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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}.
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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
 
 
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