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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
 
 
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