AUR22_RANAE
ID AUR22_RANAE Reviewed; 72 AA.
AC P82389; Q5K0E6;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Aurein-2.2 {ECO:0000303|PubMed:10951191};
DE Contains:
DE RecName: Full=Aurein-2.2.1 {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, AND SUBCELLULAR LOCATION.
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:0000250|UniProtKB:P82390}.
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=00015";
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DR EMBL; AJ850127; CAH61711.1; -; mRNA.
DR AlphaFoldDB; P82389; -.
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_0000450287"
FT PEPTIDE 50..65
FT /note="Aurein-2.2"
FT /evidence="ECO:0000269|PubMed:10951191,
FT ECO:0000269|PubMed:15721491"
FT /id="PRO_0000010147"
FT PEPTIDE 52..65
FT /note="Aurein-2.2.1"
FT /evidence="ECO:0000269|PubMed:10951191"
FT /id="PRO_0000010148"
FT PROPEP 69..72
FT /evidence="ECO:0000305|PubMed:10951191"
FT /id="PRO_0000450288"
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; 8095 MW; 4E3B2B101A566A54 CRC64;
MAFLKKSLFL VLFLGLVSLS ICEKEKRQNE EDEDENEAAN HEEGSEEKRG LFDIVKKVVG
ALGSLGKRND LE
