR EMBL; EF613243; ABU88478.1; -; mRNA.
DR EMBL; EF613244; ABU88479.1; -; mRNA.
DR EMBL; EF613245; ABU88480.1; -; mRNA.
DR EMBL; EF613246; ABU88481.1; -; mRNA.
DR EMBL; EF613247; ABU88482.1; -; mRNA.
DR EMBL; EF613248; ABU88483.1; -; mRNA.
DR EMBL; EF613249; ABU88484.1; -; mRNA.
DR EMBL; EF613250; ABU88485.1; -; mRNA.
DR EMBL; EF613251; ABU88486.1; -; mRNA.
DR EMBL; EF613252; ABU88487.1; -; mRNA.
DR EMBL; EF613253; ABU88488.1; -; mRNA.
DR EMBL; EF613254; ABU88489.1; -; mRNA.
DR EMBL; EF613255; ABU88490.1; -; mRNA.
DR EMBL; EF613256; ABU88491.1; -; mRNA.
DR EMBL; EF613257; ABU88492.1; -; mRNA.
DR EMBL; EF613258; ABU88493.1; -; mRNA.
DR EMBL; EF613259; ABU88494.1; -; mRNA.
DR AlphaFoldDB; A8DY01; -.
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:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR Pfam; PF03032; FSAP_sig_propep; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..43
FT /evidence="ECO:0000269|PubMed:17764786"
FT /id="PRO_0000313998"
FT PEPTIDE 44..69
FT /note="Pleurain-A1"
FT /id="PRO_0000313999"
FT DISULFID 63..69
FT VARIANT 7
FT /note="T -> S"
FT /evidence="ECO:0000269|PubMed:17764786"
FT CONFLICT 3
FT /note="T -> P (in Ref. 1; ABU88487)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="T -> I (in Ref. 1; ABU88481)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="L -> S (in Ref. 1; ABU88478)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="F -> V (in Ref. 1; ABU88493)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="C -> R (in Ref. 1; ABU88493)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="R -> G (in Ref. 1; ABU88482)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="D -> V (in Ref. 1; ABU88488)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="G -> E (in Ref. 1; ABU88493)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 69 AA; 8086 MW; E6193B39CA38482F CRC64;
MFTLKKTLLL LFFLGTISIS LCKQERDADE DDGRKMTEEE VKRSIITMTK EAKLPQLWKQ
IACRLYNTC