AUR31_RANAE
ID AUR31_RANAE Reviewed; 70 AA.
AC P69021; P82394; Q5K0E3;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Aurein-3.1 {ECO:0000303|PubMed:10951191};
DE Contains:
DE RecName: Full=Aurein-3.1.1 {ECO:0000303|PubMed:10951191};
DE Contains:
DE RecName: Full=Aurein-3.1.2 {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 50-66, AMIDATION AT ILE-66, 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).
CC -!- FUNCTION: Amphipathic alpha-helical antimicrobial peptide with weak to
CC potent activity against Gram-positive bacteria, and no activity against
CC Gram-negative bacteria (PubMed:10951191). Probably acts by disturbing
CC membrane functions with its amphipathic structure (PubMed:10951191).
CC Shows anticancer activity (PubMed:10951191).
CC {ECO:0000269|PubMed:10951191}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10951191,
CC ECO:0000269|PubMed:15721491}. Target cell membrane {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin dorsal glands.
CC {ECO:0000305|PubMed:10951191, ECO:0000305|PubMed:15721491}.
CC -!- MASS SPECTROMETRY: Mass=1739.57; 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=00020";
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DR EMBL; AJ850130; CAH61714.1; -; mRNA.
DR AlphaFoldDB; P69021; -.
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; IPR013157; Aurein_antimicrobial_peptide.
DR InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF08256; Antimicrobial20; 1.
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_0000450293"
FT PEPTIDE 50..66
FT /note="Aurein-3.1"
FT /evidence="ECO:0000269|PubMed:10951191"
FT /id="PRO_0000010154"
FT PEPTIDE 50..63
FT /note="Aurein-3.1.1"
FT /evidence="ECO:0000269|PubMed:10951191"
FT /id="PRO_0000010155"
FT PEPTIDE 52..66
FT /note="Aurein-3.1.2"
FT /evidence="ECO:0000269|PubMed:10951191"
FT /id="PRO_0000010156"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:10951191"
SQ SEQUENCE 70 AA; 7875 MW; AFED107FB1C5B3CC CRC64;
MAFLKKSLFL VLFLGLVSLS ICEKEKRQNE EDEDENEAAN HEEGSEEKRG LFDIVKKIAG
HIAGSIGKKR