ID   FALX8_LITFA             Reviewed;         109 AA.
AC   B5LUR0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Preprofallaxidin-8 {ECO:0000303|PubMed:18803332, ECO:0000312|EMBL:ACH53453.1};
DE   Contains:
DE     RecName: Full=Fallaxidin-2.1;
DE   Contains:
DE     RecName: Full=Fallaxidin-3.2;
DE   Contains:
DE     RecName: Full=Fallaxidin-5.2;
DE   Flags: Precursor;
OS   Litoria fallax (Eastern dwarf tree frog) (Hylomantis fallax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Hyloidea; Hylidae; Pelodryadinae; Litoria.
OX   NCBI_TaxID=115422;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACH53453.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-62; 71-75 AND 84-88,
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY, AND
RP   AMIDATION AT LEU-62; MET-75 AND MET-88.
RC   TISSUE=Skin {ECO:0000312|EMBL:ACH53453.1}, and
RC   Skin secretion {ECO:0000269|PubMed:18803332};
RX   PubMed=18803332; DOI=10.1002/rcm.3723;
RA   Jackway R.J., Bowie J.H., Bilusich D., Musgrave I.F., Surinya-Johnson K.H.,
RA   Tyler M.J., Eichinger P.C.H.;
RT   "The fallaxidin peptides from the skin secretion of the eastern dwarf tree
RT   frog Litoria fallax. Sequence determination by positive and negative ion
RT   electrospray mass spectrometry: antimicrobial activity and cDNA cloning of
RT   the fallaxidins.";
RL   Rapid Commun. Mass Spectrom. 22:3207-3216(2008).
CC   -!- FUNCTION: Fallaxidin-2.1 shows no antibacterial activity against Gram-
CC       positive or Gram-negative bacteria. Does not inhibit the formation of
CC       NO by neuronal nitric oxide synthase. Has no effect on splenocyte
CC       proliferation or smooth muscle contraction.
CC       {ECO:0000269|PubMed:18803332}.
CC   -!- FUNCTION: Fallaxidin-3.2 shows antibacterial activity against the Gram-
CC       positive bacteria E.faecalis (MIC=100 uM) and L.lactis (MIC=500 uM). No
CC       antibacterial activity against the Gram-positive bacteria B.cereus,
CC       L.innocua, M.luteus, S.epidermidis, S.uberis and S.aureus, or the Gram-
CC       negative bacteria E.cloacae and E.coli. {ECO:0000269|PubMed:18803332}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18803332}.
CC   -!- TISSUE SPECIFICITY: Expressed by the skin glands.
CC       {ECO:0000269|PubMed:18803332}.
CC   -!- MASS SPECTROMETRY: [Fallaxidin-3.2]: Mass=1678; Method=Electrospray;
CC       Note=The measured mass is that of Fallaxidin-3.2.;
CC       Evidence={ECO:0000269|PubMed:18803332};
CC   -!- MASS SPECTROMETRY: [Fallaxidin-2.1]: Mass=726; Method=Electrospray;
CC       Note=The measured mass is that of Fallaxidin-2.1.;
CC       Evidence={ECO:0000269|PubMed:18803332};
CC   -!- SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.
CC       Brevinin subfamily. {ECO:0000255}.
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DR   EMBL; EU912535; ACH53453.1; -; mRNA.
DR   AlphaFoldDB; B5LUR0; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   InterPro; IPR004275; Frog_antimicrobial_propeptide.
DR   Pfam; PF03032; FSAP_sig_propep; 1.
PE   1: Evidence at protein level;
KW   Amidation; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW   Direct protein sequencing; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255, ECO:0000312|EMBL:ACH53453.1"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000269|PubMed:18803332"
FT                   /id="PRO_0000361742"
FT   PEPTIDE         47..62
FT                   /note="Fallaxidin-3.2"
FT                   /id="PRO_0000361743"
FT   PROPEP          66..70
FT                   /evidence="ECO:0000269|PubMed:18803332"
FT                   /id="PRO_0000361744"
FT   PEPTIDE         71..75
FT                   /note="Fallaxidin-2.1"
FT                   /id="PRO_0000361745"
FT   PROPEP          79..83
FT                   /evidence="ECO:0000269|PubMed:18803332"
FT                   /id="PRO_0000361746"
FT   PEPTIDE         84..88
FT                   /note="Fallaxidin-2.1"
FT                   /id="PRO_0000361747"
FT   PROPEP          92..96
FT                   /evidence="ECO:0000269|PubMed:18803332"
FT                   /id="PRO_0000361748"
FT   PEPTIDE         97..108
FT                   /note="Fallaxidin-5.2"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000361749"
FT   PROPEP          108
FT                   /evidence="ECO:0000250|UniProtKB:P82881"
FT                   /id="PRO_0000361750"
FT   REGION          27..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         62
FT                   /note="Leucine amide"
FT                   /evidence="ECO:0000269|PubMed:18803332"
FT   MOD_RES         75
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000269|PubMed:18803332"
FT   MOD_RES         88
FT                   /note="Methionine amide"
FT                   /evidence="ECO:0000269|PubMed:18803332"
SQ   SEQUENCE   109 AA;  12865 MW;  C3C9D06CE90EB1EC CRC64;
     MASLKKSLFL VLFLGLLSLS ICEEQKRENE EDAEDENHEE ESEEKRGLLD FAKHVIGIAS
     KLGKRSEEKR FWPFMGKRSE EKRFWPFMGK RSEEKRFFRV LAKLGKLAK