ID   PLR_LITPI               Reviewed;          62 AA.
AC   Q90WP7; P82110;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Peptide leucine arginine;
DE            Short=pLR;
DE   Flags: Precursor;
OS   Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8404;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RA   Farragher S.M., Bjourson A.J., McClean S., Orr D.F., Shaw C.;
RT   "Cloning of cDNAs encoding defensive skin secretion peptides from the
RT   Northern leopard frog (Rana pipiens).";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 44-61, FUNCTION, MASS SPECTROMETRY, DISULFIDE BOND,
RP   CIRCULAR DICHROISM ANALYSIS, SYNTHESIS, AND 3D-STRUCTURE MODELING.
RC   TISSUE=Skin secretion;
RX   PubMed=11099505; DOI=10.1074/jbc.m009680200;
RA   Salmon A.L., Cross L.J.M., Irvine A.E., Lappin T.R.J., Dathe M., Krause G.,
RA   Canning P., Thim L., Beyermann M., Rothemund S., Bienert M., Shaw C.;
RT   "Peptide leucine arginine, a potent immunomodulatory peptide, isolated and
RT   structurally characterized from the skin of the Northern Leopard frog, Rana
RT   pipiens.";
RL   J. Biol. Chem. 276:10145-10152(2001).
RN   [3]
RP   FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=9673585;
RA   Boyer M., van Den Berg H.W., Shaw C., Lynch M., Johnston P.;
RT   "Breast cancer cell lines express specific binding sites for plr, a novel
RT   anti-proliferative peptide from frog skin venom.";
RL   Br. J. Cancer 78:41-41(1998).
RN   [4]
RP   FUNCTION.
RX   PubMed=14636071; DOI=10.1021/bi034521l;
RA   Mangoni M.L., Papo N., Mignogna G., Andreu D., Shai Y., Barra D.,
RA   Simmaco M.;
RT   "Ranacyclins, a new family of short cyclic antimicrobial peptides:
RT   biological function, mode of action and parameters involved in target
RT   specificity.";
RL   Biochemistry 42:14023-14035(2003).
CC   -!- FUNCTION: Mast cell degranulating peptide. Antiproliferative activity
CC       against human breast and ovarian tumor cell lines in vitro. Inhibits
CC       granulopoiesis in rat in vitro. Causes histamine release from rat
CC       peritoneal mast cells in vitro. Has antibacterial activity against
CC       Gram-positive bacteria B.megaterium Bm11, S.lentus and M.luteus, and
CC       antifungal activity against C.tropicalis, C.guiller-mondii and
CC       P.nicotianae spores. Has hemolytic activity. The mature peptide inserts
CC       into the hydrophobic core of the bacterial cell membrane and increases
CC       permeability without disrupting membrane integrity. Probably binds to
CC       the outer membrane surface before aggregating to form transmembrane
CC       pores. {ECO:0000269|PubMed:11099505, ECO:0000269|PubMed:14636071,
CC       ECO:0000269|PubMed:9673585}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC   -!- MASS SPECTROMETRY: Mass=2136; Method=Plasma desorption;
CC       Evidence={ECO:0000269|PubMed:11099505};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000305}.
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DR   EMBL; AJ414584; CAC93861.1; -; mRNA.
DR   PDB; 2M3N; NMR; -; A=44-61.
DR   PDBsum; 2M3N; -.
DR   AlphaFoldDB; Q90WP7; -.
DR   BMRB; Q90WP7; -.
DR   SMR; Q90WP7; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR   GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR032019; Frog_antimicrobial_Ranidae.
DR   Pfam; PF16048; Antimicrobial23; 1.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Fungicide; Hemolysis; Inflammatory response;
KW   Mast cell degranulation; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..41
FT                   /id="PRO_0000003461"
FT   PEPTIDE         44..61
FT                   /note="Peptide leucine arginine"
FT                   /id="PRO_0000003462"
FT   PROPEP          62
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000439058"
FT   DISULFID        48..58
FT                   /evidence="ECO:0000269|PubMed:11099505"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:2M3N"
SQ   SEQUENCE   62 AA;  7113 MW;  C8F7F58849A01A1C CRC64;
     MFTLKKSLLL LFFLGTISSS LCEQERDSDD EDQGEVTEQV VKRLVRGCWT KSYPPKPCFV
     RG