AUR25_RANAE
ID AUR25_RANAE Reviewed; 72 AA.
AC P69019; P82392; Q5K0E4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Aurein-2.5 {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], MASS SPECTROMETRY, 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, AMIDATION AT LEU-65, FUNCTION, 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, AND SYNTHESIS OF 50-65.
RX PubMed=19056250; DOI=10.1016/j.colsurfb.2008.10.007;
RA Dennison S.R., Morton L.H., Shorrocks A.J., Harris F., Phoenix D.A.;
RT "A study on the interactions of Aurein 2.5 with bacterial membranes.";
RL Colloids Surf. B Biointerfaces 68:225-230(2009).
RN [4]
RP PTM.
RX PubMed=22519529; DOI=10.2174/092986612800494110;
RA Dennison S.R., Morton L.H., Phoenix D.A.;
RT "Effect of amidation on the antimicrobial peptide aurein 2.5 from
RT Australian southern bell frogs.";
RL Protein Pept. Lett. 19:586-591(2012).
RN [5]
RP FUNCTION, AND SYNTHESIS OF 50-65.
RX PubMed=23841919; DOI=10.1111/1574-6968.12212;
RA Dennison S.R., Harris F., Morton L.H., Phoenix D.A.;
RT "Antimicrobial activity of aurein 2.5 against yeasts.";
RL FEMS Microbiol. Lett. 346:140-145(2013).
RN [6]
RP FUNCTION.
RX PubMed=24728560; DOI=10.1007/s00249-014-0959-8;
RA Dennison S.R., Morton L.H., Harris F., Phoenix D.A.;
RT "The interaction of aurein 2.5 with fungal membranes.";
RL Eur. Biophys. J. 43:255-264(2014).
RN [7]
RP STRUCTURE BY NMR IN SDS MICELLES, 3D-STRUCTURE MODELING IN BACTERIAL
RP MIMETIC MEMBRANES, AND FUNCTION.
RX PubMed=31358802; DOI=10.1038/s41598-019-47327-w;
RA Manzo G., Ferguson P.M., Hind C.K., Clifford M., Gustilo V.B., Ali H.,
RA Bansal S.S., Bui T.T., Drake A.F., Atkinson R.A., Sutton J.M., Lorenz C.D.,
RA Phoenix D.A., Mason A.J.;
RT "Temporin L and aurein 2.5 have identical conformations but subtly distinct
RT membrane and antibacterial activities.";
RL Sci. Rep. 9:10934-10934(2019).
CC -!- FUNCTION: Amphipathic alpha-helical antimicrobial peptide with moderate
CC to potent activity against Gram-positive bacteria, Gram-negative
CC bacteria and fungi (PubMed:10951191, PubMed:19056250, PubMed:23841919,
CC PubMed:24728560, PubMed:31358802). Shows also a weak activity against
CC biofilm of both Gram-positive and Gram-negative bacteria
CC (PubMed:19056250). Probably acts by disturbing membrane functions with
CC its amphipathic structure (PubMed:10951191, PubMed:23841919). Kills
CC fungi via membranolytic action (PubMed:24728560). Enhanced sterol
CC levels in lipid composition membranes reduce interaction of this
CC peptide with membranes, having a protective effect against the lytic
CC ability of the peptide (PubMed:24728560). Shows anticancer activity
CC (PubMed:10951191). {ECO:0000269|PubMed:10951191,
CC ECO:0000269|PubMed:19056250, ECO:0000269|PubMed:23841919,
CC ECO:0000269|PubMed:24728560, ECO:0000269|PubMed:31358802}.
CC -!- SUBUNIT: May be monomeric or may oligomerize as homodimers or
CC homotrimers in Gram-positive and Gram-negative bacteria mimetic
CC membranes. {ECO:0000305|PubMed:31358802}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10951191,
CC ECO:0000269|PubMed:15721491}. Target cell membrane
CC {ECO:0000269|PubMed:31358802}. Note=Contact and insertion into membrane
CC begin at the N-terminus. {ECO:0000269|PubMed:31358802}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC {ECO:0000305|PubMed:10951191}.
CC -!- PTM: C-terminal amidation enhances antibacterial activity. This
CC increase may be due to stabilization of the alpha-helical structure at
CC the membrane interface. {ECO:0000269|PubMed:22519529}.
CC -!- MASS SPECTROMETRY: Mass=1650.00; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15721491};
CC -!- MISCELLANEOUS: The primary structure of the mature peptide is identical
CC to that of aurein-2.5 from Ranoidea raniformis (AC P69018).
CC {ECO:0000305}.
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=00018";
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DR EMBL; AJ850129; CAH61713.1; -; mRNA.
DR PDB; 6GS9; NMR; -; A=50-65.
DR PDBsum; 6GS9; -.
DR AlphaFoldDB; P69019; -.
DR SMR; P69019; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; 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 3D-structure; Amidation; Amphibian defense peptide; Antibiotic;
KW Antimicrobial; Cleavage on pair of basic residues;
KW Direct protein sequencing; Fungicide; Lipid-binding; Membrane; Secreted;
KW Signal; Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..49
FT /evidence="ECO:0000305|PubMed:10951191"
FT /id="PRO_0000450291"
FT PEPTIDE 50..65
FT /note="Aurein-2.5"
FT /evidence="ECO:0000269|PubMed:10951191"
FT /id="PRO_0000043722"
FT PROPEP 69..72
FT /evidence="ECO:0000305|PubMed:10951191"
FT /id="PRO_0000450292"
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"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:6GS9"
SQ SEQUENCE 72 AA; 8129 MW; 4E3B23B21A566A54 CRC64;
MAFLKKSLFL VLFLGLVSLS ICEKEKRQNE EDEDENEAAN HEEGSEEKRG LFDIVKKVVG
AFGSLGKRND LE
