LES_RANLE
ID LES_RANLE Reviewed; 13 AA.
AC P0DTV3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 12-AUG-2020, entry version 2.
DE RecName: Full=Lesueurin {ECO:0000303|PubMed:11784303};
OS Ranoidea lesueuri (Lesueur's frog) (Litoria lesueurii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Litoria.
OX NCBI_TaxID=95134;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AMIDATION AT ALA-13, AND SYNTHESIS.
RC TISSUE=Skin secretion;
RX PubMed=11784303; DOI=10.1046/j.0014-2956.2002.02630.x;
RA Doyle J., Llewellyn L.E., Brinkworth C.S., Bowie J.H., Wegener K.L.,
RA Rozek T., Wabnitz P.A., Wallace J.C., Tyler M.J.;
RT "Amphibian peptides that inhibit neuronal nitric oxide synthase. Isolation
RT of lesuerin from the skin secretion of the Australian stony creek frog
RT Litoria lesueuri.";
RL Eur. J. Biochem. 269:100-109(2002).
CC -!- FUNCTION: Has no antimicrobial activity (PubMed:11784303). Inhibits the
CC formation of NO by neuronal nitric oxide synthase (nNOS) at micromolar
CC concentrations (PubMed:11784303). Acts by a non-competitive mechanism,
CC probably by binding to calcium/calmodulin and as a consequence blocking
CC calmodulin attachment to nNOS (PubMed:11784303). In vitro, does not
CC exhibit cytotoxicity towards 60 human tumor lines (PubMed:11784303).
CC {ECO:0000269|PubMed:11784303}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11784303}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC {ECO:0000305|PubMed:11784303}.
CC -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Amidation; Amphibian defense peptide; Calmodulin-binding;
KW Direct protein sequencing; Secreted.
FT PEPTIDE 1..13
FT /note="Lesueurin"
FT /evidence="ECO:0000269|PubMed:11784303"
FT /id="PRO_0000450232"
FT MOD_RES 13
FT /note="Alanine amide"
FT /evidence="ECO:0000269|PubMed:11784303"
SQ SEQUENCE 13 AA; 1354 MW; 5BBBC91A49583337 CRC64;
GLLDILKKVG KVA