ID   AUR23_RANAE             Reviewed;          72 AA.
AC   P82390; Q5K0E5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 2.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Aurein-2.3 {ECO:0000303|PubMed:10951191};
DE   Flags: Precursor;
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   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 50-65, MASS SPECTROMETRY,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Skin;
RX   PubMed=15721491; DOI=10.1016/j.regpep.2004.12.022;
RA   Chen T., Xue Y., Zhou M., Shaw C.;
RT   "The structural organization of aurein precursor cDNAs from the skin
RT   secretion of the Australian green and golden bell frog, Litoria aurea.";
RL   Regul. Pept. 128:75-83(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 50-65, FUNCTION, AMIDATION AT LEU-65, AND SUBCELLULAR
RP   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   [3]
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).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND PTM.
RX   PubMed=17259271; DOI=10.1529/biophysj.106.097238;
RA   Pan Y.L., Cheng J.T., Hale J., Pan J., Hancock R.E., Straus S.K.;
RT   "Characterization of the structure and membrane interaction of the
RT   antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell
RT   frogs.";
RL   Biophys. J. 92:2854-2864(2007).
CC   -!- FUNCTION: Amphipathic alpha-helical antimicrobial peptide with weak to
CC       moderate activity against Gram-positive bacteria, and no activity
CC       against Gram-negative bacteria (PubMed:10951191, PubMed:17259271).
CC       Probably acts by disturbing membrane functions with its amphipathic
CC       structure (PubMed:10951191). Strongly inhibits the formation of NO by
CC       neuronal 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       ECO:0000269|PubMed:17259271}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10951191,
CC       ECO:0000269|PubMed:15721491}. Target cell membrane
CC       {ECO:0000269|PubMed:17259271}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC       {ECO:0000305|PubMed:10951191, ECO:0000305|PubMed:15721491}.
CC   -!- PTM: Amidation is essential for antibacterial activity against Gram-
CC       positive bacteria. {ECO:0000269|PubMed:17259271}.
CC   -!- MASS SPECTROMETRY: Mass=1615.76; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15721491};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Aurein subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC       URL="https://wangapd3.com/database/query_output.php?ID=00016";
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DR   EMBL; AJ850128; CAH61712.1; -; mRNA.
DR   AlphaFoldDB; P82390; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR004275; Frog_antimicrobial_propeptide.
DR   InterPro; IPR016322; FSAP.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
DR   PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing; Immunity;
KW   Innate immunity; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..49
FT                   /evidence="ECO:0000305|PubMed:10951191"
FT                   /id="PRO_0000450289"
FT   PEPTIDE         50..65
FT                   /note="Aurein-2.3"
FT                   /evidence="ECO:0000269|PubMed:10951191,
FT                   ECO:0000269|PubMed:15721491"
FT                   /id="PRO_0000043720"
FT   PROPEP          69..72
FT                   /evidence="ECO:0000305|PubMed:10951191"
FT                   /id="PRO_0000450290"
FT   REGION          27..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         65
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:10951191"
SQ   SEQUENCE   72 AA;  8009 MW;  4E2ECDE3907C6A54 CRC64;
     MAFLKKSLFL VLFLGLVSLS ICEKEKRQNG EDEDENEAAN HEEGSEEKRG LFDIVKKVVG
     AIGSLGKRND VE