ID   AUR24_RANAE             Reviewed;          16 AA.
AC   P82391;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Aurein-2.4 {ECO:0000303|PubMed:10951191};
DE   Contains:
DE     RecName: Full=Aurein-2.4.1 {ECO:0000303|PubMed:10951191};
OS   Ranoidea aurea (Green and golden bell frog) (Litoria aurea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Ranoidea.
OX   NCBI_TaxID=8371;
RN   [1]
RP   PROTEIN SEQUENCE, AMIDATION AT LEU-16, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin secretion;
RX   PubMed=10951191; DOI=10.1046/j.1432-1327.2000.01536.x;
RA   Rozek T., Wegener K.L., Bowie J.H., Olver I.N., Carver J.A., Wallace J.C.,
RA   Tyler M.J.;
RT   "The antibiotic and anticancer active aurein peptides from the australian
RT   bell frogs Litoria aurea and Litoria raniformis the solution structure of
RT   aurein 1.2.";
RL   Eur. J. Biochem. 267:5330-5341(2000).
RN   [2]
RP   FUNCTION.
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: Antimicrobial activity against B.cereus, L.lactis, L.innocua,
CC       M.luteus, S.aureus, S.epidermidis and S.uberis (PubMed:10951191).
CC       Probably acts by disturbing membrane functions with its amphipathic
CC       structure (PubMed:10951191). Shows anticancer activity
CC       (PubMed:10951191). Strongly inhibits the formation of NO by neuronal
CC       nitric oxide synthase (nNOS) at micromolar concentrations
CC       (PubMed:11784303). Acts by a non-competitive mechanism, probably by
CC       binding to calcium/calmodulin and as a consequence blocking calmodulin
CC       attachment to nNOS (By similarity). {ECO:0000250|UniProtKB:P81835,
CC       ECO:0000269|PubMed:10951191, ECO:0000269|PubMed:11784303}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10951191}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC       {ECO:0000305|PubMed:10951191}.
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Aurein subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P82391; -.
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:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR013157; Aurein_antimicrobial_peptide.
DR   Pfam; PF08256; Antimicrobial20; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Immunity; Innate immunity; Secreted.
FT   PEPTIDE         1..16
FT                   /note="Aurein-2.4"
FT                   /evidence="ECO:0000269|PubMed:10951191"
FT                   /id="PRO_0000010149"
FT   PEPTIDE         3..16
FT                   /note="Aurein-2.4.1"
FT                   /evidence="ECO:0000269|PubMed:10951191"
FT                   /id="PRO_0000010150"
FT   MOD_RES         16
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:10951191"
SQ   SEQUENCE   16 AA;  1630 MW;  1D87980438AAE2F9 CRC64;
     GLFDIVKKVV GTIAGL