ID   FALX1_LITFA             Reviewed;          67 AA.
AC   B5LUQ4;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Preprofallaxidin-1 {ECO:0000303|PubMed:18803332, ECO:0000312|EMBL:ACH53447.1};
DE   Contains:
DE     RecName: Full=Fallaxidin-4.1;
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:ACH53447.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 47-67, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Skin {ECO:0000312|EMBL:ACH53447.1}, 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-4.1 shows antibacterial activity against the Gram-
CC       positive bacteria L.lactis (MIC=12 uM), M.luteus (MIC=100 uM),
CC       S.epidermidis (MIC=100 uM) and S.uberis (MIC=50 uM). No anti-bacterial
CC       activity against the Gram-positive bacteria B.cereus, E.faecalis,
CC       L.innocua, S.aureus, or the Gram-negative bacteria E.cloacae and
CC       E.coli. Inhibits the formation of NO by neuronal nitric oxide synthase
CC       with an IC(50) of 13.3 uM. {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: Mass=2192; Method=Electrospray;
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; EU912529; ACH53447.1; -; mRNA.
DR   AlphaFoldDB; B5LUQ4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IDA:UniProtKB.
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   Direct protein sequencing; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255, ECO:0000312|EMBL:ACH53447.1"
FT   PROPEP          23..46
FT                   /evidence="ECO:0000269|PubMed:18803332"
FT                   /id="PRO_0000361700"
FT   PEPTIDE         47..67
FT                   /note="Fallaxidin-4.1"
FT                   /id="PRO_0000361701"
FT   REGION          24..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   67 AA;  7593 MW;  951B158DAE4EFD25 CRC64;
     MASLKKSLFL VLFLGMVSLS ICDKEKREGE NEEEEEEHEE ESEEKRGLLS FLPKVIGVIG
     HLIHPPS