AUR52_RANAE
ID AUR52_RANAE Reviewed; 71 AA.
AC P69031; P82402; Q5K0E2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 25-MAY-2022, entry version 27.
DE RecName: Full=Aurein-5.2 {ECO:0000303|PubMed:10951191};
DE AltName: Full=Aurein-5.3 {ECO:0000303|PubMed:15721491};
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, FUNCTION, AND SUBCELLULAR 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 moderate
CC activity against Gram-positive bacteria (MIC=100 ug/mL against L.lactis
CC and MIC=50 ug/mL against S.uberis) (PubMed:10951191). Has no activity
CC against Gram-negative bacteria (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:0000269|PubMed:10951191, ECO:0000305|PubMed:15721491}.
CC -!- MASS SPECTROMETRY: Mass=2452.99; 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 -!- CAUTION: Aurein 5.2 may be a deamidated form of aurein 5.3.
CC {ECO:0000305|PubMed:15721491}.
CC -!- WEB RESOURCE: Name=The antimicrobial peptide database;
CC URL="https://wangapd3.com/database/query_output.php?ID=02005";
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DR EMBL; AJ850131; CAH61715.1; -; mRNA.
DR AlphaFoldDB; P69031; -.
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 InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR InterPro; IPR032021; Frog_Litoria.
DR InterPro; IPR016322; FSAP.
DR Pfam; PF16049; Antimicrobial24; 1.
DR Pfam; PF03032; FSAP_sig_propep; 1.
DR PIRSF; PIRSF001822; Dermaseptin_precursor; 1.
PE 1: Evidence at protein level;
KW Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..46
FT /evidence="ECO:0000305|PubMed:15721491"
FT /id="PRO_0000450294"
FT PEPTIDE 47..71
FT /note="Aurein-5.2"
FT /evidence="ECO:0000269|PubMed:10951191"
FT /id="PRO_0000043735"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 62
FT /note="D -> N (in Ref. 1; CAH61715)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 7825 MW; C0A1971A3B83CBEC CRC64;
MAFLKKSLFL VLFLGLVSLS ICEQEKREEE NQEEDEENEA ASEEKRGLMS SIGKALGGLI
VDVLKPKTPA S